|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
39-331 |
1.46e-168 |
|
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: 472.54 E-value: 1.46e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLSSGHEMPVLGFGTYKLRGYQ-CSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWN 117
Cdd:cd19116 1 PTIKLNDGNEIPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 118 THHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEIlmpmSGDELQTVEIDYLDTWRAMENLVKLGMVRSIGLS 197
Cdd:cd19116 81 SYHEREQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDSE----SNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 NFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHC--PVYFFSEGMKRLVKKYKR 275
Cdd:cd19116 157 NFNSEQINRLLSNCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTnpPPRLDDPTLVAIAKKYGK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 281366738 276 SASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRIV 331
Cdd:cd19116 237 TTAQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
49-321 |
1.79e-117 |
|
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: 341.38 E-value: 1.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 49 MPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTHHDPRDVRRI 128
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEA----IRESGVPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 129 CEKQLELLGFSYIDLYLMHFPVGYKYVCDEIlmpmsgdelqtveiDYLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRII 208
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEGGSKE--------------ARLETWRALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 209 QCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKN-HCPVyffsegMKRLVKKYKRSASQIVLRYLID 287
Cdd:cd19071 143 AAARIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRPLlDDPV------LKEIAKKYGKTPAQVLLRWALQ 216
|
250 260 270
....*....|....*....|....*....|....
gi 281366738 288 YGVVPIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19071 217 RGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
45-330 |
2.27e-114 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 333.56 E-value: 2.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 45 SGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTHHDPRD 124
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEA----IAASGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 125 VRRICEKQLELLGFSYIDLYLMHFPVGYKYVcdeilmpmsgdelqtveidylDTWRAMENLVKLGMVRSIGLSNFNMEQI 204
Cdd:COG0656 77 TLAAFEESLERLGLDYLDLYLIHWPGPGPYV---------------------ETWRALEELYEEGLIRAIGVSNFDPEHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 205 QRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHcPVyffsegMKRLVKKYKRSASQIVLRY 284
Cdd:COG0656 136 EELLAETGVKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGKLLDD-PV------LAEIAEKHGKTPAQVVLRW 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 281366738 285 LIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRI 330
Cdd:COG0656 209 HLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
38-329 |
1.12e-105 |
|
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: 313.19 E-value: 1.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 38 APKVRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWN 117
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 118 THHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMpMSGDELQTVEIDYLDTWRAMENLVKLGMVRSIGLS 197
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGT-MENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 NFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVYFFSEG--------MKRL 269
Cdd:cd19154 160 NFNNDQIQRILDNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTGVSPApnllqdpiVKAI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 270 VKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSR 329
Cdd:cd19154 240 AEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLR 299
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
43-331 |
1.17e-101 |
|
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: 303.15 E-value: 1.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 43 LSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGN-ISRENIFLTTKLWNTHHD 121
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPGKaVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 PRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDeiLMPMSGD-ELQTVEIDYLDTWRAMENLVKLGMVRSIGLSNFN 200
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDN--PFPKNPDgTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 201 MEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNR---KNHCPVYFFSEGMKRLVKKYKRSA 277
Cdd:cd19106 159 SRQIDDILSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRpwaKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 281366738 278 SQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRIV 331
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
46-344 |
6.69e-90 |
|
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: 273.14 E-value: 6.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDPRDV 125
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 126 RRICEKQLELLGFSYIDLYLMHFPVGYKyvCDEILMPMSGD-ELQTVEIDYLDTWRAMENLVKLGMVRSIGLSNFNMEQI 204
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFK--PGKELFPLDESgNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 205 QRIIQCS--SSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNR---KNHCPVYFFSEGMKRLVKKYKRSASQ 279
Cdd:cd19107 159 ERILNKPglKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRpwaKPEDPSLLEDPKIKEIAAKHNKTTAQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281366738 280 IVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRIVKYEIVKDHMFYPF 344
Cdd:cd19107 239 VLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPF 303
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
41-317 |
1.47e-89 |
|
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: 271.98 E-value: 1.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHH 120
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 DPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKyvcDEILMPMSGDELQTV-EIDYLDTWRAMENLVKLGMVRSIGLSNF 199
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPVALK---KGVGFPESGEDLLSLsPIPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 200 NMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRknhcPVYFFSEGMKRLV--------- 270
Cdd:cd19123 161 SVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDR----PAAMKAEGEPVLLedpvinkia 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 281366738 271 KKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19123 237 EKHGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASD 283
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
43-331 |
2.67e-88 |
|
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: 268.44 E-value: 2.67e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 43 LSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDP 122
Cdd:cd19125 5 LNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 123 RDVRRICEKQLELLGFSYIDLYLMHFPVGYKyvcDEILMPMSGDELQTveiDYLDTWRAMENLVKLGMVRSIGLSNFNME 202
Cdd:cd19125 85 EDVPPALEKTLKDLQLDYLDLYLIHWPVRLK---KGAHMPEPEEVLPP---DIPSTWKAMEKLVDSGKVRAIGVSNFSVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 203 QIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVYFFSEGMKRLVKKYKRSASQIVL 282
Cdd:cd19125 159 KLEDLLAVARVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKNVLKDPIVTKVAEKLGKTPAQVAL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 281366738 283 RYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRIV 331
Cdd:cd19125 239 RWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFSSIEQQRRVL 287
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
41-330 |
1.42e-87 |
|
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: 267.08 E-value: 1.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHH 120
Cdd:cd19155 4 VTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 DPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDE-ILMPMSGDELQTVEIDYLDTWRAMENLVKLGMVRSIGLSNF 199
Cdd:cd19155 84 RREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDsGKLDPTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 200 NMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVYFFSEG----------MKRL 269
Cdd:cd19155 164 NREQMARILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGTGSPSGsspdllqdpvVKAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366738 270 VKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRI 330
