|
Name |
Accession |
Description |
Interval |
E-value |
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
308-567 |
1.98e-118 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 350.89 E-value: 1.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAideGiVKREDVFVTTKVMPGN--YDR 385
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAAS---G-VPREELFVTTKVWNDNhgYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 386 AYQSIDESLARLGFDYIDLMLVHQSGSGD-EEVYKALCQGVADGKIRSIGISNYYTADeVERVTDGADIKPAVIQNENHL 464
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPGPGPyVETWRALEELYEEGLIRAIGVSNFDPEH-LEELLAETGVKPAVNQVELHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 465 YYQNTELQEYVKQYGTVIESWYPFGgRGhtsESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENID 544
Cdd:COG0656 156 YLQQRELLAFCREHGIVVEAYSPLG-RG---KLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLD 231
|
250 260
....*....|....*....|...
gi 1167055252 545 IFDFELSESEMQSMTSLNTGQRY 567
Cdd:COG0656 232 AFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
304-562 |
4.56e-108 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 324.14 E-value: 4.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 304 VLLNSGYEMPIIGLGTWT-QDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIdegiVKREDVFVTTKVMPGN 382
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQiPDPEECERAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSG----IPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 --YDRAYQSIDESLARLGFDYIDLMLVHQSGSGDEEVYKALCQGVADGKIRSIGISNYYtADEVERVTDGADIKPAVIQN 460
Cdd:cd19133 77 agYEKAKKAFERSLKRLGLDYLDLYLIHQPFGDVYGAWRAMEELYKEGKIRAIGVSNFY-PDRLVDLILHNEVKPAVNQI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 461 ENHLYYQNTELQEYVKQYGTVIESWYPFG-GRghtSESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHI 539
Cdd:cd19133 156 ETHPFNQQIEAVEFLKKYGVQIEAWGPFAeGR---NNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERI 232
|
250 260
....*....|....*....|...
gi 1167055252 540 AENIDIFDFELSESEMQSMTSLN 562
Cdd:cd19133 233 AENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
312-558 |
5.74e-107 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 320.97 E-value: 5.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 312 MPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGN--YDRAYQS 389
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVG----EAIRESGVPREELFITTKLWPTDhgYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 390 IDESLARLGFDYIDLMLVH--------QSGSGDEEVYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIKPAVIQNE 461
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHwpvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNF-NVEHLEELLAAARIKPAVNQIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 462 NHLYYQNTELQEYVKQYGTVIESWYPFGGrgHTSESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAE 541
Cdd:cd19071 156 LHPYLQQKELVEFCKEHGIVVQAYSPLGR--GRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKE 233
|
250
....*....|....*..
gi 1167055252 542 NIDIFDFELSESEMQSM 558
Cdd:cd19071 234 NLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
302-567 |
5.76e-89 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 276.47 E-value: 5.76e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 302 KTVLLNSGYEMPIIGLGTWT-QDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMp 380
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKlKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLW- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 GNYDRAYQ---SIDESLARLGFDYIDLMLVH---------QSGSGDE---------EVYKALCQGVADGKIRSIGISNYy 439
Cdd:cd19116 80 NSYHEREQvepALRESLKRLGLDYVDLYLIHwpvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNF- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 440 TADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFG---GRGHTSES--FNNEVIVELAEKYNKTS 514
Cdd:cd19116 159 NSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGrlvPRGQTNPPprLDDPTLVAIAKKYGKTT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1167055252 515 AQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19116 239 AQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRV 291
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
303-562 |
1.23e-83 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 261.15 E-value: 1.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 303 TVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGN 382
Cdd:cd19131 1 TITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVG----KAIRASGVPREELFITTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 --YDRAYQSIDESLARLGFDYIDLMLVHQSGSGDE---EVYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIKPAV 457
Cdd:cd19131 77 qgYDSTLRAFDESLRKLGLDYVDLYLIHWPVPAQDkyvETWKALIELKKEGRVKSIGVSNF-TIEHLQRLIDETGVVPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 458 IQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGhtseSFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPE 537
Cdd:cd19131 156 NQIELHPRFQQRELRAFHAKHGIQTESWSPLGQGG----LLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPS 231
|
250 260
....*....|....*....|....*
gi 1167055252 538 HIAENIDIFDFELSESEMQSMTSLN 562
Cdd:cd19131 232 RIAENFDVFDFELDADDMQAIAGLD 256
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
312-561 |
3.01e-82 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 257.95 E-value: 3.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 312 MPIIGLGTW-TQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGN--YDRAYQ 388
Cdd:cd19136 1 MPILGLGTFrLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDqgYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 389 SIDESLARLGFDYIDLMLVHQSG-----SGDE-------EVYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIKPA 456
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGvqglkPSDPrnaelrrESWRALEDLYKEGKLRAIGVSNY-TVRHLEELLKYCEVPPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 457 VIQNENHLYYQNTELQEYVKQYGTVIESWYPFG-GRGHTSEsfnNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSN 535
Cdd:cd19136 160 VNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGsGDLRLLE---DPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTN 236
|
250 260
....*....|....*....|....*.
gi 1167055252 536 PEHIAENIDIFDFELSESEMQSMTSL 561
Cdd:cd19136 237 PERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
306-563 |
3.86e-82 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 257.20 E-value: 3.86e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIdegiVKREDVFVTTKVmPGN--- 382
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSG----VPREELFVTTKL-PGRhhg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 YDRAYQSIDESLARLGFDYIDLMLVHQSGSGDE---EVYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIKPAVIQ 459
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDlyvEAWQALIEAREEGLVRSIGVSNF-LPEHLDRLIDETGVTPAVNQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 460 NENHLYYQNTELQEYVKQYGTVIESWYPFGgRGhtSESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHI 539
Cdd:cd19132 155 IELHPYFPQAEQRAYHREHGIVTQSWSPLG-RG--SGLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQ 231
|
250 260
....*....|....*....|....
gi 1167055252 540 AENIDIFDFELSESEMQSMTSLNT 563
Cdd:cd19132 232 RENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
306-562 |
5.72e-82 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 257.34 E-value: 5.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAideGiVKREDVFVTTKVMPGNY-- 383
Cdd:cd19127 3 LNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS---G-VDRSDIFVTTKLWISDYgy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 384 DRAYQSIDESLARLGFDYIDLMLVHQSGSGDEE----VYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIKPAVIQ 459
Cdd:cd19127 79 DKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDrtiqAYKALEKLLAEGRVRAIGVSNF-TPEHLERLIDATTVVPAVNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 460 NENHLYYQNTELQEYVKQYGTVIESWYPFGG-----RGHTSESFN---NEVIVELAEKYNKTSAQIILRWQVQAGYIAIP 531
Cdd:cd19127 158 VELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvmrygASGPTGPGDvlqDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIP 237
|
250 260 270
....*....|....*....|....*....|.
gi 1167055252 532 GSSNPEHIAENIDIFDFELSESEMQSMTSLN 562
Cdd:cd19127 238 KSVHPERIAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
303-567 |
2.04e-81 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 255.78 E-value: 2.04e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 303 TVLLNSGYEMPIIGLGTW-TQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPG 381
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFkVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVG----KGIKESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 N--YDRAYQSIDESLARLGFDYIDLMLVHQSGSG-DEEVYKALCQGVADGKIRSIGISNYYTADEVERVTDgADIKPAVI 458
Cdd:cd19157 77 DqgYDSTLKAFEASLERLGLDYLDLYLIHWPVKGkYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAD-AEIVPMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 459 QNENHLYYQNTELQEYVKQYGTVIESWYPFggrgHTSESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEH 538
Cdd:cd19157 156 QVEFHPRLTQKELRDYCKKQGIQLEAWSPL----MQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHR 231
|
250 260
....*....|....*....|....*....
gi 1167055252 539 IAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19157 232 IIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
304-562 |
5.36e-80 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 251.97 E-value: 5.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 304 VLLNSGYEMPIIGLGTW-TQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRkaidEGIVKREDVFVTTKVMPGN 382
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFqTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIR----ESGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 --YDRAYQSIDESLARLGFDYIDLMLVHQSGSGD-EEVYKALCQGVADGKIRSIGISNYYTaDEVERVTDGADIKPAVIQ 459
Cdd:cd19126 77 qrARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKfIDTWKALEKLYASGKVKAIGVSNFQE-HHLEELLAHADVVPAVNQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 460 NENHLYYQNTELQEYVKQYGTVIESWYPFGgRGHTSEsfnNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHI 539
Cdd:cd19126 156 VEFHPYLTQKELRGYCKSKGIVVEAWSPLG-QGGLLS---NPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRI 231
|
250 260
....*....|....*....|...
gi 1167055252 540 AENIDIFDFELSESEMQSMTSLN 562
Cdd:cd19126 232 KENADIFDFELSEDDMTAIDALN 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
301-566 |
2.80e-75 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 241.16 E-value: 2.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 301 SKTVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMP 380
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 GNYDRA--YQSIDESLARLGFDYIDLMLVH-------QSGSGD--------------EEVYKALCQGVADGKIRSIGISN 437
Cdd:cd19154 81 HEHAPEdvEEALRESLKKLQLEYVDLYLIHapaafkdDEGESGtmengmsihdavdvEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 438 yYTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHTSES-----------FNNEVIVEL 506
Cdd:cd19154 161 -FNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTkstgvspapnlLQDPIVKAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 507 AEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQR 566
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
309-561 |
4.04e-75 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 239.08 E-value: 4.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGNY--DRA 386
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVG----EAIAASGVPRDELFLTTKVWPDNYspDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 387 YQSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNyYTADEVERVTDGADIKPAVIQNENHL 464
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHWPNKDVplAETLGALNEAQEAGLARHIGVSN-FTVALLREAVELSEAPLFTNQVEYHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 465 YYQNTELQEYVKQYGTVIESWYPFgGRGhtsESFNNEVIVELAEKYNKTSAQIILRWQV-QAGYIAIPGSSNPEHIAENI 543
Cdd:cd19140 160 YLDQRKLLDAAREHGIALTAYSPL-ARG---EVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENL 235
|
250
....*....|....*...
gi 1167055252 544 DIFDFELSESEMQSMTSL 561
Cdd:cd19140 236 DIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
306-561 |
7.03e-75 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 239.55 E-value: 7.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGNYD- 384
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 385 -RAYQSIDESLARLGFDYIDLMLVH-----QSGSGD-----------EEVYKALCQGVADGKIRSIGISNyYTADEVERV 447
Cdd:cd19125 85 eDVPPALEKTLKDLQLDYLDLYLIHwpvrlKKGAHMpepeevlppdiPSTWKAMEKLVDSGKVRAIGVSN-FSVKKLEDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 448 TDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHTSESFN---NEVIVELAEKYNKTSAQIILRWQVQ 524
Cdd:cd19125 164 LAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKNvlkDPIVTKVAEKLGKTPAQVALRWGLQ 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 1167055252 525 AGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSL 561
Cdd:cd19125 244 RGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
312-558 |
8.70e-75 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 237.94 E-value: 8.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 312 MPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGN--YDRAYQS 389
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVG----EAIAESGVPREDLFITTKVWRDHlrPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 390 IDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIKPAVIQNENHLYYQ 467
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPNPTVplEETLGALKELKEAGKVKSIGVSNF-TIELLEEALDISPLPIAVNQVEFHPFLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 468 NTELQEYVKQYGTVIESWYPFGgRGhtsESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFD 547
Cdd:cd19073 156 QAELLEYCRENDIVITAYSPLA-RG---EVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFD 231
|
250
....*....|.
gi 1167055252 548 FELSESEMQSM 558
Cdd:cd19073 232 WELTSEDVAKI 242
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
303-569 |
4.80e-74 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 238.50 E-value: 4.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 303 TVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVM--- 379
Cdd:cd19113 2 DIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWnnf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 380 --PGNYDRAyqsIDESLARLGFDYIDLMLVH------------------QSGSGDE---------EVYKALCQGVADGKI 430
Cdd:cd19113 82 hdPKNVETA---LNKTLSDLKLDYVDLFLIHfpiafkfvpieekyppgfYCGDGDNfvyedvpilDTWKALEKLVDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 431 RSIGISNyYTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFG---------GRG-HTSESFNN 500
Cdd:cd19113 159 KSIGVSN-FPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvelnqGRAlNTPTLFEH 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167055252 501 EVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRYEN 569
Cdd:cd19113 238 DTIKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFND 306
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
303-567 |
8.16e-73 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 233.59 E-value: 8.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 303 TVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAideGIvKREDVFVTTKVmpGN 382
Cdd:cd19134 2 TVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAAS---GI-PRGELFVTTKL--AT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 YDRAYQSIDE----SLARLGFDYIDLMLVHQSGsGDEEVY----KALCQGVADGKIRSIGISNYyTADEVERVTDGADIK 454
Cdd:cd19134 76 PDQGFTASQAacraSLERLGLDYVDLYLIHWPA-GREGKYvdswGGLMKLREEGLARSIGVSNF-TAEHLENLIDLTFFT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 455 PAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFG-GRghtseSFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGS 533
Cdd:cd19134 154 PAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGvGR-----LLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRS 228
|
250 260 270
....*....|....*....|....*....|....
gi 1167055252 534 SNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19134 229 SNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
304-567 |
9.93e-72 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 230.87 E-value: 9.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 304 VLLNSGYEMPIIGLGTW-TQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRkaidEGIVKREDVFVTTKVMPGN 382
Cdd:cd19156 1 VKLANGVEMPRLGLGVWrVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR----ESGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 --YDRAYQSIDESLARLGFDYIDLMLVHQSGSGD-EEVYKALCQGVADGKIRSIGISNYYtADEVERVTDGADIKPAVIQ 459
Cdd:cd19156 77 qgYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKfKDTWKAFEKLYKEKKVRAIGVSNFH-EHHLEELLKSCKVAPMVNQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 460 NENHLYYQNTELQEYVKQYGTVIESWYPFGgRGHTSEsfnNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHI 539
Cdd:cd19156 156 IELHPLLTQEPLRKFCKEKNIAVEAWSPLG-QGKLLS---NPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERI 231
|
250 260
....*....|....*....|....*...