Cdd:cd19155 244 AERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
39-324 |
8.86e-87 |
|
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: 264.86 E-value: 8.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLSSGHEMPVLGFGTYKLRGY---QCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKL 115
Cdd:cd19108 1 QRVKLNDGHFIPVLGFGTYAPEEVpksKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 116 WNTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKyvcdeilmpmSGDELQTVE---------IDYLDTWRAMENLV 186
Cdd:cd19108 81 WCTFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALK----------PGEELFPKDengklifdtVDLCATWEAMEKCK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 187 KLGMVRSIGLSNFNMEQIQRIIQCS--SSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKN----HCPVY 260
Cdd:cd19108 151 DAGLAKSIGVSNFNRRQLEMILNKPglKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEwvdqNSPVL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281366738 261 FFSEGMKRLVKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19108 231 LEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGL 294
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
46-325 |
1.69e-86 |
|
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: 263.59 E-value: 1.69e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDPRDV 125
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 126 RRICEKQLELLGFSYIDLYLMHFPVGYKYVCDeilmpmsGDELQTVEIDYLDTWRAMENLVKLGMVRSIGLSNFNMEQIQ 205
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKKD-------KGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 206 RIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHC-----PVYFFSEGMKRLVKKYKRSASQI 280
Cdd:cd19111 154 KILAYAKVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSlwpdqPDLLEDPTVLAIAKELDKTPAQV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281366738 281 VLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIK 325
Cdd:cd19111 234 LLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLD 278
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
48-346 |
8.49e-85 |
|
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: 259.89 E-value: 8.49e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 48 EMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDPRDVRR 127
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 128 ICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMPMSGDELQTvEIDYLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRI 207
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPS-DTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 208 IQCSS--SKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHC---PVyffsegMKRLVKKYKRSASQIVL 282
Cdd:cd19110 162 LNKPGlrVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVDLiddPV------IQRIAKKHGKSPAQILI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281366738 283 RYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRIVKYEIVKDHMFYPFEL 346
Cdd:cd19110 236 RFQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHI 299
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
49-317 |
9.61e-84 |
|
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: 254.89 E-value: 9.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 49 MPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQikmgNISRENIFLTTKLWNTHHDPRDVRRI 128
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAES----GVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 129 CEKQLELLGFSYIDLYLMHFPVgykyvcdeilmpmsgdelQTVEIDylDTWRAMENLVKLGMVRSIGLSNFNMEQIQRII 208
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN------------------PTVPLE--ETLGALKELKEAGKVKSIGVSNFTIELLEEAL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 209 QCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVyffsegmKRLVKKYKRSASQIVLRYLIDY 288
Cdd:cd19073 137 DISPLPIAVNQVEFHPFLYQAELLEYCRENDIVITAYSPLARGEVLRDPVI-------QEIAEKYDKTPAQVALRWLVQK 209
|
250 260
....*....|....*....|....*....
gi 281366738 289 GVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19073 210 GIVVIPKASSEDHLKENLAIFDWELTSED 238
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
49-324 |
1.26e-83 |
|
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: 255.63 E-value: 1.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 49 MPVLGFGTYKLRGYQ-CSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDPRDVRR 127
Cdd:cd19136 1 MPILGLGTFRLRGEEeVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 128 ICEKQLELLGFSYIDLYLMHFPVGYKyvcdeilmpMSGDELQTVEIDyLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRI 207
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQG---------LKPSDPRNAELR-RESWRALEDLYKEGKLRAIGVSNYTVRHLEEL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 208 IQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNrknhcPVYFFSEGMKRLVKKYKRSASQIVLRYLID 287
Cdd:cd19136 151 LKYCEVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGD-----LRLLEDPTVLAIAKKYGRTPAQVLLRWALQ 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 281366738 288 YGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19136 226 QGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
37-324 |
1.66e-82 |
|
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: 252.63 E-value: 1.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 37 MAPKVRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLW 116
Cdd:cd19135 1 GTPTVRLSNGVEMPILGLGTSHSGGYSHEAVVYALKECGYRHIDTAKRYGCEELLGKA----IKESGVPREDLFLTTKLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 117 NTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGykyvcdeilmPMSGDELQTVEidyLDTWRAMENLVKLGMVRSIGL 196
Cdd:cd19135 77 PSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDC----------PSSGKNVKETR---AETWRALEELYDEGLCRAIGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 197 SNFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVyffsegmKRLVKKYKRS 276
Cdd:cd19135 144 SNFLIEHLEQLLEDCSVVPHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTV-------TELAKKYQKT 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 281366738 277 ASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19135 217 PAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
41-324 |
1.20e-81 |
|
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: 250.18 E-value: 1.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTYKLRGYQ-CSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTH 119
Cdd:cd19133 1 VTLNNGVEMPILGFGVFQIPDPEeCERAVLEAIKAGYRLIDTAAAYGNEEAVGRA----IKKSGIPREELFITTKLWIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 120 HDPRDVRRICEKQLELLGFSYIDLYLMHFPVGykyvcdeilmpmsgdelqtveiDYLDTWRAMENLVKLGMVRSIGLSNF 199
Cdd:cd19133 77 AGYEKAKKAFERSLKRLGLDYLDLYLIHQPFG----------------------DVYGAWRAMEELYKEGKIRAIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 200 NMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQpNRKNhcpvyFFSEG-MKRLVKKYKRSAS 278
Cdd:cd19133 135 YPDRLVDLILHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAE-GRNN-----LFENPvLTEIAEKYGKSVA 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 281366738 279 QIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19133 209 QVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
39-329 |
1.44e-81 |
|
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: 252.02 E-value: 1.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNT 118
Cdd:cd19112 1 STITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 119 HHDprDVRRICEKQLELLGFSYIDLYLMHFPVGYKYvcDEILMPMSG-DELQTVEID----YLDTWRAMENLVKLGMVRS 193
Cdd:cd19112 81 DHG--HVIEACKDSLKKLQLDYLDLYLVHFPVATKH--TGVGTTGSAlGEDGVLDIDvtisLETTWHAMEKLVSAGLVRS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 194 IGLSNFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHcpvYFFSEG------MK 267
Cdd:cd19112 157 IGISNYDIFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAE---WFGSVSplddpvLK 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366738 268 RLVKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSR 329
Cdd:cd19112 234 DLAKKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
46-344 |
1.71e-81 |
|
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: 251.64 E-value: 1.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYK-----LRGyQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHH 120
Cdd:cd19109 1 GNSIPIIGLGTYSepkttPKG-ACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 DPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKyvCDEILMPMsgDELQTV---EIDYLDTWRAMENLVKLGMVRSIGLS 197