gi 1167055252 540 AENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19156 232 QENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
306-567 |
1.36e-71 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 231.89 E-value: 1.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEG-IVKREDVFVTTKVMPGNY- 383
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGkAVPREDLFVTSKLWNTKHh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 384 -DRAYQSIDESLARLGFDYIDLMLVHQS---GSGDE------------------EVYKALCQGVADGKIRSIGISNYyTA 441
Cdd:cd19106 81 pEDVEPALRKTLKDLQLDYLDLYLIHWPyafERGDNpfpknpdgtirydsthykETWKAMEKLVDKGLVKAIGLSNF-NS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 442 DEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGR----GHTSES--FNNEVIVELAEKYNKTSA 515
Cdd:cd19106 160 RQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPdrpwAKPDEPvlLEEPKVKALAKKYNKSPA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1167055252 516 QIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19106 240 QILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRY 291
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
302-569 |
1.96e-71 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 231.61 E-value: 1.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 302 KTVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPG 381
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 NYDRAYQSIDESLARLGFDYIDLMLVH-------------QSGSGDEEV------------YKALCQGVADGKIRSIGIS 436
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttGSALGEDGVldidvtislettWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 437 NY---YTADeverVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHTSESFN------NEVIVELA 507
Cdd:cd19112 161 NYdifLTRD----CLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEWFGsvspldDPVLKDLA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167055252 508 EKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRYEN 569
Cdd:cd19112 237 KKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQ 298
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
302-561 |
2.60e-71 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 229.52 E-value: 2.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 302 KTVLLNSGYEMPIIGLGTWtQDDETTEESVYSALKD-GYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMP 380
Cdd:cd19135 3 PTVRLSNGVEMPILGLGTS-HSGGYSHEAVVYALKEcGYRHIDTAKRYGCEELLG----KAIKESGVPREDLFLTTKLWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 GNY--DRAYQSIDESLARLGFDYIDLMLVHQSGSGD---------EEVYKALCQGVADGKIRSIGISNYYTADeVERVTD 449
Cdd:cd19135 78 SDYgyESTKQAFEASLKRLGVDYLDLYLLHWPDCPSsgknvketrAETWRALEELYDEGLCRAIGVSNFLIEH-LEQLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 450 GADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGgRGhtsESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIA 529
Cdd:cd19135 157 DCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA-KG---KALEEPTVTELAKKYQKTPAQILIRWSIQNGVVT 232
|
250 260 270
....*....|....*....|....*....|..
gi 1167055252 530 IPGSSNPEHIAENIDIFDFELSESEMQSMTSL 561
Cdd:cd19135 233 IPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
301-569 |
2.34e-70 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 228.84 E-value: 2.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 301 SKTVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMP 380
Cdd:cd19115 2 SPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 GNYD--RAYQSIDESLARLGFDYIDLMLVH--------------------------QSGSGDEEVYKALCQGVADGKIRS 432
Cdd:cd19115 82 TFHDgeRVEPICRKQLADWGIDYFDLFLIHfpialkyvdpavryppgwfydgkkveFSNAPIQETWTAMEKLVDKGLARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 433 IGISNYyTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRG----------HTSESFNNEV 502
Cdd:cd19115 162 IGVSNF-SAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGPQSfleldlpgakDTPPLFEHDV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167055252 503 IVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRYEN 569
Cdd:cd19115 241 IKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNN 307
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
301-545 |
9.80e-65 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 213.51 E-value: 9.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 301 SKTVLLNSGYEMPIIGLGTWTQDD--ETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKV 378
Cdd:cd19119 1 EISFKLNTGASIPALGLGTASPHEdrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 MPGNYDRAYQSIDESLARLGFDYIDLMLVH--------------------------QSGSGDE-EVYKALCQGVADGKIR 431
Cdd:cd19119 81 WPTFYDEVERSLDESLKALGLDYVDLLLVHwpvcfekdsddsgkpftpvnddgktrYAASGDHiTTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 432 SIGISNyYTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHTseSFNNEVIVELAEKYN 511
Cdd:cd19119 161 AIGVSN-YSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--NLKNPLVKKIAEKYN 237
|
250 260 270
....*....|....*....|....*....|....
gi 1167055252 512 KTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDI 545
Cdd:cd19119 238 VSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI 271
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
302-566 |
1.12e-64 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 213.93 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 302 KTVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPG 381
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 NyDRAYQ---SIDESLARLGFDYIDLMLVH----------QSGSGDEE-------------VYKALCQGVADGKIRSIGI 435
Cdd:cd19155 82 G-NRREKvekFLLKSLEKLQLDYVDLYLIHfpvgslskedDSGKLDPTgehkqdyttdlldIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 436 SNyYTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFG---------GRGHTSES----FNNEV 502
Cdd:cd19155 161 SN-FNREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGspgaahfspGTGSPSGSspdlLQDPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167055252 503 IVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQR 566
Cdd:cd19155 240 VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
306-566 |
1.38e-63 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 209.93 E-value: 1.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGNYDR 385
Cdd:PRK11565 9 LQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVG----KALKEASVAREELFITTKLWNDDHKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 386 AYQSIDESLARLGFDYIDLMLVHQSGSGDE---EVYKALCQGVADGKIRSIGISNYYTAdEVERVTDGADIKPAVIQNEN 462
Cdd:PRK11565 85 PREALEESLKKLQLDYVDLYLMHWPVPAIDhyvEAWKGMIELQKEGLIKSIGVCNFQIH-HLQRLIDETGVTPVINQIEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 463 HLYYQNTELQEYVKQYGTVIESWYPF--GGRGhtseSFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIA 540
Cdd:PRK11565 164 HPLMQQRQLHAWNATHKIQTESWSPLaqGGKG----VFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIA 239
|
250 260
....*....|....*....|....*.
gi 1167055252 541 ENIDIFDFELSESEMQSMTSLNTGQR 566
Cdd:PRK11565 240 ENFDVFDFRLDKDELGEIAKLDQGKR 265
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
306-562 |
4.95e-63 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 207.84 E-value: 4.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGNY-- 383
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVG----AAIAASGIPRDELFVTTKLWNDRHdg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 384 DRAYQSIDESLARLGFDYIDLMLVH--QSGSGDE-EVYKALCQGVADGKIRSIGISNYYTAdEVERVTDGADIKPAVIQN 460
Cdd:cd19130 80 DEPAAAFAESLAKLGLDQVDLYLVHwpTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFLPP-HLERIVAATGVVPAVNQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 461 ENHLYYQNTELQEYVKQYGTVIESWYPFGgrghTSESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIA 540
Cdd:cd19130 159 ELHPAYQQRTIRDWAQAHDVKIEAWSPLG----QGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERME 234
|
250 260
....*....|....*....|..
gi 1167055252 541 ENIDIFDFELSESEMQSMTSLN 562
Cdd:cd19130 235 DNLDVFDFDLTDTEIAAIDALD 256
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
309-567 |
1.32e-62 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 207.74 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVmPGNYDRA-- 386
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKL-PPVYLEFkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 387 -YQSIDESLARLGFDYIDLMLVH---------------QSGSGDEEVYKALCQGVADGKIRSIGISNyYTADEVERVTDG 450
Cdd:cd19111 80 tEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSN-FNPRQINKILAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 451 ADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHTSES--------FNNEVIVELAEKYNKTSAQIILRWQ 522
Cdd:cd19111 159 AKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSlwpdqpdlLEDPTVLAIAKELDKTPAQVLLRFV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1167055252 523 VQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19111 239 LQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
309-559 |
2.60e-62 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 206.31 E-value: 2.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTWTQ--------DDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMP 380
Cdd:cd19120 1 GSKIPAIAFGTGTAwyksgdddIQRDLVDSVKLALKAGFRHIDTAEMYGNEKEVG----EALKESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 GNYDrAYQSIDESLARLGFDYIDLMLVH------QSGSGDEEVYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIK 454
Cdd:cd19120 77 GIKD-PREALRKSLAKLGVDYVDLYLIHspffakEGGPTLAEAWAELEALKDAGLVRSIGVSNF-RIEDLEELLDTAKIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 455 PAVIQNENH--LYYQNTELQEYVKQYGTVIESWYPFGGRGHTSESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPG 532
Cdd:cd19120 155 PAVNQIEFHpyLYPQQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTT 234
|
250 260
....*....|....*....|....*..
gi 1167055252 533 SSNPEHIAENIDIFDFELSESEMQSMT 559
Cdd:cd19120 235 SSKEERMKEYLEAFDFELTEEEVEEID 261
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
306-561 |
1.94e-59 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 198.91 E-value: 1.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDeGIVKREDVFVTTKVMPGNYDR 385
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIA-GGVKREDLFVTTKLWSTYHRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 386 AYQSIDESLARLGFDYIDLMLVH----QSGSGDEEVYKALCQGVAD--------------------GKIRSIGISNYYTA 441
Cdd:cd19121 85 VELCLDRSLKSLGLDYVDLYLVHwpvlLNPNGNHDLFPTLPDGSRDldwdwnhvdtwkqmekvlktGKTKAIGVSNYSIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 442 dEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGhtSESFNNEVIVELAEKYNKTSAQIILRW 521
Cdd:cd19121 165 -YLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTG--SPLISDEPVVEIAKKHNVGPGTVLISY 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1167055252 522 QVQAGYIAIPGSSNPEHIAENIDIFDFElsESEMQSMTSL 561
Cdd:cd19121 242 QVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
312-561 |
1.59e-58 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 195.65 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 312 MPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGNY--DRAYQS 389
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLskDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 390 IDESLARLGFDYIDLMLVHQSGSGD----EEVYKALCQGVADGKIRSIGISNYYTA--DEVERVTDGADIkpAVIQNENH 463
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSPNDevpvEEYIGALAEAKEQGLTRHIGVSNFTIAllDEAIAVVGAGAI--ATNQIELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 464 LYYQNTELQEYVKQYGTVIESWYPFGgRGHTSEsfnNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENI 543
Cdd:cd19139 155 PYLQNRKLVAHCKQHGIHVTSYMTLA-YGKVLD---DPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNL 230
|
250
....*....|....*...
gi 1167055252 544 DIFDFELSESEMQSMTSL 561
Cdd:cd19139 231 LALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
306-561 |
4.12e-58 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 195.71 E-value: 4.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDE-GIVKREDVFVTTKVMPGNYD 384
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 385 RAY--QSIDESLARLGFDYIDLMLVH----------------QSGSGDE----------EVYKALCQGVADGKIRSIGIS 436
Cdd:cd19118 81 PEYvePALDDTLKELGLDYLDLYLIHwpvafkptgdlnpltaVPTNGGEvdldlsvslvDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 437 NYyTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGG-RGHTSESFNNEVIVELAEKYNKTSA 515
Cdd:cd19118 161 NF-SIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNnLAGLPLLVQHPEVKAIAAKLGKTPA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1167055252 516 QIILRWQVQAGYIAIPGSSNPEHIAENIDifDFELSESEMQSMTSL 561
Cdd:cd19118 240 QVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
309-567 |
1.29e-57 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 195.08 E-value: 1.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGNY--DRA 386
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHgkDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 387 YQSIDESLARLGFDYIDLMLVH---------------------------QSGSGDEEVYKALCQGVADGKIRSIGISNYY 439
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHfpipaayvdpaenypflwkdkelkkfpLEQSPMQECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 440 TADEVERVTdGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRG---------HTSESFNNEVIVELAEKY 510
Cdd:cd19114 161 VQLILDLLT-YAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVytkvtkhlkHFTNLLEHPVVKKLADKH 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167055252 511 NKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19114 240 KRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARF 296
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
308-561 |
4.78e-57 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 192.87 E-value: 4.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGT--WTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVK-REDVFVTTKVMPG--N 382
Cdd:cd19124 1 SGQTMPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSdaH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 YDRAYQSIDESLARLGFDYIDLMLVH-----QSGSGD-------------EEVYKALCQGVADGKIRSIGISNYyTADEV 444
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHwpvslKPGKFSfpieeedflpfdiKGVWEAMEECQRLGLTKAIGVSNF-SCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 445 ERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGH---TSESFNNEVIVELAEKYNKTSAQIILRW 521
Cdd:cd19124 160 QELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTkwgSNAVMESDVLKEIAAAKGKTVAQVSLRW 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1167055252 522 QVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSL 561
Cdd:cd19124 240 VYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
301-567 |
7.02e-57 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 193.01 E-value: 7.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 301 SKTVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTK--- 377
Cdd:cd19123 1 MKTLPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKlwn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 378 -------VMPgnydrayqSIDESLARLGFDYIDLMLVH-----QSG-----SGD----------EEVYKALCQGVADGKI 430
Cdd:cd19123 81 nshapedVLP--------ALEKTLADLQLDYLDLYLMHwpvalKKGvgfpeSGEdllslspiplEDTWRAMEELVDKGLC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 431 RSIGISNyYTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFgGRGHTSESFNNE--------- 501
Cdd:cd19123 153 RHIGVSN-FSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPL-GSGDRPAAMKAEgepvlledp 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 502 VIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19123 231 VINKIAEKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
299-561 |
1.89e-56 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 191.17 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 299 FESKTVLLNSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRkaiDEGiVKREDVFVTTKV 378
Cdd:cd19117 1 PSSKTFKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIK---DSG-VPREEIFITTKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 MPGNYDRAYQSIDESLARLGFDYIDLMLVHQSGS----GDEEVYKA------------------LCQG-VADGKIRSIGI 435
Cdd:cd19117 77 WCTWHRRVEEALDQSLKKLGLDYVDLYLMHWPVPldpdGNDFLFKKddgtkdhepdwdfiktweLMQKlPATGKVKAIGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 436 SNYYTADeVERV--TDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGhtSESFNNEVIVELAEKYNKT 513
Cdd:cd19117 157 SNFSIKN-LEKLlaSPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTN--APLLKEPVIIKIAKKHGKT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1167055252 514 SAQIILRWQVQAGYIAIPGSSNPEHIAENIDIfdFELSESEMQSMTSL 561
Cdd:cd19117 234 PAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
309-556 |
2.52e-56 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 190.13 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTWT---------QDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgiVKREDVFVTT 376
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVG----KAIKG--FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 377 KVMPGN--YDRAYQSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNYYTAD--EVERVTDG 450
Cdd:cd19072 75 KVSPDHlkYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIpiEETLRAMEELVEEGKIRYIGVSNFSLEEleEAQSYLKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 451 ADIkpAVIQNENHLYYQN--TELQEYVKQYGTVIESWYPFGgRGHTSESFNNEVIVELAEKYNKTSAQIILRWQV-QAGY 527
Cdd:cd19072 155 GPI--VANQVEYNLFDREeeSGLLPYCQKNGIAIIAYSPLE-KGKLSNAKGSPLLDEIAKKYGKTPAQIALNWLIsKPNV 231
|
250 260
....*....|....*....|....*....
gi 1167055252 528 IAIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19072 232 IAIPKASNIEHLEENAGALGWELSEEDLQ 260
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
312-566 |
1.97e-53 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 182.53 E-value: 1.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 312 MPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGngvrKAIDEGIVKREDVFVTTKVMPGNY--DRAYQS 389
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIDNLakDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 390 IDESLARLGFDYIDLMLVHQSGSGDE----EVYKALCQGVADGKIRSIGISNYyTADEVERVTD--GADiKPAVIQNENH 463
Cdd:PRK11172 79 LKESLQKLRTDYVDLTLIHWPSPNDEvsveEFMQALLEAKKQGLTREIGISNF-TIALMKQAIAavGAE-NIATNQIELS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 464 LYYQNTELQEYVKQYGTVIESWYPFGgrghTSESFNNEVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENI 543
Cdd:PRK11172 157 PYLQNRKVVAFAKEHGIHVTSYMTLA----YGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNL 232
|
250 260
....*....|....*....|...
gi 1167055252 544 DIFDFELSESEMQSMTSLNTGQR 566
Cdd:PRK11172 233 LAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
307-569 |
2.04e-53 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 183.43 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGNY--D 384
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHrpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 385 RAYQSIDESLARLGFDYIDLMLVHQSGS---GDE-------------------EVYKALCQGVADGKIRSIGISNyYTAD 442
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAfqpGDEqdprdangnviyddgvtllDTWRAMERLVDEGRCKAIGLSD-VSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 443 EVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFggrGHTSES--FNNEVIVELAEKYNKTSAQIILR 520
Cdd:cd19129 160 KLREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPL---GHGMEPklLEDPVITAIARRVNKTPAQVLLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1167055252 521 WQVQAGYIAIPGSSNPEHIAENIDIfdFELSESEMQSMTS-LNTGQRYEN 569
Cdd:cd19129 237 WAIQRGTALLTTSKTPSRIRENFDI--STLPEDAMREINEgIKTRYRFNS 284
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
309-566 |
7.03e-53 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 182.62 E-value: 7.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGNYDRAY- 387
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 388 -QSIDESLARLGFDYIDLMLVH-----QSGSG----DE------------EVYKALCQGVADGKIRSIGISNyYTADEVE 445
Cdd:cd19107 81 kGACQKTLSDLKLDYLDLYLIHwptgfKPGKElfplDEsgnvipsdttflDTWEAMEELVDEGLVKAIGVSN-FNHLQIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 446 RVTD--GADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFG------GRGHTSESFNNEVIVELAEKYNKTSAQI 517
Cdd:cd19107 160 RILNkpGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpwAKPEDPSLLEDPKIKEIAAKHNKTTAQV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1167055252 518 ILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQR 566
Cdd:cd19107 240 LIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
309-567 |
4.73e-51 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 177.68 E-value: 4.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTWTQDDETTE----ESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGNYD 384
Cdd:cd19109 1 GNSIPIIGLGTYSEPKTTPKgacaEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 385 --RAYQSIDESLARLGFDYIDLMLVHQSGS---GDE------------------EVYKALCQGVADGKIRSIGISNYyTA 441
Cdd:cd19109 81 peLVRPTLERTLKVLQLDYVDLYIIEMPMAfkpGDEiyprdengkwlyhktnlcATWEALEACKDAGLVKSIGVSNF-NR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 442 DEVERVTD--GADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHTS-------ESFNNEVIVELAEKYNK 512
Cdd:cd19109 160 RQLELILNkpGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIwvnvsspPLLEDPLLNSIGKKYNK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1167055252 513 TSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRY 294
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
311-566 |
8.88e-51 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 176.69 E-value: 8.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 311 EMPIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGNYDRAY--Q 388
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLvkT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 389 SIDESLARLGFDYIDLMLVH-----QSGSGDEEV----------------YKALCQGVADGKIRSIGISNYyTADEVERV 447
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHwpmgfKPGEPDLPLdrsgmvipsdtdfldtWEAMEDLVIEGLVKNIGVSNF-NHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 448 TD--GADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHTSESFNNEVIVELAEKYNKTSAQIILRWQVQA 525
Cdd:cd19110 162 LNkpGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVDLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1167055252 526 GYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQR 566
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLR 282
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
313-561 |
2.48e-49 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 171.94 E-value: 2.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 313 PIIGLGTWTQDDETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVMPGNYDR---AYQs 389
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPenvKEQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 390 IDESLARLGFDYIDLMLVHQ---------------------SGSGDEEVYKALCQGVADGKIRSIGISNYYTAdEVERVT 448
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWplafdmdtdgdprddnqiqslSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTK-LLTDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 449 DGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGR-GHTSESF-NNEVIVELAEKYNKTSAQIILRWQVQ-- 524
Cdd:cd19128 160 NYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSyGDGNLTFlNDSELKALATKYNTTPPQVIIAWHLQkw 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1167055252 525 -AGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSL 561
Cdd:cd19128 240 pKNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
315-562 |
5.16e-49 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 171.73 E-value: 5.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTWT-------QDDETTEESVYSALKDGYRLIDTAQYYG---NETGVGngvrKAIDEGIVKREDVFVTTKVMPGNYD 384
Cdd:pfam00248 1 IGLGTWQlgggwgpISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLG----EALKDYPVKRDKVVIATKVPDGDGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 385 RAY--------QSIDESLARLGFDYIDLMLVHQSG--SGDEEVYKALCQGVADGKIRSIGISNYyTADEVERVTDGADIK 454
Cdd:pfam00248 77 WPSggskenirKSLEESLKRLGTDYIDLYYLHWPDpdTPIEETWDALEELKKEGKIRAIGVSNF-DAEQIEKALTKGKIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 455 PAVIQNENHLYY--QNTELQEYVKQYGTVIESWYPFG-----GRGHTSESFNN------------------EVIVELAEK 509
Cdd:pfam00248 156 IVAVQVEYNLLRrrQEEELLEYCKKNGIPLIAYSPLGgglltGKYTRDPDKGPgerrrllkkgtplnlealEALEEIAKE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1167055252 510 YNKTSAQIILRW--QVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLN 562
Cdd:pfam00248 236 HGVSPAQVALRWalSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
302-555 |
1.48e-47 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 167.04 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 302 KTVLLNSGYEMPIIGLGTWT--QDDETTEESVySALKD----GYRLIDTAQYYGN---ETGVGNGVRkaideGIvkREDV 372
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYmgEDPAKRAQEI-EALRAgidlGMTLIDTAEMYGDggsEELVGEAIR-----GR--RDKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 373 FVTTKVMPGN--YDRAYQSIDESLARLGFDYIDLMLVHQSGSGD-EEVYKALCQGVADGKIRSIGISNYYTAD--EVERV 447
Cdd:cd19138 73 FLVSKVLPSNasRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPlAETVAAMEELKKEGKIRAWGVSNFDTDDmeELWAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 448 TDGadIKPAVIQNENHLYYQNTE--LQEYVKQYGTVIESWYPFG-GRGHTSESFNNEVIVELAEKYNKTSAQIILRWQV- 523
Cdd:cd19138 153 PGG--GNCAANQVLYNLGSRGIEydLLPWCREHGVPVMAYSPLAqGGLLRRGLLENPTLKEIAARHGATPAQVALAWVLr 230
|
250 260 270
....*....|....*....|....*....|..
gi 1167055252 524 QAGYIAIPGSSNPEHIAENIDIFDFELSESEM 555
Cdd:cd19138 231 DGNVIAIPKSGSPEHARENAAAADLELTEEDL 262
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
303-567 |
8.87e-45 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 160.47 E-value: 8.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 303 TVLLNSGYEMPIIGLGTWTQDD---ETTEESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEGIVKREDVFVTTKVM 379
Cdd:cd19108 2 RVKLNDGHFIPVLGFGTYAPEEvpkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 380 PGNY--DRAYQSIDESLARLGFDYIDLMLVH---QSGSGDEEV------------------YKAL--CQGVadGKIRSIG 434
Cdd:cd19108 82 CTFHrpELVRPALEKSLKKLQLDYVDLYLIHfpvALKPGEELFpkdengklifdtvdlcatWEAMekCKDA--GLAKSIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 435 ISNyYTADEVERVTD--GADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGHT---SES----FNNEVIVE 505
Cdd:cd19108 160 VSN-FNRRQLEMILNkpGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKewvDQNspvlLEDPVLCA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167055252 506 LAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSLNTGQRY 567
Cdd:cd19108 239 LAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLRY 300
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
306-558 |
4.67e-43 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 155.47 E-value: 4.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 306 LNSGYEMPIIGLGTWTQDDETTE--ESVYSALKDGYRLIDTAQYYGNETGVGNGVRKAIDEG-IVKREDVFVTTKVMPG- 381
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGAKGEtyAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 -NYDRAYQSIDESLARLGFDYIDLMLVHQSGSGD-------------------------EEVYKALCQGVADGKIRSIGI 435
Cdd:cd19122 83 hEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEkndqrspklgpdgkyvilkdltenpEPTWRAMEEIYESGKAKAIGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 436 SNYyTADEVERVTDGADIKPAVIQNENHLYYQNTELQEYVKQYGTVIESWYPFGGRGH---TSESFN-NEVIVELAEKYN 511
Cdd:cd19122 163 SNW-TIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQvpsTGERVSeNPTLNEVAEKGG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1167055252 512 KTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIfdFELSESEMQSM 558
Cdd:cd19122 242 YSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAI 286
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
307-556 |
3.06e-41 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 151.48 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTWT-------QDDETTEESVYSALKDGYRLIDTAQYYG---NETGVGNGVRKaidegiVKREDVFVTT 376
Cdd:COG0667 8 RSGLKVSRLGLGTMTfggpwggVDEAEAIAILDAALDAGINFFDTADVYGpgrSEELLGEALKG------RPRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 377 KV--------MPGNYDRAY--QSIDESLARLGFDYIDLMLVHqsgSGD-----EEVYKALCQGVADGKIRSIGISNyYTA 441
Cdd:COG0667 82 KVgrrmgpgpNGRGLSREHirRAVEASLRRLGTDYIDLYQLH---RPDpdtpiEETLGALDELVREGKIRYIGVSN-YSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 442 DEVERVTDGAD--IKPAVIQNENHLYYQN--TELQEYVKQYGTVIESWYPFGG--------RGHT-------SESFNN-- 500
Cdd:COG0667 158 EQLRRALAIAEglPPIVAVQNEYSLLDRSaeEELLPAARELGVGVLAYSPLAGglltgkyrRGATfpegdraATNFVQgy 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167055252 501 ---------EVIVELAEKYNKTSAQIILRWQVQAGYI--AIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:COG0667 238 lternlalvDALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSAEDLA 304
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
311-556 |
8.58e-39 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 143.91 E-value: 8.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 311 EMPIIGLGTWT-----------QDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgIVKREDVFVTT 376
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLG----RFLKE-LGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 377 KVMPGNYDRAYQSI----DESLARLGFDYIDLMLVHQSG---SGDEEVYKALCQGVADGKIRSIGISNYyTADEVERV-- 447
Cdd:cd19093 76 KFAPLPWRLTRRSVvkalKASLERLGLDSIDLYQLHWPGpwySQIEALMDGLADAVEEGLVRAVGVSNY-SADQLRRAhk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 448 -TDGADIKPAVIQNENHLYYQN---TELQEYVKQYGTVI-----------------ESWYPFGGRGHTSESFNNEV---- 502
Cdd:cd19093 155 aLKERGVPLASNQVEYSLLYRDpeqNGLLPACDELGITLiaysplaqglltgkyspENPPPGGRRRLFGRKNLEKVqpll 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 503 --IVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19093 235 daLEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVA 290
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
309-556 |
8.03e-38 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 140.40 E-value: 8.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLGTW----------TQDDETTEeSVYSALKDGYRLIDTAQYYG---NETGVGngvrKAIDEgiVKREDVFVT 375
Cdd:cd19137 1 GEKIPALGLGTWgiggfltpdySRDEEMVE-LLKTAIELGYTHIDTAEMYGgghTEELVG----KAIKD--FPREDLFIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 376 TKVMPGN--YDRAYQSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNYyTADEVERVTDGA 451
Cdd:cd19137 74 TKVWPTNlrYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIplEETLSAMAEGVRQGLIRYIGVSNF-NRRLLEEAISKS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 452 DIKPAVIQNENHLY---YQNTELQEYVKQYGTVIESWYPFGgRGHTSEsfnNEVIVELAEKYNKTSAQIILRWQVQA-GY 527
Cdd:cd19137 153 QTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLR-RGLEKT---NRTLEEIAKNYGKTIAQIALAWLIQKpNV 228
|
250 260
....*....|....*....|....*....