Cdd:cd19109 80 PPELVRPTLERTLKVLQLDYVDLYIIEMPMAFK--PGDEIYPR--DENGKWlyhKTNLCATWEALEACKDAGLVKSIGVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 NFNMEQIQRIIQCS--SSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKN----HCPVYFFSEGMKRLVK 271
Cdd:cd19109 156 NFNRRQLELILNKPglKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIwvnvSSPPLLEDPLLNSIGK 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366738 272 KYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRIVKYEIVKDHMFYPF 344
Cdd:cd19109 236 KYNKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
41-324 |
6.41e-81 |
|
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: 248.44 E-value: 6.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTqikmGNISRENIFLTTKLWNTHH 120
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA----SGVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 DPRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilMPMSGDelqtveidYLDTWRAMENLVKLGMVRSIGLSNFN 200
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWP-----------VPAQDK--------YVETWKALIELKKEGRVKSIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 201 MEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQpNRKNHCPVyffsegMKRLVKKYKRSASQI 280
Cdd:cd19131 139 IEHLQRLIDETGVVPVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQ-GGLLSDPV------IGEIAEKHGKTPAQV 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 281366738 281 VLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19131 212 VIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
45-326 |
7.38e-81 |
|
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: 249.11 E-value: 7.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 45 SGHEMPVLGFGTYKLrgYQCS----AAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNI-SRENIFLTTKLWNTH 119
Cdd:cd19124 1 SGQTMPVIGMGTASD--PPSPedikAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVkSRDELFVTSKLWCSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 120 HDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYK------YVCDEILMPMsgdelqtveiDYLDTWRAMENLVKLGMVRS 193
Cdd:cd19124 79 AHPDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKpgkfsfPIEEEDFLPF----------DIKGVWEAMEECQRLGLTKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 194 IGLSNFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVYFFSEGMKRLVKKY 273
Cdd:cd19124 149 IGVSNFSCKKLQELLSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWGSNAVMESDVLKEIAAAK 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 281366738 274 KRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKP 326
Cdd:cd19124 229 GKTVAQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEIPQ 281
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
43-321 |
1.55e-80 |
|
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: 247.18 E-value: 1.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 43 LSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTqikmGNISRENIFLTTKLWNTHHDP 122
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRR----SGVPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 123 RDVRRICEKQLELLGFSYIDLYLMHFPVgykyvcdeilmPMSGDelqtveidYLDTWRAMENLVKLGMVRSIGLSNFNME 202
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWPN-----------PSRDL--------YVEAWQALIEAREEGLVRSIGVSNFLPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 203 QIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVyffsegMKRLVKKYKRSASQIVL 282
Cdd:cd19132 138 HLDRLIDETGVTPAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSGLLDEPV------IKAIAEKHGKTPAQVVL 211
|
250 260 270
....*....|....*....|....*....|....*....
gi 281366738 283 RYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19132 212 RWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
39-317 |
1.63e-78 |
|
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: 244.28 E-value: 1.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNT 118
Cdd:cd19113 1 PDIKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 119 HHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMPM-----SGDELQTVEIDYLDTWRAMENLVKLGMVRS 193
Cdd:cd19113 81 FHDPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVPIEEKYPPgfycgDGDNFVYEDVPILDTWKALEKLVDAGKIKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 194 IGLSNFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLG--------QPNRKNhCPVYFFSEG 265
Cdd:cd19113 161 IGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGpqsfvelnQGRALN-TPTLFEHDT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 281366738 266 MKRLVKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKED 291
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
43-315 |
1.79e-78 |
|
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: 243.09 E-value: 1.79e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 43 LSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKM-GNISRENIFLTTKLWNTHHD 121
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEePGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 PRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMPMSGDELQTVEID----YLDTWRAMENLVKLGMVRSIGLS 197
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLTAVPTNGGEVDLDlsvsLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 NFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGqpNRKNHCPVYFFSEGMKRLVKKYKRSA 277
Cdd:cd19118 161 NFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLG--NNLAGLPLLVQHPEVKAIAAKLGKTP 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 281366738 278 SQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDE 315
Cdd:cd19118 239 AQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVELSDDE 276
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
40-330 |
1.88e-78 |
|
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: 242.30 E-value: 1.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 40 KVRLSSGHEMPVLGFGTYKLR-GYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNT 118
Cdd:cd19157 1 TVTLNNGVKMPWLGLGVFKVEeGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKG----IKESGIPREELFITSKVWNA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 119 HHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVcdeilmpmsgdelqtveidylDTWRAMENLVKLGMVRSIGLSN 198
Cdd:cd19157 77 DQGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGKYK---------------------ETWKALEKLYKDGRVRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 199 FNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHcpvyffsEGMKRLVKKYKRSAS 278
Cdd:cd19157 136 FQVHHLEDLLADAEIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQLLDN-------PVLKEIAEKYNKSVA 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 281366738 279 QIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRI 330
Cdd:cd19157 209 QVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
37-317 |
3.64e-78 |
|
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: 243.10 E-value: 3.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 37 MAPKVRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLW 116
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 117 NTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMP----MSGDELQTVEIDYLDTWRAMENLVKLGMVR 192
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKYVDPAVRYPpgwfYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 193 SIGLSNFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLG--------QPNRKNHCPVyFFSE 264
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFGpqsfleldLPGAKDTPPL-FEHD 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 281366738 265 GMKRLVKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19115 240 VIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEE 292
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
46-317 |
2.41e-77 |
|
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: 2.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTHHDPRDV 125
Cdd:cd19140 5 GVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA----IAASGVPRDELFLTTKVWPDNYSPDDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 126 RRICEKQLELLGFSYIDLYLMHFPvgykyvcdEILMPMSgdelqtveidylDTWRAMENLVKLGMVRSIGLSNFNMEQIQ 205
Cdd:cd19140 81 LASVEESLRKLRTDYVDLLLLHWP--------NKDVPLA------------ETLGALNEAQEAGLARHIGVSNFTVALLR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 206 RIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHcPVyffsegMKRLVKKYKRSASQIVLRYL 285
Cdd:cd19140 141 EAVELSEAPLFTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLARGEVLKD-PV------LQEIGRKHGKTPAQVALRWL 213
|
250 260 270
....*....|....*....|....*....|...