gi 1167055252 528 IAIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19137 229 VAIPKAGRVEHLKENLKATEIKLSEEEMK 257
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
315-556 |
1.55e-36 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 137.66 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTW--------TQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgivKREDVFVTTKVmpGNY 383
Cdd:cd19084 7 IGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILG----KALKG---RRDDVVIATKC--GLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 384 -------------DRAYQSIDESLARLGFDYIDLMLVHqsgSGD-----EEVYKALCQGVADGKIRSIGISNyYTADEVE 445
Cdd:cd19084 78 wdggkgvtkdlspESIRKEVEQSLRRLQTDYIDLYQIH---WPDpntpiEETAEALEKLKKEGKIRYIGVSN-FSVEQLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 446 RVTDGADIkpAVIQNENHLYYQNTE--LQEYVKQYGTVIESW-----------------YPFGGRGHTSESFNNE----- 501
Cdd:cd19084 154 EARKYGPI--VSLQPPYSMLEREIEeeLLPYCRENGIGVLPYgplaqglltgkykkeptFPPDDRRSRFPFFRGEnfekn 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167055252 502 -----VIVELAEKYNKTSAQIILRWQVQ--AGYIAIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19084 232 leivdKLKEIAEKYGKSLAQLAIAWTLAqpGVTSAIVGAKNPEQLEENAGALDWELTEEELK 293
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
313-560 |
1.91e-34 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 131.94 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 313 PIIGLGTWT---------QDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaidegivKREDVFVTTKVMP 380
Cdd:cd19085 2 SRLGLGCWQfgggywwgdQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 GN--YDRAYQSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNYYTADeVERVTDGADIkpA 456
Cdd:cd19085 75 DNltPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVplEETMEALEKLKEEGKIRAIGVSNFGPAQ-LEEALDAGRI--D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 457 VIQNENHLYYQN--TELQEYVKQYGTVIESWYP---------------------------FGGRGHTSESFNN-EVIVEL 506
Cdd:cd19085 152 SNQLPYNLLWRAieYEILPFCREHGIGVLAYSPlaqglltgkfssaedfppgdartrlfrHFEPGAEEETFEAlEKLKEI 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 507 AEKYNKTSAQIILRWQVQAGYI--AIPGSSNPEHIAENIDIFDFELSESEMQSMTS 560
Cdd:cd19085 232 ADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERLDE 287
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
315-544 |
1.26e-32 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 124.94 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTWT----QDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIdEGIVKREDVFVTTKV--------M 379
Cdd:cd06660 3 LGLGTMTfggdGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLG----RWL-KGRGNRDDVVIATKGghppggdpS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 380 PGNYDRAY--QSIDESLARLGFDYIDLMLVHQSGSG--DEEVYKALCQGVADGKIRSIGISNyYTADEVERVTDGAD--- 452
Cdd:cd06660 78 RSRLSPEHirRDLEESLRRLGTDYIDLYYLHRDDPStpVEETLEALNELVREGKIRYIGVSN-WSAERLAEALAYAKahg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 453 -IKPAVIQNENHLYYQN---TELQEYVKQYGTVIESWYPFgGRGhtsesfnnevivelaekynktSAQIILRWQVQAGY- 527
Cdd:cd06660 157 lPGFAAVQPQYSLLDRSpmeEELLDWAEENGLPLLAYSPL-ARG---------------------PAQLALAWLLSQPFv 214
|
250
....*....|....*...
gi 1167055252 528 -IAIPGSSNPEHIAENID 544
Cdd:cd06660 215 tVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
312-551 |
3.93e-28 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 113.08 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 312 MPIIGLGTWTQ--DDETTEESVYSALKDGYRLIDTAQYYG---NETGVGNGVRKAidegivkREDVFVTTKV-----MPG 381
Cdd:cd19088 9 MRLTGPGIWGPpaDREEAIAVLRRALELGVNFIDTADSYGpdvNERLIAEALHPY-------PDDVVIATKGglvrtGPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 NYDRA------YQSIDESLARLGFDYIDLMLVH---QSGSGDEEVyKALCQGVADGKIRSIGISNYyTADEVERVTDGAD 452
Cdd:cd19088 82 WWGPDgspeylRQAVEASLRRLGLDRIDLYQLHridPKVPFEEQL-GALAELQDEGLIRHIGLSNV-TVAQIEEARAIVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 453 IkpAVIQNENHLYYQNTE-LQEYVKQYGTVIESWYPFGGRGHTsesFNNEVIVELAEKYNKTSAQIILRWQVQ--AGYIA 529
Cdd:cd19088 160 I--VSVQNRYNLANRDDEgVLDYCEAAGIAFIPWFPLGGGDLA---QPGGLLAEVAARLGATPAQVALAWLLArsPVMLP 234
|
250 260
....*....|....*....|..
gi 1167055252 530 IPGSSNPEHIAENIDIFDFELS 551
Cdd:cd19088 235 IPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
307-558 |
6.63e-28 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 113.83 E-value: 6.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGT----------WTQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgIVKREDVF 373
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILG----RALKE-FAPRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 374 VTTKV-MPGNYD-------RAY--QSIDESLARLGFDYIDLMLVHqsgSGD-----EEVYKALCQGVADGKIRSIGISNY 438
Cdd:cd19079 82 IATKVyFPMGDGpngrglsRKHimAEVDASLKRLGTDYIDLYQIH---RWDyetpiEETLEALHDVVKSGKVRYIGASSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 439 YtADEVERVTDGADI----KPAVIQNENHLYYQN--TELQEYVKQYGTVIESWYPF------GGRGHTSESFN------- 499
Cdd:cd19079 159 Y-AWQFAKALHLAEKngwtKFVSMQNHYNLLYREeeREMIPLCEEEGIGVIPWSPLargrlaRPWGDTTERRRsttdtak 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167055252 500 -------------NEVIVELAEKYNKTSAQIILRWQVQAGYIAIP--GSSNPEHIAENIDIFDFELSESEMQSM 558
Cdd:cd19079 238 lkydyfteadkeiVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
307-556 |
2.69e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.29 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTW---TQDDETTEESVYSALKDGYRLIDTAQYYGN-ETGVGNGVRKAidegivkREDVFVTTKVMPG- 381
Cdd:COG1453 8 KTGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLPPWv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 -NYDRAYQSIDESLARLGFDYIDLMLVHQSGSGDE--------EVYKALCQGVADGKIRSIGISNYYTADEVERVTDGAD 452
Cdd:COG1453 81 rDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDlekvlkpgGALEALEKAKAEGKIRHIGFSTHGSLEVIKEAIDTGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 453 IkpAVIQneNHLYYQNTELQ------EYVKQYG---TVIEswyPF-GGRGHTsesfNNEVIVELAEKyNKTSAQIILRW- 521
Cdd:COG1453 161 F--DFVQ--LQYNYLDQDNQageealEAAAEKGigvIIMK---PLkGGRLAN----PPEKLVELLCP-PLSPAEWALRFl 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1167055252 522 ----QVQAgyiAIPGSSNPEHIAENIDIFD-FE-LSESEMQ 556
Cdd:COG1453 229 lshpEVTT---VLSGMSTPEQLDENLKTADnLEpLTEEELA 266
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
302-436 |
3.78e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 101.40 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 302 KTVLLNSGYEMPIIGLGTWTQ---DDETTEESVYSALKDGYRLIDTAQYYGN-ETGVGNGVRKaidegivKREDVFVTTK 377
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLgrlSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATK 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167055252 378 VMPGNYDRAYQSIDESLARLGFDYIDLMLVHQSGSGDE--------EVYKALCQGVADGKIRSIGIS 436
Cdd:cd19100 74 TGARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDldqvfgpgGALEALLEAKEEGKIRFIGIS 140
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
307-560 |
4.35e-24 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 103.12 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTW---------TQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgivKREDVFV 374
Cdd:cd19149 6 KSGIEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVG----KAIKG---RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 375 TTK------------VMPGNYDRAY---------QSIDESLARLGFDYIDLMLVH-QSGSGD-EEVYKALCQGVADGKIR 431
Cdd:cd19149 79 ATKcglrwdreggsfFFVRDGVTVYknlspesirEEVEQSLKRLGTDYIDLYQTHwQDVETPiEETMEALEELKRQGKIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 432 SIGISNYYTADEVERVTDGadiKPAVIQ------NENHlyyqNTELQEYVKQYGTVIESWYPFG-----GRGHTSESF-- 498
Cdd:cd19149 159 AIGASNVSVEQIKEYVKAG---QLDIIQekysmlDRGI----EKELLPYCKKNNIAFQAYSPLEqglltGKITPDREFda 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 499 -------------NNEVIVE-------LAEKYNKTSAQIILRWQV-QAGYI-AIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19149 232 gdarsgipwfspeNREKVLAllekwkpLCEKYGCTLAQLVIAWTLaQPGITsALCGARKPEQAEENAKAGDIRLSAEDIA 311
|
....
gi 1167055252 557 SMTS 560
Cdd:cd19149 312 TMRS 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
302-556 |
4.83e-24 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 102.68 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 302 KTVLL-NSGYEMPIIGLG----TW---TQDDETTEESVYSALKDGYRLIDTAQYYG---NETGVGNGVRKaidegivKRE 370
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGcmgmSAfygPADEEESIATLHRALELGVTFLDTADMYGpgtNEELLGKALKD-------RRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 371 DVFVTTK------------VMPGNYDRAYQSIDESLARLGFDYIDLMLVHQSgsgD-----EEVYKALCQGVADGKIRSI 433
Cdd:cd19076 74 EVVIATKfgivrdpgsgfrGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRV---DpnvpiEETVGAMAELVEEGKVRYI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 434 GISNyYTADEVERvtdGADIKP-AVIQNENHLYYQN--TELQEYVKQYGTVIESWYPFgGRG------------------ 492
Cdd:cd19076 151 GLSE-ASADTIRR---AHAVHPiTAVQSEYSLWTRDieDEVLPTCRELGIGFVAYSPL-GRGfltgaikspedlpeddfr 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 493 -----HTSESF-NNEVIVE----LAEKYNKTSAQIILRWQVQAG--YIAIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19076 226 rnnprFQGENFdKNLKLVEkleaIAAEKGCTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVGALDVVLTPEELA 301
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
315-544 |
8.22e-24 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 100.24 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTWT--------QDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgivKREDVFVTTKV----- 378
Cdd:cd19086 6 IGFGTWGlggdwwgdVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLG----KALKG---RRDKVVIATKFgnrfd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 ----MPGNYDRAY--QSIDESLARLGFDYIDLMLVH---QSGSGDEEVYKALCQGVADGKIRSIGIS-NyyTADEVERVT 448
Cdd:cd19086 79 ggpeRPQDFSPEYirEAVEASLKRLGTDYIDLYQLHnppDEVLDNDELFEALEKLKQEGKIRAYGVSvG--DPEEALAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 449 DGADIkpAVIQNENHLYYQNTE--LQEYVKQYGT-VIeswypfgGRGHTSESFnneviveLAEKYnktsAQIILRW---- 521
Cdd:cd19086 157 RRGGI--DVVQVIYNLLDQRPEeeLFPLAEEHGVgVI-------ARVPLASGL-------LTGKL----AQAALRFilsh 216
|
250 260
....*....|....*....|....
gi 1167055252 522 -QVQagyIAIPGSSNPEHIAENID 544
Cdd:cd19086 217 pAVS---TVIPGARSPEQVEENAA 237
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
315-553 |
2.06e-23 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 100.74 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTWTQ-----DDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaidegiVKREDVFVTTKVM----PGN 382
Cdd:cd19074 7 LSLGTWLTfggqvDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVFwptgPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 YDRA------YQSIDESLARLGFDYIDLMLVHqsgSGD-----EEVYKALCQGVADGKIRSIGISNyYTADEVERVTDGA 451
Cdd:cd19074 81 NDRGlsrkhiFESIHASLKRLQLDYVDIYYCH---RYDpetplEETVRAMDDLIRQGKILYWGTSE-WSAEQIAEAHDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 452 D----IKPAVIQNENHLYYQN--TELQEYVKQYGTVIESWYPF------------------------GGRGHTSESFNNE 501
Cdd:cd19074 157 RqfglIPPVVEQPQYNMLWREieEEVIPLCEKNGIGLVVWSPLaqglltgkyrdgipppsrsratdeDNRDKKRRLLTDE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 502 VI------VELAEKYNKTSAQIILRWQVQAGYI--AIPGSSNPEHIAENIDIFDFELSES 553
Cdd:cd19074 237 NLekvkklKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
307-556 |
2.39e-23 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 100.32 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGT-------WTQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaidegiVKREDVFVTT 376
Cdd:cd19163 8 KTGLKVSKLGFGAsplggvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKALKG------IPRDSYYLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 377 KVmpGNYD------------RAYQSIDESLARLGFDYIDLMLVHQ---SGSGD---EEVYKALCQGVADGKIRSIGISNY 438
Cdd:cd19163 82 KV--GRYGldpdkmfdfsaeRITKSVEESLKRLGLDYIDIIQVHDiefAPSLDqilNETLPALQKLKEEGKVRFIGITGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 439 ---YTADEVERVTDGADikpaVIQNENHLYYQNTELQEYV---KQYGTVIESWYPFGGRGHTSESF------NNEVI--- 503
Cdd:cd19163 160 pldVLKEVLERSPVKID----TVLSYCHYTLNDTSLLELLpffKEKGVGVINASPLSMGLLTERGPpdwhpaSPEIKeac 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167055252 504 ---VELAEKYNKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19163 236 akaAAYCKSRGVDISKLALQFALSNPDIAttLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
304-559 |
5.38e-23 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 99.60 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 304 VLLNSGYEMPIIGLGT----WTQDDETTEESVYSALKDGYRLIDTAQYYGN----------ETGVGNGVRKAidegiVKR 369
Cdd:cd19081 1 PLGRTGLSVSPLCLGTmvfgWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnaggesETIIGRWLKSR-----GKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 370 EDVFVTTKV---MPGNY---DRAY--QSIDESLARLGFDYIDLMLVHQSgsgD-----EEVYKALCQGVADGKIRSIGIS 436
Cdd:cd19081 76 DRVVIATKVgfpMGPNGpglSRKHirRAVEASLRRLQTDYIDLYQAHWD---DpatplEETLGALNDLIRQGKVRYIGAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 437 NyYTADEVERVTDGAD----IKPAVIQNENHLYYQNT---ELQEYVKQYGTVIESWYPFGG------------------R 491
Cdd:cd19081 153 N-YSAWRLQEALELSRqhglPRYVSLQPEYNLVDRESfegELLPLCREEGIGVIPYSPLAGgfltgkyrseadlpgstrR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167055252 492 GHTSESFNNE-------VIVELAEKYNKTSAQIILRWQVQAGYIAIP--GSSNPEHIAENIDIFDFELSESEMQSMT 559
Cdd:cd19081 232 GEAAKRYLNErglrildALDEVAAEHGATPAQVALAWLLARPGVTAPiaGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
313-544 |
1.16e-22 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 97.31 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 313 PIIGLGTW-------TQDDETTEESVYSALKDGYRLIDTAQYYGN-ETGVGNGVRKaidegiVKREDVFVTTKVMPGN-- 382
Cdd:cd19095 1 SVLGLGTSgigrvwgVPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHGeg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 383 --------YDRAYQSIDESLARLGFDYIDLMLVHqSGSGDE---EVYKALCQGVADGKIRSIGISNYYtaDEVERV--TD 449
Cdd:cd19095 75 grdrkdfsPAAIRASIERSLRRLGTDYIDLLQLH-GPSDDEltgEVLETLEDLKAAGKVRYIGVSGDG--EELEAAiaSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 450 GADikpaVIQNENHLYYQ-NTELQEYVKQYGT-VI------ESWYPFGGRGHTSESFNNEVIVELAEKYNKTSAQIILRW 521
Cdd:cd19095 152 VFD----VVQLPYNVLDReEEELLPLAAEAGLgVIvnrplaNGRLRRRVRRRPLYADYARRPEFAAEIGGATWAQAALRF 227
|
250 260
....*....|....*....|....*
gi 1167055252 522 QVQAGYI--AIPGSSNPEHIAENID 544
Cdd:cd19095 228 VLSHPGVssAIVGTTNPEHLEENLA 252
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
315-555 |
2.72e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 97.36 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTW------------TQDDETTEESVYSALKDGYRLIDTAQYYG---NETGVGngvrKAIDEgivKREDVFVTTKV- 378
Cdd:cd19102 4 IGLGTWaiggggwgggwgPQDDRDSIAAIRAALDLGINWIDTAAVYGlghSEEVVG----RALKG---LRDRPIVATKCg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 -MPGNYDRAYQS---------IDESLARLGFDYIDLMLVH-QSGSGD-EEVYKALCQGVADGKIRSIGISNyYTADEVER 446
Cdd:cd19102 77 lLWDEEGRIRRSlkpasiraeCEASLRRLGVDVIDLYQIHwPDPDEPiEEAWGALAELKEEGKVRAIGVSN-FSVDQMKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 447 VtdgADIKP-AVIQNENHLYYQN--TELQEYVKQYGT-VI---------------ESW---YPFGGRGHTSESFN----- 499
Cdd:cd19102 156 C---QAIHPiASLQPPYSLLRRGieAEILPFCAEHGIgVIvyspmqsglltgkmtPERvasLPADDWRRRSPFFQepnla 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 500 -NEVIVE----LAEKYNKTSAQIILRW-----QVQAgyiAIPGSSNPEHIAENIDIFDFELSESEM 555
Cdd:cd19102 233 rNLALVDalrpIAERHGRTVAQLAIAWvlrrpEVTS---AIVGARRPDQIDETVGAADLRLTPEEL 295
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
307-551 |
2.98e-22 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 96.86 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTW-----TQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEGIVKREDVFVTTKV 378
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFG----EALALNPGLREKIEIQTKC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 -----------MPGNYD--RAY--QSIDESLARLGFDYIDLMLVHQSgsgD-----EEVYKALCQGVADGKIRSIGISNY 438
Cdd:cd19092 77 girlgddprpgRIKHYDtsKEHilASVEGSLKRLGTDYLDLLLLHRP---DplmdpEEVAEAFDELVKSGKVRYFGVSNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 439 YTAdEVERVTDGADIKPAVIQNE---NHLYYQNTELQEYVKQYGTVIESWYPFGG----RGHTSESFN-NEVIVELAEKY 510
Cdd:cd19092 154 TPS-QIELLQSYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLGGgrlfGGFDERFQRlRAALEELAEEY 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1167055252 511 NKTSAQIILRWQVQ--AGYIAIPGSSNPEHIAENIDIFDFELS 551
Cdd:cd19092 233 GVTIEAIALAWLLRhpARIQPILGTTNPERIRSAVKALDIELT 275
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
313-547 |
3.88e-22 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 96.09 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 313 PIIGLGT--------WTQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaidegiVKREDVFVTTKVMPG 381
Cdd:cd19096 1 SVLGFGTmrlpesddDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE------GPREKFYLATKLPPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 ---NYDRAYQSIDESLARLGFDYIDLMLVHqsGSGDEEVYKALCQG---------VADGKIRSIGISNYYTADEVERVTD 449
Cdd:cd19096 75 svkSAEDFRRILEESLKRLGVDYIDFYLLH--GLNSPEWLEKARKGglleflekaKKEGLIRHIGFSFHDSPELLKEILD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 450 GADIKPAVIqnenHLYYQNTELQEYVKQY--------GTVIESwyPFGGRGHTsesFNNEVIVELAEKYNKTSAQIILRW 521
Cdd:cd19096 153 SYDFDFVQL----QYNYLDQENQAGRPGIeyaakkgmGVIIME--PLKGGGLA---NNPPEALAILCGAPLSPAEWALRF 223
|
250 260
....*....|....*....|....*...
gi 1167055252 522 QVQAGYI--AIPGSSNPEHIAENIDIFD 547
Cdd:cd19096 224 LLSHPEVttVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
303-545 |
2.94e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 93.42 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 303 TVLLNSGYEMPIIGLGT-WTQDDETteESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaidegiVKREDVFVTTKV 378
Cdd:cd19105 4 RTLGKTGLKVSRLGFGGgGLPRESP--ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 MP--GNYDRA--YQSIDESLARLGFDYIDLMLVHQSGSG-----DEEVYKALCQGVADGKIRSIGISNYYTADEVerVTD 449
Cdd:cd19105 76 SPrlDKKDKAelLKSVEESLKRLQTDYIDIYQLHGVDTPeerllNEELLEALEKLKKEGKVRFIGFSTHDNMAEV--LQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 450 GADIKPA-VIQ-NENHLYYQNtELQEYV-----KQYGTVieSWYPFGGRGhtseSFNNEVIVELAEKYnkTSAQIILRWQ 522
Cdd:cd19105 154 AIESGWFdVIMvAYNFLNQPA-ELEEALaaaaeKGIGVV--AMKTLAGGY----LQPALLSVLKAKGF--SLPQAALKWV 224
|
250 260
....*....|....*....|....*
gi 1167055252 523 VQAGYI--AIPGSSNPEHIAENIDI 545
Cdd:cd19105 225 LSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
315-544 |
3.74e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 94.31 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTW-----TQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKAIDEGIVKREDVFVTTKV--MPGNYD 384
Cdd:cd19099 6 LGLGTYrgdsdDETDEEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKAgyIPGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 385 R-------------------------------AY--QSIDESLARLGFDYIDLMLVH-----QSGSGDEEVYK------- 419
Cdd:cd19099 86 EplrplkyleeklgrglidvadsaglrhcispAYleDQIERSLKRLGLDTIDLYLLHnpeeqLLELGEEEFYDrleeafe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 420 ALCQGVADGKIRSIGIS------NYYTADEVERVTDGADIKPAVIQNENHLYY-Q----------NTELQEYVKQYGTVI 482
Cdd:cd19099 166 ALEEAVAEGKIRYYGIStwdgfrAPPALPGHLSLEKLVAAAEEVGGDNHHFKViQlplnllepeaLTEKNTVKGEALSLL 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167055252 483 ESWYPFGGRGHTSESFN-------NEVIVELAEKYNKTSAQIILRWQVQA-GYI-AIPGSSNPEHIAENID 544
Cdd:cd19099 246 EAAKELGLGVIASRPLNqgqllgeLRLADLLALPGGATLAQRALQFARSTpGVDsALVGMRRPEHVDENLA 316
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
308-561 |
4.67e-21 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 94.02 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGT---------WTQDDETTEESVYSALKDGYRLIDTAQYYG---NETGVGNGVRKAidegivKREDVFVT 375
Cdd:cd19083 7 SDIDVNPIGLGTnavgghnlyPNLDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEY------NRNEVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 376 TKvmpG-----------NYDRAY--QSIDESLARLGFDYIDLMLVH--QSGSGDEEVYKALCQGVADGKIRSIGISNyYT 440
Cdd:cd19083 81 TK---GahkfggdgsvlNNSPEFlrSAVEKSLKRLNTDYIDLYYIHfpDGETPKAEAVGALQELKDEGKIRAIGVSN-FS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 441 ADEVERVTdgADIKPAVIQNENHLYYQNTE--LQEYVKQYGTVIESWYP-----FGGRGHTSESFNNEVI---------- 503
Cdd:cd19083 157 LEQLKEAN--KDGYVDVLQGEYNLLQREAEedILPYCVENNISFIPYFPlasglLAGKYTKDTKFPDNDLrndkplfkge 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167055252 504 ------------VELAEKYNKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENIDIFDFELSESEMQSMTSL 561
Cdd:cd19083 235 rfsenldkvdklKSIADEKGVTVAHLALAWYLTRPAIDvvIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
312-561 |
2.16e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 92.01 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 312 MPIIGLGTW---------------TQDDETTEESVYSALKDGYRLIDTAQYYG---NETGVGNGVRKaidegiVKREDVF 373
Cdd:cd19103 4 LPKIALGTWswgsggaggdqvfgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYGmgaSEKILGEFLKR------YPREDYI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 374 VTTKVMPG----NYDRAYQSIDESLARLGFDYIDLMLVHQSgSGDEEVYKALCQGVADGKIRSIGISNYYTAD--EVERV 447
Cdd:cd19103 78 ISTKFTPQiagqSADPVADMLEGSLARLGTDYIDIYWIHNP-ADVERWTPELIPLLKSGKVKHVGVSNHNLAEikRANEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 448 TDGADIKPAVIQNENHLYYQNTE---LQEYVKQYGTVIESW---------------YPFGGRGHTSESFN---------N 500
Cdd:cd19103 157 LAKAGVSLSAVQNHYSLLYRSSEeagILDYCKENGITFFAYmvleqgalsgkydtkHPLPEGSGRAETYNpllpqleelT 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167055252 501 EVIVELAEKYNKTSAQIILRWQVQAGYIAIPGSSNPEHIAENIDIFDFELSESEMQSMTSL 561
Cdd:cd19103 237 AVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
313-553 |
9.62e-19 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 86.45 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 313 PIIGLGT-------WTQDDETTEESVYSALKDGYRLIDTAQYYGN-ETGVGNGVRKaidegiVKREDVFVTTKV-----M 379
Cdd:cd19090 1 SALGLGTaglggvfGGVDDDEAVATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVgrlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 380 PGNY--DRAYQSIDESLARLGFDYIDLMLVH-------QSGSGDEEVYKALCQGVADGKIRSIGISNyYTADEVERVTDG 450
Cdd:cd19090 75 TADYsaDRVRRSVEESLERLGRDRIDLLMIHdpervpwVDILAPGGALEALLELKEEGLIKHIGLGG-GPPDLLRRAIET 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 451 ADIKPAVIQNENHLYYQN--TELQEYVKQYGT-VIESWyPFgGRGHTSESFNNEV-----------------IVELAEKY 510
Cdd:cd19090 154 GDFDVVLTANRYTLLDQSaaDELLPAAARHGVgVINAS-PL-GMGLLAGRPPERVrytyrwlspelldrakrLYELCDEH 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1167055252 511 NKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENIDIFDFELSES 553
Cdd:cd19090 232 GVPLPALALRFLLRDPRIStvLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
315-558 |
1.31e-18 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 86.59 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTWT--------QDDETTEESVYSALKDGYRLIDTAQYYG---NETGVGngvrKAIdEGIVKREDVFVTTKV----- 378
Cdd:cd19148 7 IALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVG----KAL-KEYGKRDRVVIATKVglewd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 ------MPGNYDRAYQSIDESLARLGFDYIDLMLVH--QSGSGDEEVYKALCQGVADGKIRSIGISNyYTADEVERVTDG 450
Cdd:cd19148 82 eggevvRNSSPARIRKEVEDSLRRLQTDYIDLYQVHwpDPLVPIEETAEALKELLDEGKIRAIGVSN-FSPEQMETFRKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 451 ADIkpAVIQNENHLYYQ--NTELQEYVKQYGTVIESWYP-----FGGRGHTSESFNN----------------------E 501
Cdd:cd19148 161 APL--HTVQPPYNLFEReiEKDVLPYARKHNIVTLAYGAlcrglLSGKMTKDTKFEGddlrrtdpkfqeprfsqylaavE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 502 VIVELA-EKYNKTSAQIILRWQVQAGY--IAIPGSSNPEHIAENIDIFDFELSESEMQSM 558
Cdd:cd19148 239 ELDKLAqERYGKSVIHLAVRWLLDQPGvsIALWGARKPEQLDAVDEVFGWSLNDEDMKEI 298
|
|
| PRK06934 |
PRK06934 |
flavodoxin; Provisional |
70-162 |
2.31e-18 |
|
flavodoxin; Provisional
Pssm-ID: 180760 [Multi-domain] Cd Length: 221 Bit Score: 84.19 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 70 TKSIAKRIAETIGADIYEIRTVKAYPKDGYETLDIAQEERRTGNLPEIVDDLPDLKEYSTVIIGGPIWNAYVSTPLARYL 149
Cdd:PRK06934 73 TQYVAQIIQEETGGDLFRIETVKPYPRQHDPLLKYAEQEVKEGGRPEMREKIQNLADYDQIFIGYPIWWYKMPMVMYSFF 152
|
90
....*....|...