gi 281366738 286 ID-YGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19140 214 LQqEGVAAIPKATNPERLEENLDIFDFTLSDEE 246
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
41-324 |
1.25e-74 |
|
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: 232.33 E-value: 1.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTYKLR-GYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQikmgNISRENIFLTTKLWNTH 119
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPdGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRES----GVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 120 HDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVcdeilmpmsgdelqtveidylDTWRAMENLVKLGMVRSIGLSNF 199
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWPGKDKFI---------------------DTWKALEKLYASGKVKAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 200 NMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNrknhcpvYFFSEGMKRLVKKYKRSASQ 279
Cdd:cd19126 136 QEHHLEELLAHADVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQGG-------LLSNPVLAAIGEKYGKSAAQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281366738 280 IVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19126 209 VVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
41-330 |
1.26e-74 |
|
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: 232.79 E-value: 1.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTYKLR-GYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQikmgNISRENIFLTTKLWNTH 119
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQdGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRES----GVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 120 HDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVcdeilmpmsgdelqtveidylDTWRAMENLVKLGMVRSIGLSNF 199
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFK---------------------DTWKAFEKLYKEKKVRAIGVSNF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 200 NMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPN-RKNHCpvyffsegMKRLVKKYKRSAS 278
Cdd:cd19156 136 HEHHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKlLSNPV--------LKAIGKKYGKSAA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 281366738 279 QIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRI 330
Cdd:cd19156 208 QVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
46-329 |
1.90e-73 |
|
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: 230.91 E-value: 1.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDPRDV 125
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 126 RRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMPMSGD--ELQTVEIDYL---DTWRAMENLVKLGMVRSIGLSNFN 200
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAENYPFLWKdkELKKFPLEQSpmqECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 201 MEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQ------PNRKNHCPVYFFSEGMKRLVKKYK 274
Cdd:cd19114 161 VQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNavytkvTKHLKHFTNLLEHPVVKKLADKHK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 281366738 275 RSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSR 329
Cdd:cd19114 241 RDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
46-317 |
3.84e-73 |
|
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: 229.04 E-value: 3.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGT-YKLRGYQ-------CSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWN 117
Cdd:cd19120 1 GSKIPAIAFGTgTAWYKSGdddiqrdLVDSVKLALKAGFRHIDTAEMYGNEKEVGEA----LKESGVPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 118 THHDPRDVrriCEKQLELLGFSYIDLYLMHFPvgykYVCDEilmpmSGDELQTVeidyldtWRAMENLVKLGMVRSIGLS 197
Cdd:cd19120 77 GIKDPREA---LRKSLAKLGVDYVDLYLIHSP----FFAKE-----GGPTLAEA-------WAELEALKDAGLVRSIGVS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 NFNMEQIQRIIQCSSSKPVVNQVEIWPGFL--QKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPvyfFSEGMKRLVKKYKR 275
Cdd:cd19120 138 NFRIEDLEELLDTAKIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRDAGGP---LDPVLEKIAEKYGV 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 281366738 276 SASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19120 215 TPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEE 256
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
44-329 |
1.63e-70 |
|
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: 223.10 E-value: 1.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 44 SSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDPR 123
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 124 DVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMPMSGDELQTVEIDYLDTWRAMENLVKLGMVRSIGLSNFNMEQ 203
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 204 IQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKN--HCPVyffsegMKRLVKKYKRSASQIV 281
Cdd:cd19129 161 LREIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGMEPKllEDPV------ITAIARRVNKTPAQVL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 281366738 282 LRYLIDYGVVPIPKAANPIHIKENLNIFDFKlDEADTRLLRGIKPKSR 329
Cdd:cd19129 235 LAWAIQRGTALLTTSKTPSRIRENFDISTLP-EDAMREINEGIKTRYR 281
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
42-324 |
2.30e-70 |
|
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: 222.02 E-value: 2.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 42 RLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGnISRENIFLTTKLWNTHHd 121
Cdd:cd19121 5 KLNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAIAGG-VKREDLFVTTKLWSTYH- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 pRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMPMSGDELQTVEIDY--LDTWRAMENLVKLGMVRSIGLSNF 199
Cdd:cd19121 83 -RRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPDGSRDLDWDWnhVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 200 NMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNrknhCPVyFFSEGMKRLVKKYKRSASQ 279
Cdd:cd19121 162 SIPYLEELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTG----SPL-ISDEPVVEIAKKHNVGPGT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281366738 280 IVLRYLIDYGVVPIPKAANPIHIKENLNIFDFklDEADTRLLRGI 324
Cdd:cd19121 237 VLISYQVARGAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKLNDI 279
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
39-317 |
3.05e-70 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 221.48 E-value: 3.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALrtqiKMGNISRENIFLTTKLWNT 118
Cdd:PRK11565 5 TVIKLQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKAL----KEASVAREELFITTKLWND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 119 HHDprDVRRICEKQLELLGFSYIDLYLMHFPVgykyvcdeilmPmsgdelqtvEID-YLDTWRAMENLVKLGMVRSIGLS 197
Cdd:PRK11565 81 DHK--RPREALEESLKKLQLDYVDLYLMHWPV-----------P---------AIDhYVEAWKGMIELQKEGLIKSIGVC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 NFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKnhcpvYFFSEGMKRLVKKYKRSA 277
Cdd:PRK11565 139 NFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKG-----VFDQKVIRDLADKYGKTP 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 281366738 278 SQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:PRK11565 214 AQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDE 253
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
42-315 |
1.14e-68 |
|
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: 217.75 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 42 RLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTHHd 121
Cdd:cd19117 7 KLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQG----IKDSGVPREEIFITTKLWCTWH- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 pRDVRRICEKQLELLGFSYIDLYLMHFPVGY--KYVCDEILMPMSGDELQTvEIDYLDTWRAMENLVKLGMVRSIGLSNF 199
Cdd:cd19117 82 -RRVEEALDQSLKKLGLDYVDLYLMHWPVPLdpDGNDFLFKKDDGTKDHEP-DWDFIKTWELMQKLPATGKVKAIGVSNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 200 NMEQIQRIIQCSSSK--PVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNrknhCPVYfFSEGMKRLVKKYKRSA 277
Cdd:cd19117 160 SIKNLEKLLASPSAKivPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTN----APLL-KEPVIIKIAKKHGKTP 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 281366738 278 SQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDE 315
Cdd:cd19117 235 AQVIISWGLQRGYSVLPKSVTPSRIESNFKLFTLSDEE 272
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
41-317 |
2.31e-68 |
|
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: 216.50 E-value: 2.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQikmgNISRENIFLTTKLWNTHH 120
Cdd:cd19127 1 ITLNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRS----GVDRSDIFVTTKLWISDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 DPRDVRRICEKQLELLGFSYIDLYLMHFPVgykyvcdeilmPMSGDelqtveiDYLDTWRAMENLVKLGMVRSIGLSNFN 200
Cdd:cd19127 77 GYDKALRGFDASLRRLGLDYVDLYLLHWPV-----------PNDFD-------RTIQAYKALEKLLAEGRVRAIGVSNFT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 201 MEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRK----NHCPVYFFS-EGMKRLVKKYKR 275
Cdd:cd19127 139 PEHLERLIDATTVVPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYgasgPTGPGDVLQdPTITGLAEKYGK 218
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 281366738 276 SASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19127 219 TPAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAED 260
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
50-317 |
8.62e-68 |
|
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: 215.46 E-value: 8.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWNTHHDPRDVRRIC 129
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 130 EKQLELLGFSYIDLYLMHFPVgyKYVCDEILMPMSGDELQTVEIDYL-DTWRAMENLVKLGMVRSIGLSNFNMEQIQRII 208
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPL--AFDMDTDGDPRDDNQIQSLSKKPLeDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 209 QCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVYFFSEgMKRLVKKYKRSASQIVL-----R 283
Cdd:cd19128 160 NYCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTFLNDSE-LKALATKYNTTPPQVIIawhlqK 238
|
250 260 270
....*....|....*....|....*....|....