gi 1167055252 150 ELTDLSEKTVIPF 162
Cdd:PRK06934 153 EQHDFSGKTLIPF 165
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
307-555 |
2.80e-18 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 86.13 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGT-------------WTQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgivKRE 370
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEgesEEILG----KALKG---RRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 371 DVFVTTKV---MPGNYDRA-------YQSIDESLARLGFDYIDLMLVHQ--SGSGDEEVYKALCQGVADGKIRSIGISNy 438
Cdd:cd19091 81 DVLIATKVrgrMGEGPNDVglsrhhiIRAVEASLKRLGTDYIDLYQLHGfdALTPLEETLRALDDLVRQGKVRYIGVSN- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 439 YTADEVERVTDGAD----IKPAVIQnenhLYYQ------NTELQEYVKQYGTVIESWYPFGG-----------------R 491
Cdd:cd19091 160 FSAWQIMKALGISErrglARFVALQ----AYYSllgrdlEHELMPLALDQGVGLLVWSPLAGgllsgkyrrgqpapegsR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167055252 492 GHTSE----SFNNE-------VIVELAEKYNKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENIDIFDFELSESEM 555
Cdd:cd19091 236 LRRTGfdfpPVDRErgydvvdALREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAGLSLTPEEI 312
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
323-560 |
4.62e-18 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 84.98 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 323 DDETTEESVYSALKDGYRLIDTAQYYG---NETGVGngvrKAIDEgivKREDVFVTTK----------VMPG---NYDRA 386
Cdd:cd19078 23 DKEEMIELIRKAVELGITFFDTAEVYGpytNEELVG----EALKP---FRDQVVIATKfgfkidggkpGPLGldsRPEHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 387 YQSIDESLARLGFDYIDLMLVHQSgsgD-----EEVYKALCQGVADGKIRSIGIS--NYYT---ADEVERVTdgadikpa 456
Cdd:cd19078 96 RKAVEGSLKRLQTDYIDLYYQHRV---DpnvpiEEVAGTMKELIKEGKIRHWGLSeaGVETirrAHAVCPVT-------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 457 VIQNENHLYYQN--TELQEYVKQYGTVIESWYPFgGRGHTSESFN------------------------NEVIVEL---- 506
Cdd:cd19078 165 AVQSEYSMMWREpeKEVLPTLEELGIGFVPFSPL-GKGFLTGKIDentkfdegddraslprftpealeaNQALVDLlkef 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 507 AEKYNKTSAQIILRWQV-QAGYIA-IPGSSNPEHIAENIDIFDFELSESEMQSMTS 560
Cdd:cd19078 244 AEEKGATPAQIALAWLLaKKPWIVpIPGTTKLSRLEENIGAADIELTPEELREIED 299
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
315-544 |
2.19e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 82.76 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTW----TQDDETTEESVYSALKDGYRLIDTAQYYG--NETGVGNGVRKAI-----DEGivKREDVFVTTKV--MPG 381
Cdd:cd19752 3 LCLGTMyfgtRTDEETSFAILDRYVAAGGNFLDTANNYAfwTEGGVGGESERLIgrwlkDRG--NRDDVVIATKVgaGPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 NYDRAY------------QSIDESLARLGFDYIDLMLVH--QSGSGDEEVYKALCQGVADGKIRSIGISNYYTadevERV 447
Cdd:cd19752 81 DPDGGPespeglsaetieQEIDKSLRRLGTDYIDLYYAHvdDRDTPLEETLEAFNELVKAGKVRAIGASNFAA----WRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 448 TDGADI-------KPAVIQnENHLYYQ-------------NTELQEYVK-------------QYGTVIESWYPFGGRGHT 494
Cdd:cd19752 157 ERARQIarqqgwaEFSAIQ-QRHSYLRprpgadfgvqrivTDELLDYASsrpdltllaysplLSGAYTRPDRPLPEQYDG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1167055252 495 SESFNN-EVIVELAEKYNKTSAQIILRW--QVQAGYIAIPGSSNPEHIAENID 544
Cdd:cd19752 236 PDSDARlAVLEEVAGELGATPNQVVLAWllHRTPAIIPLLGASTVEQLEENLA 288
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
317-556 |
8.79e-17 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 81.11 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 317 LGTWTQDDE-----TTEESvySALKDGYR-----LIDTAQYYGNETGvgngvRKAIDEGIV-KREDVFVTTK----VMP- 380
Cdd:cd19080 15 LGTMTFGTEwgwgaDREEA--RAMFDAYVeaggnFIDTANNYTNGTS-----ERLLGEFIAgNRDRIVLATKytmnRRPg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 -----GNYDRA-YQSIDESLARLGFDYIDLMLVHqsgSGD-----EEVYKALCQGVADGKIRSIGISNyYTADEVERVTD 449
Cdd:cd19080 88 dpnagGNHRKNlRRSVEASLRRLQTDYIDLLYVH---AWDfttpvEEVMRALDDLVRAGKVLYVGISD-TPAWVVARANT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 450 GADIK----PAVIQNENHLYYQNTELqEYV---KQYGTVIESWYPFGG-----------RGHTSESFNN----------- 500
Cdd:cd19080 164 LAELRgwspFVALQIEYSLLERTPER-ELLpmaRALGLGVTPWSPLGGglltgkyqrgeEGRAGEAKGVtvgfgkltern 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167055252 501 ----EVIVELAEKYNKTSAQIILRWQVQAGYIAIP--GSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19080 243 waivDVVAAVAEELGRSAAQVALAWVRQKPGVVIPiiGARTLEQLKDNLGALDLTLSPEQLA 304
|
|
| PRK07116 |
PRK07116 |
flavodoxin; Provisional |
60-162 |
1.52e-16 |
|
flavodoxin; Provisional
Pssm-ID: 180850 Cd Length: 160 Bit Score: 77.02 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 60 IVVYYSWSENTKSIAKRIAETIGADIYEIRTVKAYP--------KDGYETLDIAQEERRtgnlPEIVDDLPDLKEYSTVI 131
Cdd:PRK07116 6 LVAYFSATGTTKKVAEKLAEVTGADLFEIKPEQPYTaadldwndKKSRSSVEMADKSSR----PAIAKKIENIAEYDVIF 81
|
90 100 110
....*....|....*....|....*....|.
gi 1167055252 132 IGGPIWNAYVSTPLARYLELTDLSEKTVIPF 162
Cdd:PRK07116 82 LGFPIWWYVAPRIINTFLESYDFSGKTVIPF 112
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
334-459 |
1.72e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 79.49 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 334 ALKDGYRLIDTAQYYGN-ETGVGngvrkaidEGIVKREDVFVTTKVMPGNYDRA------YQSIDESLARLGFDYIDLML 406
Cdd:cd19097 35 ALKAGINTLDTAPAYGDsEKVLG--------KFLKRLDKFKIITKLPPLKEDKKedeaaiEASVEASLKRLKVDSLDGLL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 407 VHQSG---SGDEEVYKALCQGVADGKIRSIGISnYYTADEVERVTDgaDIKPAVIQ 459
Cdd:cd19097 107 LHNPDdllKHGGKLVEALLELKKEGLIRKIGVS-VYSPEELEKALE--SFKIDIIQ 159
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
316-471 |
2.53e-16 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 79.89 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 316 GLGTWTQDDETT---EESVYSALKDGYRLIDTAQYYGNETG---VGNGVRKAIdegiVKREDVFVTTKVmpGNY------ 383
Cdd:cd19153 21 ALGGVYGDGLEQdeaVAIVAEAFAAGINHFDTSPYYGAESSeavLGKALAALQ----VPRSSYTVATKV--GRYrdsefd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 384 ---DRAYQSIDESLARLGFDYIDLMLVHQSGSGD-----EEVYKALCQGVADGKIRSIGISNY---YTADEVERVTDGAd 452
Cdd:cd19153 95 ysaERVRASVATSLERLHTTYLDVVYLHDIEFVDydtlvDEALPALRTLKDEGVIKRIGIAGYpldTLTRATRRCSPGS- 173
|
170
....*....|....*....
gi 1167055252 453 ikPAVIQNENHLYYQNTEL 471
Cdd:cd19153 174 --LDAVLSYCHLTLQDARL 190
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
315-555 |
3.80e-16 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 79.21 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLG----TWTQDDETTEES---VYSALKDGYRLIDTAQYYGNETGVGN--GVRKAIDEGIVKREDVFV--------TTK 377
Cdd:cd19077 8 IGLGlmglTWRPNPTPDEEAfetMKAALDAGSNLWNGGEFYGPPDPHANlkLLARFFRKYPEYADKVVLsvkggldpDTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 378 VMPGNYDRAYQSIDESLARLGF-DYIDLmlvHQSGSGD-----EEVYKALCQGVADGKIRSIGISNYyTADEVERVtdgA 451
Cdd:cd19077 88 RPDGSPEAVRKSIENILRALGGtKKIDI---FEPARVDpnvpiEETIKALKELVKEGKIRGIGLSEV-SAETIRRA---H 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 452 DIKP-AVIQNENHLYYQ---NTELQEYVKQYGTVIESWYPFG------------------GRGH----TSESFNN----- 500
Cdd:cd19077 161 AVHPiAAVEVEYSLFSReieENGVLETCAELGIPIIAYSPLGrglltgriksladipegdFRRHldrfNGENFEKnlklv 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167055252 501 EVIVELAEKYNKTSAQIILRW---QVQAGYIAIPGSSNPEHIAENIDIFDFELSESEM 555
Cdd:cd19077 241 DALQELAEKKGCTPAQLALAWilaQSGPKIIPIPGSTTLERVEENLKAANVELTDEEL 298
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
301-554 |
1.54e-15 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 77.87 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 301 SKTVLLNSGYEMPIIGLGTW--------TQDDETTEESVYSALKDGYRLIDTAQYYG-NETGVGNGVRKAIDegivKRED 371
Cdd:cd19144 2 PTRTLGRNGPSVPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYGdSEELIGRWFKQNPG----KREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 372 VFVTTKV----------MPGNYDRAY--QSIDESLARLGFDYIDLMLVHQ--SGSGDEEVYKALCQGVADGKIRSIGISN 437
Cdd:cd19144 78 IFLATKFgieknvetgeYSVDGSPEYvkKACETSLKRLGVDYIDLYYQHRvdGKTPIEKTVAAMAELVQEGKIKHIGLSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 438 yYTADEVERvtdGADIKP-AVIQNENHLYYQNTE-----LQEYVKQYGTVIESWYPFgGRG------------------- 492
Cdd:cd19144 158 -CSAETLRR---AHAVHPiAAVQIEYSPFSLDIErpeigVLDTCRELGVAIVAYSPL-GRGfltgairspddfeegdfrr 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1167055252 493 ----HTSESF--NNEV---IVELAEKYNKTSAQIILRWQVQAG--YIAIPGSSNPEHIAENIDIFDFELSESE 554
Cdd:cd19144 233 maprFQAENFpkNLELvdkIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEE 305
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
315-552 |
4.79e-15 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 76.45 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTWTQDDETTEESVYS----ALKDGYRLIDTA---------QYYG-NETGVGNGVRKAidegiVKREDVFVTTKVMP 380
Cdd:cd19094 4 ICLGTMTWGEQNTEAEAHEqldyAFDEGVNFIDTAemypvppspETQGrTEEIIGSWLKKK-----GNRDKVVLATKVAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 381 G--------------NYDRAYQSIDESLARLGFDYIDLMLVH-------QSGSGD-------------EEVYKALCQGVA 426
Cdd:cd19094 79 PgegitwprgggtrlDRENIREAVEGSLKRLGTDYIDLYQLHwpdrytpLFGGGYytepseeedsvsfEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 427 DGKIRSIGISNyYTADEVERVTDGADI----KPAVIQNENHL-------------YYQNTELQEYVKQYGTVI------E 483
Cdd:cd19094 159 AGKIRHIGLSN-ETPWGVMKFLELAEQlglpRIVSIQNPYSLlnrnfeeglaeacHRENVGLLAYSPLAGGVLtgkyldG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 484 SWYPFGGR----GHTSESFNNE-------VIVELAEKYNKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENIDIFDFEL 550
Cdd:cd19094 238 AARPEGGRlnlfPGYMARYRSPqaleavaEYVKLARKHGLSPAQLALAWVRSRPFVTstIIGATTLEQLKENIDAFDVPL 317
|
..