gi 281366738 284 YLIDYGVvpIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19128 239 WPKNYSV--IPKSANKSRCQQNFDINDLALTKED 270
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
46-322 |
1.70e-67 |
|
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: 214.02 E-value: 1.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGYQCS------AAVHC---AIETGFRHFDTAYYY---ENEKEIGEALRtqikmgNISRENIFLTT 113
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKdysddkKAIEAlryAIELGINLIDTAEMYgggHAEELVGKAIK------GFDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 114 KLWNTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYkyvcdeilmpmsgdelqtveIDYLDTWRAMENLVKLGMVRS 193
Cdd:cd19072 75 KVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPS--------------------IPIEETLRAMEELVEEGKIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 194 IGLSNFNMEQIQRIIQCSSSKPVV-NQVEI-----WPgflQKDLVDYCRYNGIIVTAFSPLGQPNRKNHcpvyFFSEGMK 267
Cdd:cd19072 135 IGVSNFSLEELEEAQSYLKKGPIVaNQVEYnlfdrEE---ESGLLPYCQKNGIAIIAYSPLEKGKLSNA----KGSPLLD 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 281366738 268 RLVKKYKRSASQIVLRYLI-DYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLR 322
Cdd:cd19072 208 EIAKKYGKTPAQIALNWLIsKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
41-308 |
5.70e-67 |
|
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: 213.90 E-value: 5.70e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 41 VRLSSGHEMPVLGFGTY---KLRGyQCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKLWN 117
Cdd:cd19119 4 FKLNTGASIPALGLGTAsphEDRA-EVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 118 THHDprDVRRICEKQLELLGFSYIDLYLMHFPVGYKYVCDEILMPM-----SGDELQTVEIDYLDTWRAMENLVKLGMVR 192
Cdd:cd19119 83 TFYD--EVERSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKPFtpvndDGKTRYAASGDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 193 SIGLSNFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHcpvyfFSEGMKRLVKK 272
Cdd:cd19119 161 AIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAPNL-----KNPLVKKIAEK 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 281366738 273 YKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNI 308
Cdd:cd19119 236 YNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI 271
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
43-315 |
9.13e-65 |
|
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: 207.07 E-value: 9.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 43 LSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTHHDP 122
Cdd:cd19130 4 LNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAA----IAASGIPRDELFVTTKLWNDRHDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 123 RDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilMPMSGDelqtveidYLDTWRAMENLVKLGMVRSIGLSNFNME 202
Cdd:cd19130 80 DEPAAAFAESLAKLGLDQVDLYLVHWP-----------TPAAGN--------YVHTWEAMIELRAAGRTRSIGVSNFLPP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 203 QIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNrknhcpvYFFSEGMKRLVKKYKRSASQIVL 282
Cdd:cd19130 141 HLERIVAATGVVPAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK-------LLGDPPVGAIAAAHGKTPAQIVL 213
|
250 260 270
....*....|....*....|....*....|...
gi 281366738 283 RYLIDYGVVPIPKAANPIHIKENLNIFDFKLDE 315
Cdd:cd19130 214 RWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTD 246
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
39-330 |
3.77e-61 |
|
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: 197.77 E-value: 3.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLSSGHEMPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNT 118
Cdd:cd19134 1 PTVTLNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRA----IAASGIPRGELFVTTKLATP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 119 HHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGykyvcdeilmpmsgdelqtVEIDYLDTWRAMENLVKLGMVRSIGLSN 198
Cdd:cd19134 77 DQGFTASQAACRASLERLGLDYVDLYLIHWPAG-------------------REGKYVDSWGGLMKLREEGLARSIGVSN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 199 FNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPNRKNHCPVyffsegmKRLVKKYKRSAS 278
Cdd:cd19134 138 FTAEHLENLIDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVGRLLDNPAV-------TAIAAAHGRTPA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 281366738 279 QIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRI 330
Cdd:cd19134 211 QVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
43-317 |
7.06e-58 |
|
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: 190.53 E-value: 7.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 43 LSSGHEMPVLGFGTYKLRGY--QCSAAVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMG-NISRENIFLTTKLWNTH 119
Cdd:cd19122 3 LNNGVKIPAVGFGTFANEGAkgETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 120 HDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKYvcDEILMPMSGDELQTVEIDYLD-----TWRAMENLVKLGMVRSI 194
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAEK--NDQRSPKLGPDGKYVILKDLTenpepTWRAMEEIYESGKAKAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 195 GLSNFNMEQIQRIIQCSSSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQPN-------RKNHCPVyffsegMK 267
Cdd:cd19122 161 GVSNWTIPGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNqvpstgeRVSENPT------LN 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 281366738 268 RLVKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDfkLDEAD 317
Cdd:cd19122 235 EVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKSIE--LSDED 282
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
52-324 |
2.56e-52 |
|
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: 175.96 E-value: 2.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 52 LGFGTYKLRGYQCS-------AAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQIKMgnisRENIFLTTKL------ 115
Cdd:pfam00248 1 IGLGTWQLGGGWGPiskeealEALRAALEAGINFIDTAEVYgdgKSEELLGEALKDYPVK----RDKVVIATKVpdgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 116 WNTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYKyvcdeilmpmsgdelqtveiDYLDTWRAMENLVKLGMVRSIG 195
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDT--------------------PIEETWDALEELKKEGKIRAIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 196 LSNFNMEQIQRIIQCSSSKPVVNQVE--IWPGFLQKDLVDYCRYNGIIVTAFSPLGQP-----NRKNHCPVYFFSEG--- 265
Cdd:pfam00248 137 VSNFDAEQIEKALTKGKIPIVAVQVEynLLRRRQEEELLEYCKKNGIPLIAYSPLGGGlltgkYTRDPDKGPGERRRllk 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366738 266 ------------MKRLVKKYKRSASQIVLRYLI--DYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:pfam00248 217 kgtplnlealeaLEEIAKEHGVSPAQVALRWALskPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDEL 289
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
46-321 |
2.13e-51 |
|
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: 172.37 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGY---------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmgNISRENIFLTT 113
Cdd:cd19137 1 GEKIPALGLGTWGIGGFltpdysrdeEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIK------DFPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 114 KLWNTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgdelqTVEIDYLDTWRAMENLVKLGMVRS 193
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP--------------------NPNIPLEETLSAMAEGVRQGLIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 194 IGLSNFNMEQIQRIIQCSSSKPVVNQVE---IWPGFLQKDLVDYCRYNGIIVTAFSPLgqpnRKNHCPVyffSEGMKRLV 270
Cdd:cd19137 135 IGVSNFNRRLLEEAISKSQTPIVCNQVKynlEDRDPERDGLLEYCQKNGITVVAYSPL----RRGLEKT---NRTLEEIA 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 281366738 271 KKYKRSASQIVLRYLIDY-GVVPIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19137 208 KNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
49-317 |
2.63e-50 |
|
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: 169.07 E-value: 2.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 49 MPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTHHDPRDVRRI 128
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 129 CEKQLELLGFSYIDLYLMHFPVGYKYVcdeilmPMSgdelqtveiDYLDtwrAMENLVKLGMVRSIGLSNFNMEQIQRII 208
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWPSPNDEV------PVE---------EYIG---ALAEAKEQGLTRHIGVSNFTIALLDEAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 209 QCSSSKPVV-NQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQpNRKNHCPVyffsegMKRLVKKYKRSASQIVLRYLID 287
Cdd:cd19139 139 AVVGAGAIAtNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLAY-GKVLDDPV------LAAIAERHGATPAQIALAWAMA 211
|
250 260 270
....*....|....*....|....*....|
gi 281366738 288 YGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19139 212 RGYAVIPSSTKREHLRSNLLALDLTLDADD 241
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
39-321 |
2.79e-49 |
|
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: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLSSGHEMPVLGFGTYKL-----RGYQCSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRTQikmgnisRENIF 110
Cdd:cd19138 1 RTVTLPDGTKVPALGQGTWYMgedpaKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 111 LTTKLWNTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGYkyvcdeilmPMSgdelqtveidylDTWRAMENLVKLGM 190
Cdd:cd19138 74 LVSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGV---------PLA------------ETVAAMEELKKEGK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 191 VRSIGLSNFNMEQIQRIIQCSSSKP-VVNQVEIWPGF--LQKDLVDYCRYNGIIVTAFSPLGQPNRKNHcpVYFFSEGMK 267
Cdd:cd19138 133 IRAWGVSNFDTDDMEELWAVPGGGNcAANQVLYNLGSrgIEYDLLPWCREHGVPVMAYSPLAQGGLLRR--GLLENPTLK 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 281366738 268 RLVKKYKRSASQIVLRYLI-DYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19138 211 EIAARHGATPAQVALAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
48-322 |
4.09e-42 |
|
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: 149.30 E-value: 4.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 48 EMPVLGFGTY----KLRGY-------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmGNISRENIFLTT 113
Cdd:cd19093 1 EVSPLGLGTWqwgdRLWWGygeygdeDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLK-----ELGDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 114 KLWNTHHD--PRDVRRICEKQLELLGFSYIDLYLMHFPVGYkYVCDEILmpmsgdelqtveidyldtWRAMENLVKLGMV 191
Cdd:cd19093 76 KFAPLPWRltRRSVVKALKASLERLGLDSIDLYQLHWPGPW-YSQIEAL------------------MDGLADAVEEGLV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 192 RSIGLSNFNMEQIQRIIQCSSSK---PVVNQVE---IWPGFLQKDLVDYCRYNGIIVTAFSPLGQ--------------- 250
Cdd:cd19093 137 RAVGVSNYSADQLRRAHKALKERgvpLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQglltgkyspenpppg 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366738 251 -----PNRKNHCPVYFFSEGMKRLVKKYKRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLR 322
Cdd:cd19093 217 grrrlFGRKNLEKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
44-324 |
6.58e-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: 146.48 E-value: 6.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 44 SSGHEMPVLGFGTYKL-RGY------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmgNISRENIFLTT 113
Cdd:COG0667 8 RSGLKVSRLGLGTMTFgGPWggvdeaEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK------GRPRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 114 KL--------WNTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELQTVEidylDTWRAMENL 185
Cdd:COG0667 82 KVgrrmgpgpNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP----------------DPDTPIE----ETLGALDEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 186 VKLGMVRSIGLSNFNMEQIQRI--IQCSSSKPVVNQVE---IWPGFLqKDLVDYCRYNGIIVTAFSPLGQ------PNRK 254
Cdd:COG0667 142 VREGKIRYIGVSNYSAEQLRRAlaIAEGLPPIVAVQNEyslLDRSAE-EELLPAARELGVGVLAYSPLAGglltgkYRRG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 255 NHCP------VYFFS-----------EGMKRLVKKYKRSASQIVLRYLIDYGVV--PIPKAANPIHIKENLNIFDFKLDE 315
Cdd:COG0667 221 ATFPegdraaTNFVQgylternlalvDALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEENLAAADLELSA 300
|
....*....