gi 1167055252 551 SE 552
Cdd:cd19094 318 SD 319
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
314-475 |
2.26e-14 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 73.85 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 314 IIGLGT----WTQDDET--TEESVYSALKDGYRLIDTAQYYGN-ETGVGNGVRKAIDEgiVKREDVFVTTKVmpGNY--- 383
Cdd:cd19164 17 IFGAATfsyqYTTDPESipPVDIVRRALELGIRAFDTSPYYGPsEIILGRALKALRDE--FPRDTYFIITKV--GRYgpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 384 ------DRAYQSIDESLARLGFDYIDLMLVHQ-SGSGDEEVYKALCQGV---ADGKIRSIGISNY--YTADEVERVTDGA 451
Cdd:cd19164 93 dfdyspEWIRASVERSLRRLHTDYLDLVYLHDvEFVADEEVLEALKELFklkDEGKIRNVGISGYplPVLLRLAELARTT 172
|
170 180
....*....|....*....|....*
gi 1167055252 452 DIKPA-VIQNENHLYYQNTELQEYV 475
Cdd:cd19164 173 AGRPLdAVLSYCHYTLQNTTLLAYI 197
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
317-438 |
3.48e-14 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 73.38 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 317 LGTWTQDDETTEESVYS----ALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgivKREDVFVTTKV---M-PGNYDR 385
Cdd:cd19087 18 LGTMNFGGRTDEETSFAimdrALDAGINFFDTADVYGGgrsEEIIG----RWIAG---RRDDIVLATKVfgpMgDDPNDR 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167055252 386 ---AY---QSIDESLARLGFDYIDLMLVHQ--SGSGDEEVYKALCQGVADGKIRSIGISNY 438
Cdd:cd19087 91 glsRRhirRAVEASLRRLQTDYIDLYQMHHfdRDTPLEETLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
307-544 |
4.36e-14 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 73.06 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTW-----TQDDETTEESVYSALKDGYRLIDTAQYYGNETG-----VGNGVRkaiDEGIVKREDVFVTT 376
Cdd:cd19089 6 RSGLHLPAISLGLWhnfgdYTSPEEARELLRTAFDLGITHFDLANNYGPPPGsaeenFGRILK---RDLRPYRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 377 KV---M-PGNY----DRAY--QSIDESLARLGFDYIDLMLVHQSgsgD-----EEVYKALCQGVADGKIRSIGISNYyTA 441
Cdd:cd19089 83 KAgygMwPGPYgdggSRKYllASLDQSLKRMGLDYVDIFYHHRY---DpdtplEETMTALADAVRSGKALYVGISNY-PG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 442 DEVER---VTDGADIKPAVIQNENHLYYQNTE--LQEYVKQYGTVIESW-----------YPFG----------GRGHTS 495
Cdd:cd19089 159 AKARRaiaLLRELGVPLIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFsplaqglltdkYLNGippdsrraaeSKFLTE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1167055252 496 ESFNNEV------IVELAEKYNKTSAQIILRWQVQAGYI--AIPGSSNPEHIAENID 544
Cdd:cd19089 239 EALTPEKleqlrkLNKIAAKRGQSLAQLALSWVLRDPRVtsVLIGASSPSQLEDNVA 295
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
314-544 |
5.42e-14 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 72.97 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 314 IIGLGTWTQDDETTEESVYSALKD-----GYRLIDTAQYYGN---ETGVGngvrkaidEGIVKREDVFVTTKVMPG---- 381
Cdd:cd19075 4 ILGTMTFGSQGRFTTAEAAAELLDaflerGHTEIDTARVYPDgtsEELLG--------ELGLGERGFKIDTKANPGvggg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 382 -NYDRAYQSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNyYTADEVERVTDGAD----IK 454
Cdd:cd19075 76 lSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTplEETLAAIDELYKEGKFKEFGLSN-YSAWEVAEIVEICKengwVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 455 PAViqnenhlyYQ---N-------TELQEYVKQYGTVIESWYP-----FGGRGHTSES------FNN------------- 500
Cdd:cd19075 155 PTV--------YQgmyNaitrqveTELFPCLRKLGIRFYAYSPlaggfLTGKYKYSEDkagggrFDPnnalgklyrdryw 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1167055252 501 --------EVIVELAEKYNKTSAQIILRW-------QVQAGYIAIPGSSNPEHIAENID 544
Cdd:cd19075 227 kpsyfealEKVEEAAEKEGISLAEAALRWlyhhsalDGEKGDGVILGASSLEQLEENLA 285
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
315-543 |
1.10e-13 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 71.82 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 315 IGLGTWTQDDETTEESVYSALkDGY-----RLIDTAQYYGNETGVGnGVRKAIDEGI---VKREDVFVTTK--------V 378
Cdd:cd19082 3 IVLGTADFGTRIDEEEAFALL-DAFvelggNFIDTARVYGDWVERG-ASERVIGEWLksrGNRDKVVIATKgghpdledM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 MPGNYDRAY--QSIDESLARLGFDYIDLMLVHQsgsgD------EEVYKALCQGVADGKIRSIGISNYYTadevERVTDG 450
Cdd:cd19082 81 SRSRLSPEDirADLEESLERLGTDYIDLYFLHR----DdpsvpvGEIVDTLNELVRAGKIRAFGASNWST----ERIAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 451 ADI-----KPAVIQNENH---------------LYYQNTELQEYVKQYGTVIESWYP-----FGGRGHTSESFNNEV--- 502
Cdd:cd19082 153 NAYakahgLPGFAASSPQwslarpneppwpgptLVAMDEEMRAWHEENQLPVFAYSSqargfFSKRAAGGAEDDSELrrv 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1167055252 503 ------------IVELAEKYNKTSAQIILRWQVQAGY--IAIPGSSNPEHIAENI 543
Cdd:cd19082 233 yyseenferlerAKELAEEKGVSPTQIALAYVLNQPFptVPIIGPRTPEQLRDSL 287
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
324-436 |
1.22e-13 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 72.12 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 324 DETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKAIdegiVKREDVFVTTKVmpGNY--------DRAYQSIDE 392
Cdd:PLN02587 30 EEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALG----IPREKYVVSTKC--GRYgegfdfsaERVTKSVDE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1167055252 393 SLARLGFDYIDLMLVH--QSGSGDE---EVYKALCQGVADGKIRSIGIS 436
Cdd:PLN02587 104 SLARLQLDYVDILHCHdiEFGSLDQivnETIPALQKLKESGKVRFIGIT 152
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
308-558 |
2.01e-12 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 68.86 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGTW-----TQDDETTEESVYSALKDGYRLIDTAQYYGNETGVG--NGVRKAIDEGIVKREDVFVTTK--- 377
Cdd:PRK09912 21 SGLRLPALSLGLWhnfghVNALESQRAILRKAFDLGITHFDLANNYGPPPGSAeeNFGRLLREDFAAYRDELIISTKagy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 378 -VMPGNY----DRAY--QSIDESLARLGFDYIDLMLVHQ--SGSGDEEVYKALCQGVADGKIRSIGISNYYTadevERVT 448
Cdd:PRK09912 101 dMWPGPYgsggSRKYllASLDQSLKRMGLEYVDIFYSHRvdENTPMEETASALAHAVQSGKALYVGISSYSP----ERTQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 449 DGADIK-----PAVIQNENH----LYYQNTELQEYVKQYGTVIESWYPF---------------GGRGH----------- 493
Cdd:PRK09912 177 KMVELLrewkiPLLIHQPSYnllnRWVDKSGLLDTLQNNGVGCIAFTPLaqglltgkylngipqDSRMHregnkvrgltp 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167055252 494 ---TSESFNN-EVIVELAEKYNKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENIDIF-DFELSESEMQSM 558
Cdd:PRK09912 257 kmlTEANLNSlRLLNEMAQQRGQSMAQMALSWLLKDERVTsvLIGASRAEQLEENVQALnNLTFSTEELAQI 328
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
318-460 |
2.99e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 67.68 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 318 GTW-TQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEgivKREDVFVTTKVMPGN------YDRAY 387
Cdd:cd19104 24 GLMgRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLG----RALKG---LPAGPYITTKVRLDPddlgdiGGQIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 388 QSIDESLARLGFDYIDLMLVH-QSGSGDEEVYKAL--------CQGVAD--------GKIRSIGISNYYTADEVERVTDG 450
Cdd:cd19104 97 RSVEKSLKRLKRDSVDLLQLHnRIGDERDKPVGGTlsttdvlgLGGVADaferlrseGKIRFIGITGLGNPPAIRELLDS 176
|
170
....*....|
gi 1167055252 451 AdiKPAVIQN 460
Cdd:cd19104 177 G--KFDAVQV 184
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
308-555 |
5.07e-12 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 67.09 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGTWTQ--DD---ETTEESVYSALKDGYRLIDTAQYYG-----NETGVGNGVRKAIDEgivKREDVFVTTK 377
Cdd:cd19150 8 SGLKLPALSLGLWHNfgDDtplETQRAILRTAFDLGITHFDLANNYGpppgsAEENFGRILREDFAG---YRDELIISTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 378 ----VMPGNY----DRAY--QSIDESLARLGFDYIDLMLVHQ--SGSGDEEVYKALCQGVADGKIRSIGISNYYTadevE 445
Cdd:cd19150 85 agydMWPGPYgewgSRKYllASLDQSLKRMGLDYVDIFYSHRfdPDTPLEETMGALDHAVRSGKALYVGISSYSP----E 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 446 RVTDGADI-----KPAVIQNENH----LYYQNTELQEYVKQYGT-----------VIESWY----PFGGRGHTSESFNNE 501
Cdd:cd19150 161 RTREAAAIlrelgTPLLIHQPSYnmlnRWVEESGLLDTLQELGVgciaftplaqgLLTDKYlngiPEGSRASKERSLSPK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1167055252 502 VIVE-----------LAEKYNKTSAQIILRWQVQAGYI--AIPGSSNPEHIAENIDIFD-FELSESEM 555
Cdd:cd19150 241 MLTEanlnsiralneIAQKRGQSLAQMALAWVLRDGRVtsALIGASRPEQLEENVGALDnLTFSADEL 308
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
338-560 |
7.27e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 66.46 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 338 GYRLIDTAQYYGN-ETGVGNGVRKAIDEGIVkREDVFVTTKVMP----GNYDRAY--QSIDESLARLGFDYIDLMLVHQS 410
Cdd:cd19101 36 GLTTFDCADIYGPaEELIGEFRKRLRRERDA-ADDVQIHTKWVPdpgeLTMTRAYveAAIDRSLKRLGVDRLDLVQFHWW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 411 GSGDE---EVYKALCQGVADGKIRSIGISNYYTAdEVERVTDgADIKPAVIQNENHLYYQNTE--LQEYVKQ-------Y 478
Cdd:cd19101 115 DYSDPgylDAAKHLAELQEEGKIRHLGLTNFDTE-RLREILD-AGVPIVSNQVQYSLLDRRPEngMAALCEDhgikllaY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 479 GTVI-----ESW--------YPFGGRGHTS----------ESFNNEVIVEL---AEKYNKTSAQIILRWQVQ----AGyi 528
Cdd:cd19101 193 GTLAggllsEKYlgvpeptgPALETRSLQKyklmidewggWDLFQELLRTLkaiADKHGVSIANVAVRWVLDqpgvAG-- 270
|
250 260 270
....*....|....*....|....*....|..
gi 1167055252 529 AIPGSSNPEHIAENIDIFDFELSESEMQSMTS 560
Cdd:cd19101 271 VIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| FldA |
COG0716 |
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
60-219 |
1.03e-11 |
|
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 62.61 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 60 IVVYYSWSENTKSIAKRIAETIGAdiyeirtvkaypkDGYETLDIAQEerrtgnlpeivdDLPDLKEYSTVIIGGPIWNA 139
Cdd:COG0716 2 LIVYGSTTGNTEKVAEAIAEALGA-------------AGVDLFEIEDA------------DLDDLEDYDLLILGTPTWAG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 140 YVSTPLARYLE--LTDLSEKTVIPFSTSQGSGQSSYLKDFQERV--RTAERIGEYkdiqfpANYSSDTFSDEEIDEMLAP 215
Cdd:COG0716 57 ELPDDWEDFLEelKEDLSGKKVALFGTGDSSGYGDALGELKELLeeKGAKVVGGY------DFEGSKAPDAEDTEERAEE 130
|
....