gi 281366738 316 ADTRLLRGI 324
Cdd:COG0667 301 EDLAALDAA 309
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
50-306 |
4.92e-40 |
|
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: 141.89 E-value: 4.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRGY----QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQIKmgnisRENIFLTTKLWNTHH-- 120
Cdd:cd06660 1 SRLGLGTMTFGGDgdeeEAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-----RDDVVIATKGGHPPGgd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 ------DPRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELQTVEidylDTWRAMENLVKLGMVRSI 194
Cdd:cd06660 76 psrsrlSPEHIRRDLEESLRRLGTDYIDLYYLHRD----------------DPSTPVE----ETLEALNELVREGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 195 GLSNFNMEQIQRIIQCSSSK----PVVNQVE---IWPGFLQKDLVDYCRYNGIIVTAFSPLGQpnrknhcpvyffseGMk 267
Cdd:cd06660 136 GVSNWSAERLAEALAYAKAHglpgFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR--------------GP- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 281366738 268 rlvkkykrsaSQIVLRYLI--DYGVVPIPKAANPIHIKENL 306
Cdd:cd06660 201 ----------AQLALAWLLsqPFVTVPIVGARSPEQLEENL 231
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
46-322 |
1.72e-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: 134.19 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGY--------QCSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRTQikmgnisRENIFLTTK 114
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTwwgevddqESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 ---LWN----THHD--PRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELQTVEidylDTWRAMENL 185
Cdd:cd19084 74 cglRWDggkgVTKDlsPESIRKEVEQSLRRLQTDYIDLYQIHWP----------------DPNTPIE----ETAEALEKL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 186 VKLGMVRSIGLSNFNMEQIQRIIQCssSKPVVNQVE---IWPGFlQKDLVDYCRYNGIIVTAFSPLGQ------------ 250
Cdd:cd19084 134 KKEGKIRYIGVSNFSVEQLEEARKY--GPIVSLQPPysmLEREI-EEELLPYCRENGIGVLPYGPLAQglltgkykkept 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 251 --PN--RKNHcpVYFFSEG----------MKRLVKKYKRSASQIVLRYLIDY-GV-VPIPKAANPIHIKENLNIFDFKLD 314
Cdd:cd19084 211 fpPDdrRSRF--PFFRGENfeknleivdkLKEIAEKYGKSLAQLAIAWTLAQpGVtSAIVGAKNPEQLEENAGALDWELT 288
|
....*...
gi 281366738 315 EADTRLLR 322
Cdd:cd19084 289 EEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
50-324 |
1.89e-36 |
|
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: 134.25 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRGY---------QCSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRTQikmgnisRENIFLTTKLWN 117
Cdd:cd19085 2 SRLGLGCWQFGGGywwgdqddeESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 118 THHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGykyvcdeilmpmsgdelqtvEIDYLDTWRAMENLVKLGMVRSIGLS 197
Cdd:cd19085 75 DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSS--------------------DVPLEETMEALEKLKEEGKIRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 NFNMEQIQRIIQcsSSKPVVNQVE---IWPGfLQKDLVDYCRYNGIIVTAFSPLGQ--------------PNRKNHCPVY 260
Cdd:cd19085 135 NFGPAQLEEALD--AGRIDSNQLPynlLWRA-IEYEILPFCREHGIGVLAYSPLAQglltgkfssaedfpPGDARTRLFR 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281366738 261 FFSEGM-----------KRLVKKYKRSASQIVLRYLI--DYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19085 212 HFEPGAeeetfealeklKEIADELGVTMAQLALAWVLqqPGVTSVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
49-331 |
1.44e-35 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 130.91 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 49 MPVLGFGTYKLRGYQCSAAVHCAIETGFRHFDTAYYYENEKEIGEAlrtqIKMGNISRENIFLTTKLWNTHHDPRDVRRI 128
Cdd:PRK11172 3 IPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIDNLAKDKLIPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 129 CEKQLELLGFSYIDLYLMHFPVgykyvcdeilmpmSGDELQTVEIdyldtwraMENLV---KLGMVRSIGLSNFNMEQIQ 205
Cdd:PRK11172 79 LKESLQKLRTDYVDLTLIHWPS-------------PNDEVSVEEF--------MQALLeakKQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 206 RIIQCSSSKPV-VNQVEIWPgFLQ-KDLVDYCRYNGIIVTAFSPLGQpNRKNHCPVyffsegMKRLVKKYKRSASQIVLR 283
Cdd:PRK11172 138 QAIAAVGAENIaTNQIELSP-YLQnRKVVAFAKEHGIHVTSYMTLAY-GKVLKDPV------IARIAAKHNATPAQVILA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 281366738 284 YLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGIKPKSRIV 331
Cdd:PRK11172 210 WAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGRLV 257
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
46-329 |
1.69e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 108.75 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGYQCSAA---VHCAIETGFRHFDTAYYYEN-EKEIGEALRTQikmgnisRENIFLTTKLWNTHHD 121
Cdd:COG1453 10 GLEVSVLGFGGMRLPRKDEEEAealIRRAIDNGINYIDTARGYGDsEEFLGKALKGP-------RDKVILATKLPPWVRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 PRDVRRICEKQLELLGFSYIDLYLMHfpvgykYVCDEILMPMSGDElqtveidyLDTWRAMENLVKLGMVRSIGLSNFNM 201
Cdd:COG1453 83 PEDMRKDLEESLKRLQTDYIDLYLIH------GLNTEEDLEKVLKP--------GGALEALEKAKAEGKIRHIGFSTHGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 202 -EQIQRII--------QCSsskpvVNQVEiWPGFLQKDLVDYCRYNGIIVTAFSPL--GQpnrknhcpVYFFSEGMKRLV 270
Cdd:COG1453 149 lEVIKEAIdtgdfdfvQLQ-----YNYLD-QDNQAGEEALEAAAEKGIGVIIMKPLkgGR--------LANPPEKLVELL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366738 271 KKyKRSASQIVLRYLIDY-GV-VPIPKAANPIHIKENLNIFD--FKLDEADTRLLRGIKPKSR 329
Cdd:COG1453 215 CP-PLSPAEWALRFLLSHpEVtTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERLAEELG 276