gi 1167055252 216 WIES 219
Cdd:COG0716 131 WLKQ 134
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
307-555 |
1.74e-10 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 62.42 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTW-----TQDDETTEESVYSALKDGYRLIDTAQYYG-----NETGVGNGVRKAIDEgivKREDVFVTT 376
Cdd:cd19151 7 RSGLKLPAISLGLWhnfgdVDRYENSRAMLRRAFDLGITHFDLANNYGpppgsAEENFGRILKEDLKP---YRDELIIST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 377 K----VMPGNY----DRAY--QSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNYytadEV 444
Cdd:cd19151 84 KagytMWPGPYgdwgSKKYliASLDQSLKRMGLDYVDIFYHHRPDPETplEETMGALDQIVRQGKALYVGISNY----PP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 445 ERVTDGADI-----KPAVIQNENHLYYQNT---ELQEYVKQYGTVIESWYPFGG---------------RGHTSESFNN- 500
Cdd:cd19151 160 EEAREAAAIlkdlgTPCLIHQPKYSMFNRWveeGLLDVLEEEGIGCIAFSPLAQglltdrylngipedsRAAKGSSFLKp 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1167055252 501 -----EVIV------ELAEKYNKTSAQIILRWQVQAGYI--AIPGSSNPEHIAENIDIFD-FELSESEM 555
Cdd:cd19151 240 eqiteEKLAkvrrlnEIAQARGQKLAQMALAWVLRNKRVtsVLIGASKPSQIEDAVGALDnREFSEEEL 308
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
308-543 |
2.04e-10 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 62.08 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGTWTQ-----DDETTEESVYSALKDGYRLIDTAQYY---GNETGVGNGVRKAidegIVKREDVFVTTKVM 379
Cdd:cd19141 8 SGLRVSCLGLGTWVTfgsqiSDEVAEELVTLAYENGINLFDTAEVYaagKAEIVLGKILKKK----GWRRSSYVITTKIF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 380 PG-------NYDRAY--QSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNYYTADEVERVT 448
Cdd:cd19141 84 WGgkaeterGLSRKHiiEGLKASLERLQLEYVDIVFANRPDPNTpmEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 449 DGAD---IKPAVIQNENHLYYQ---NTELQEYVKQYGTVIESWYPFGGrGHTSESFNNEV-------------------- 502
Cdd:cd19141 164 VARQfnlIPPIVEQAEYHLFQRekvEMQLPELFHKIGVGAMTWSPLAC-GILSGKYDDGVpeysraslkgyqwlkekils 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1167055252 503 ------------IVELAEKYNKTSAQIILRW--QVQAGYIAIPGSSNPEHIAENI 543
Cdd:cd19141 243 eegrrqqaklkeLQIIADRLGCTLPQLAIAWclKNEGVSSVLLGASSTEQLYENL 297
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
309-555 |
3.62e-10 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 61.29 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 309 GYEMPIIGLG-----TWTQDDETTEES---VYSALKDGYRLIDTAQYYG---NETGVGngvrKAIDEGIvkREDVFVTTK 377
Cdd:cd19145 9 GLEVSAQGLGcmglsGDYGAPKPEEEGialIHHAFNSGVTFLDTSDIYGpntNEVLLG----KALKDGP--REKVQLATK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 378 V---------MPGNYDRAY--QSIDESLARLGFDYIDLMLVHQSGSG--DEEVYKALCQGVADGKIRSIGISNyYTADEV 444
Cdd:cd19145 83 FgiheiggsgVEVRGDPAYvrAACEASLKRLDVDYIDLYYQHRIDTTvpIEITMGELKKLVEEGKIKYIGLSE-ASADTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 445 ERvtdGADIKP-AVIQNENHLYYQNTElQEYV---KQYGTVIESWYPFG-----GRGHTSESFN---------------- 499
Cdd:cd19145 162 RR---AHAVHPiTAVQLEWSLWTRDIE-EEIIptcRELGIGIVPYSPLGrgffaGKAKLEELLEnsdvrkshprfqgenl 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167055252 500 --NEVIVE----LAEKYNKTSAQIILRWQVQAG--YIAIPGSSNPEHIAENIDIFDFELSESEM 555
Cdd:cd19145 238 ekNKVLYErveaLAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNIGALSVKLTKEDL 301
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
307-542 |
3.84e-10 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 61.46 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 307 NSGYEMPIIGLGTW-----TQDDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGngvrKAIDEGIVKREDVFVTTKV 378
Cdd:cd19143 8 RSGLKVSALSFGSWvtfgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMG----QAIKELGWPRSDYVVSTKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 M-----PGNYDRA------YQSIDESLARLGFDYIDLMLVHQSgsgD-----EEVYKALCQGVADGKIRSIGISNyYTAD 442
Cdd:cd19143 84 FwggggPPPNDRGlsrkhiVEGTKASLKRLQLDYVDLVFCHRP---DpatpiEETVRAMNDLIDQGKAFYWGTSE-WSAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 443 EVERVTDGAD----IKPAVIQNENHLYYQNTELQEYVKQY-----GTVIesWYPF---------------GGRGHTSESF 498
Cdd:cd19143 160 QIEEAHEIADrlglIPPVMEQPQYNLFHRERVEVEYAPLYekyglGTTT--WSPLasglltgkynngipeGSRLALPGYE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167055252 499 ------------NNEVIVEL---AEKYNKTSAQIILRWQVQAGYI--AIPGSSNPEHIAEN 542
Cdd:cd19143 238 wlkdrkeelgqeKIEKVRKLkpiAEELGCSLAQLAIAWCLKNPNVstVITGATKVEQLEEN 298
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
308-488 |
4.30e-10 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 61.15 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGTWTQ-----DDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaidEGIvKREDVFVTTKVM 379
Cdd:cd19160 11 SGLRVSCLGLGTWVTfgsqiSDETAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKS---KGW-RRSSYVVTTKIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 380 PGNYDRAYQSIDE---------SLARLGFDYIDLMLVHQS--GSGDEEVYKALCQGVADGKIRSIGISNYYTADEVERVT 448
Cdd:cd19160 87 WGGQAETERGLSRkhiieglrgSLDRLQLEYVDIVFANRSdpNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1167055252 449 DGAD---IKPAVIQNENHLYYQN---TELQEYVKQYGTVIESWYPF 488
Cdd:cd19160 167 VARQfnlIPPVCEQAEYHLFQREkveMQLPELYHKIGVGSVTWSPL 212
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
313-436 |
4.48e-10 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 60.84 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 313 PIIGLGTWTQ-------DDETTEeSVYSALKDGYRLIDTAQYYG---NETGVGNGVRKAidegivKREDVFVTTKV---- 378
Cdd:cd19162 1 PRLGLGAASLgnlaragEDEAAA-TLDAAWDAGIRYFDTAPLYGlglSERRLGAALARH------PRAEYVVSTKVgrll 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 379 MPGN--------------YDRAYQSIDESLARLGFDYIDLMLVHQSGSGDE----EVYKALCQGVADGKIRSIGIS 436
Cdd:cd19162 74 EPGAagrpagadrrfdfsADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLqaltDAFPALEELRAEGVVGAIGVG 149
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
308-543 |
1.54e-09 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 59.67 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGTWTQ-----DDETTEESVYSALKDGYRLIDTAQYYG---NETGVGNGVRKAidegIVKREDVFVTTKVM 379
Cdd:cd19159 9 SGLRVSCLGLGTWVTfggqiSDEVAERLMTIAYESGVNLFDTAEVYAagkAEVILGSIIKKK----GWRRSSLVITTKLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 380 PG---------NYDRAYQSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNyYTADEVERVT 448
Cdd:cd19159 85 WGgkaeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTpmEEIVRAMTHVINQGMAMYWGTSR-WSAMEIMEAY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 449 DGAD----IKPAVIQNENHLYYQ---NTELQEYVKQYGTVIESWYPFGGrGHTSESFNNEV------------------- 502
Cdd:cd19159 164 SVARqfnmIPPVCEQAEYHLFQRekvEVQLPELYHKIGVGAMTWSPLAC-GIISGKYGNGVpessraslkcyqwlkeriv 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1167055252 503 -------------IVELAEKYNKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENI 543
Cdd:cd19159 243 seegrkqqnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSsvLLGSSTPEQLIENL 298
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
325-558 |
2.68e-09 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 58.88 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 325 ETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaidegiVKREDVFVTTKV----------------------- 378
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE------KPRDEFVLSTKVgrllkparegsvpdpngfvdplp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 MPGNYDRAYQ----SIDESLARLGFDYIDLMLVHQSGS---GDEEV-----------YKALCQGVADGKIRSIGISnyyt 440
Cdd:cd19161 94 FEIVYDYSYDgimrSFEDSLQRLGLNRIDILYVHDIGVythGDRKErhhfaqlmsggFKALEELKKAGVIKAFGLG---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 441 ADEVE---RVTDGADIKPAVIQNENHLYYQNT--ELQEYVKQYGTVIESWYPFGG-----RGHTSESFN----------- 499
Cdd:cd19161 170 VNEVQiclEALDEADLDCFLLAGRYSLLDQSAeeEFLPRCEQRGTSLVIGGVFNSgilatGTKSGAKFNygdapaeiisr 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167055252 500 NEVIVELAEKYNKTSAQIILRWQVQAGYIA--IPGSSNPEHIAENIDIFDFELSESEMQSM 558
Cdd:cd19161 250 VMEIEKICDAYNVPLAAAALQFPLRHPAVAsvLTGARNPAQLRQNVEAFQTDIPEELWQAL 310
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
308-430 |
5.83e-09 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 57.86 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 308 SGYEMPIIGLGTWTQ-----DDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKaideGIVKREDVFVTTKVM 379
Cdd:cd19142 9 SGLRVSNVGLGTWSTfstaiSEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKK----KGWKRSSYIVSTKIY 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1167055252 380 --PGNYDRAY------QSIDESLARLGFDYIDLMLVHQSGS--GDEEVYKALCQGVADGKI 430
Cdd:cd19142 85 wsYGSEERGLsrkhiiESVRASLRRLQLDYIDIVIIHKADPmcPMEEVVRAMSYLIDNGLI 145
|
|
| Flavodoxin_4 |
pfam12682 |
Flavodoxin; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that ... |
59-164 |
7.37e-09 |
|
Flavodoxin; This is a family of flavodoxins. Flavodoxins are electron transfer proteins that carry a molecule of non-covalently bound FMN.
Pssm-ID: 403777 Cd Length: 155 Bit Score: 55.09 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 59 MIVVYYSWSENTKSIAKRIAETIGADIYEIRTVKAYPKDGYETLD----IAQEERRTGNLPEIVDDLPDLKEYSTVIIGG 134
Cdd:pfam12682 2 ILVAYFSCSGVTKAVAEKLAAITGADLYEIKPEVPYTEADLDWNDkksrSSVE*RDALSRPAISGTLFHPEKYEVLFVGF 81
|
90 100 110
....*....|....*....|....*....|
gi 1167055252 135 PIWNAYVSTPLARYLELTDLSEKTVIPFST 164
Cdd:pfam12682 82 PVWWYIAPTIINTFLESYDFAGKIVVPFAT 111
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
313-435 |
2.41e-07 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 52.61 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 313 PIIGLGT------WTQ-DDETTEESVYSALKDGYRLIDTAQYYGN---ETGVGNGVRKAidegivKREDVFVTTKV---- 378
Cdd:cd19152 1 PKLGFGTaplgnlYEAvSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 379 ---------------MPGNYDRAY--------QSIDESLARLGFDYIDLMLVHQ-----SGSGDEEV--------YKALC 422
Cdd:cd19152 75 vplqeveptfepgfwNPLPFDAVFdysydgilRSIEDSLQRLGLSRIDLLSIHDpdedlAGAESDEHfaqaikgaFRALE 154
|
170
....*....|...
gi 1167055252 423 QGVADGKIRSIGI 435
Cdd:cd19152 155 ELREEGVIKAIGL 167
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
305-489 |
2.07e-06 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 50.08 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 305 LLNSGYEMPIIGLGTWTQ-----DDETTEESVYSALKDGYRLIDTAQYYG---NETGVGNGVRKaidEGIvKREDVFVTT 376
Cdd:cd19158 6 LGKSGLRVSCLGLGTWVTfggqiTDEMAEHLMTLAYDNGINLFDTAEVYAagkAEVVLGNIIKK---KGW-RRSSLVITT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 377 KVMPG---------NYDRAYQSIDESLARLGFDYIDLMLVHQSGSGD--EEVYKALCQGVADGKIRSIGISNYYTADEVE 445
Cdd:cd19158 82 KIFWGgkaeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTpmEETVRAMTHVINQGMAMYWGTSRWSSMEIME 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1167055252 446 RVTDGAD---IKPAVIQNENHLYYQ---NTELQEYVKQYGTVIESWYPFG 489
Cdd:cd19158 162 AYSVARQfnlIPPICEQAEYHMFQRekvEVQLPELFHKIGVGAMTWSPLA 211
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
342-555 |
7.07e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 44.96 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 342 IDTAQYYGneTGVGNG-VRKAIDEGivkREDVFVTTKV-----MPGNYDRAY------QSIDESLARLGFDYID-----L 404
Cdd:PRK10376 57 IDTSDFYG--PHVTNQlIREALHPY---PDDLTIVTKVgarrgEDGSWLPAFspaelrRAVHDNLRNLGLDVLDvvnlrL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 405 ML-VHQSGSGD-EEVYKALCQGVADGKIRSIGISNYyTAdevERVTDGADIKPAV-IQNE-NHLYYQNTELQEYVKQYGT 480
Cdd:PRK10376 132 MGdGHGPAEGSiEEPLTVLAELQRQGLVRHIGLSNV-TP---TQVAEARKIAEIVcVQNHyNLAHRADDALIDALARDGI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 481 VIESWYPFGGrghtsesFN---NEVIVELAEKYNKTSAQIILRWQVQ--AGYIAIPGSSNPEHIAENIDIFDFELSESEM 555
Cdd:PRK10376 208 AYVPFFPLGG-------FTplqSSTLSDVAASLGATPMQVALAWLLQrsPNILLIPGTSSVAHLRENLAAAELVLSEEVL 280
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
325-556 |
1.07e-04 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 44.72 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 325 ETTEESVYSAL----KDGYRLIDTAQYY---GNETGVGNGVRKAIDegivkREDVFVTTKVMPGnYDRA--------YQ- 388
Cdd:cd19146 31 ECDKETAFKLLdafyEQGGNFIDTANNYqgeESERWVGEWMASRGN-----RDEMVLATKYTTG-YRRGgpikiksnYQg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 389 --------SIDESLARLGFDYIDLMLVH--QSGSGDEEVYKALCQGVADGKIRSIGIS----------NYYTADEVERvt 448
Cdd:cd19146 105 nhakslrlSVEASLKKLQTSYIDILYVHwwDYTTSIPELMQSLNHLVAAGKVLYLGVSdtpawvvskaNAYARAHGLT-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 449 dgadikPAVI-QNENHLYYQNTElQEYVKQYGTVIESWYPFG--GRGH--TSESFNN-------------------EVIV 504
Cdd:cd19146 183 ------QFVVyQGHWSAAFRDFE-RDILPMCEAEGMALAPWGvlGQGQfrTEEEFKRrgrsgrkggpqtekerkvsEKLE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1167055252 505 ELAEKYNKTSAQIILRWQVQ-AGYI-AIPGSSNPEHIAENIDIFDFELSESEMQ 556
Cdd:cd19146 256 KVAEEKGTAITSVALAYVMHkAPYVfPIVGGRKVEHLKGNIEALGISLSDEEIQ 309
|
|
| WrbA |
COG0655 |
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ... |
60-150 |
1.44e-04 |
|
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion];
Pssm-ID: 440420 [Multi-domain] Cd Length: 181 Bit Score: 42.99 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167055252 60 IVVYYSWSE--NTKSIAKRIAETIGADIYEIRTVKAYpkdgyeTLDIAQEERRTGNLPEIVDD-----LPDLKEYSTVII 132
Cdd:COG0655 3 LVINGSPRKngNTAALAEAVAEGAEEAGAEVELIRLA------DLDIKPCIGCGGTGKCVIKDdmnaiYEKLLEADGIIF 76
|
90
....*....|....*...
gi 1167055252 133 GGPIWNAYVSTPLARYLE 150
Cdd:COG0655 77 GSPTYFGNMSAQLKAFID 94
|
|
| PRK06242 |
PRK06242 |
flavodoxin; Provisional |
60-100 |
2.31e-03 |
|
flavodoxin; Provisional
Pssm-ID: 180484 [Multi-domain] Cd Length: 150 Bit Score: 38.74 E-value: 2.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1167055252 60 IVVYYSWSE-NTKSIAKRIAETIGADIYEIRTVKAYPKDGYE 100
Cdd:PRK06242 4 LIVYASVHHgNTEKIAKAIAEVLDAEVIDPGDVNPEDLSEYD 45
|
|
| |