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
51-321 |
3.04e-26 |
|
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: 106.60 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 51 VLGFGTYKL--------RGYQCS----AAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQikmgnisRENIFLTTK- 114
Cdd:cd19102 3 TIGLGTWAIggggwgggWGPQDDrdsiAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 --LWN------THHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGykyvcdeilmpmsgdelqtvEIDYLDTWRAMENLV 186
Cdd:cd19102 76 glLWDeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP--------------------DEPIEEAWGALAELK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 187 KLGMVRSIGLSNFNMEQIQRiiqCSSSKPV-VNQveiwPGF------LQKDLVDYCRYNGIIVTAFSPLGQ--------- 250
Cdd:cd19102 136 EEGKVRAIGVSNFSVDQMKR---CQAIHPIaSLQ----PPYsllrrgIEAEILPFCAEHGIGVIVYSPMQSglltgkmtp 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 251 -------PNRKNHCPVYF----------FSEGMKRLVKKYKRSASQIVLRY-LIDYGVV-PIPKAANPIHIKENLNIFDF 311
Cdd:cd19102 209 ervaslpADDWRRRSPFFqepnlarnlaLVDALRPIAERHGRTVAQLAIAWvLRRPEVTsAIVGARRPDQIDETVGAADL 288
|
330
....*....|
gi 281366738 312 KLDEADTRLL 321
Cdd:cd19102 289 RLTPEELAEI 298
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
39-321 |
4.69e-25 |
|
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: 103.45 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRL-SSGHEMPVLGFGT------YKLRGYQCSAAV-HCAIETGFRHFDTAYYY---ENEKEIGEALRTQikmgnisRE 107
Cdd:cd19076 1 PTRKLgTQGLEVSALGLGCmgmsafYGPADEEESIATlHRALELGVTFLDTADMYgpgTNEELLGKALKDR-------RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 108 NIFLTTKlWNTHHDPRD-----------VRRICEKQLELLGFSYIDLYLMHFPvgykyvcDeilmpmsgdelQTVEIDyl 176
Cdd:cd19076 74 EVVIATK-FGIVRDPGSgfrgvdgrpeyVRAACEASLKRLGTDVIDLYYQHRV-------D-----------PNVPIE-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 177 DTWRAMENLVKLGMVRSIGLSNFNMEQIQRiiqCSSSKPVVN-QVE--IWPGFLQKDLVDYCRYNGIIVTAFSPL----- 248
Cdd:cd19076 133 ETVGAMAELVEEGKVRYIGLSEASADTIRR---AHAVHPITAvQSEysLWTRDIEDEVLPTCRELGIGFVAYSPLgrgfl 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 249 -GQPNRKNHCPVYFFSEGMKR-----------LVKKYKR-------SASQIVLRYLIDYG--VVPIPKAANPIHIKENLN 307
Cdd:cd19076 210 tGAIKSPEDLPEDDFRRNNPRfqgenfdknlkLVEKLEAiaaekgcTPAQLALAWVLAQGddIVPIPGTKRIKYLEENVG 289
|
330
....*....|....
gi 281366738 308 IFDFKLDEADTRLL 321
Cdd:cd19076 290 ALDVVLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
45-322 |
1.32e-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: 102.35 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 45 SGHEMPVLGFGTYKLRGY---------QCSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRTQikmgnisRENIFLT 112
Cdd:cd19149 7 SGIEASVIGLGTWAIGGGpwwggsddnESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR-------RDKVVLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 113 TK---LWNT----HHDPRDVRRI------------CEKQLELLGFSYIDLYLMHFpvgykyvcdeilmpmsgdelQTVEI 173
Cdd:cd19149 80 TKcglRWDReggsFFFVRDGVTVyknlspesireeVEQSLKRLGTDYIDLYQTHW--------------------QDVET 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 174 DYLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCSSskPVVNQVE---IWPGfLQKDLVDYCRYNGIIVTAFSPLGQ 250
Cdd:cd19149 140 PIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQ--LDIIQEKysmLDRG-IEKELLPYCKKNNIAFQAYSPLEQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 251 ----------------PNRKNHcP---------VYFFSEGMKRLVKKYKRSASQIVLRYLIDYG--VVPIPKAANPIHIK 303
Cdd:cd19149 217 glltgkitpdrefdagDARSGI-PwfspenrekVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAE 295
|
330
....*....|....*....
gi 281366738 304 ENLNIFDFKLDEADTRLLR 322
Cdd:cd19149 296 ENAKAGDIRLSAEDIATMR 314
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
44-322 |
1.34e-23 |
|
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: 99.17 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 44 SSGHEMPVLGFGTYKLRGY-----QCSAAVHCAIETGFRHFDTA--Y-YYENEKEIGEALRTQikmgNISRENIFLTTK- 114
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWgesaeELLSLIEAALELGITTFDHAdiYgGGKCEELFGEALALN----PGLREKIEIQTKc 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 ---------LWNTHH---DPRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgdelqtveiDYL----DT 178
Cdd:cd19092 77 girlgddprPGRIKHydtSKEHILASVEGSLKRLGTDYLDLLLLHRP------------------------DPLmdpeEV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 179 WRAMENLVKLGMVRSIGLSNFNMEQIQrIIQCSSSKP-VVNQVEIWP---GFLQKDLVDYCRYNGIIVTAFSPLGQPN-R 253
Cdd:cd19092 133 AEAFDELVKSGKVRYFGVSNFTPSQIE-LLQSYLDQPlVTNQIELSLlhtEAIDDGTLDYCQLLDITPMAWSPLGGGRlF 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281366738 254 KNHCPVYF-FSEGMKRLVKKYKRSASQIVLRYLIDY--GVVPIPKAANPIHIKENLNIFDFKLDEAD-TRLLR 322
Cdd:cd19092 212 GGFDERFQrLRAALEELAEEYGVTIEAIALAWLLRHpaRIQPILGTTNPERIRSAVKALDIELTREEwYEIYE 284
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-306 |
3.96e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 91.00 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 40 KVRL-SSGHEMPVLGFGTYKLRGY---QCSAAVHCAIETGFRHFDTAYYYEN-EKEIGEALRTQikmgnisRENIFLTTK 114
Cdd:cd19100 1 YRRLgRTGLKVSRLGFGGGPLGRLsqeEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 LWNthHDPRDVRRICEKQLELLGFSYIDLYLMHFpVGYKYVCDEILMPMsgdelqtveidyldtwRAMENLVKL---GMV 191
Cdd:cd19100 74 TGA--RDYEGAKRDLERSLKRLGTDYIDLYQLHA-VDTEEDLDQVFGPG----------------GALEALLEAkeeGKI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 192 RSIGLSNFNMEQIQR--------IIQCSsskpvVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGqpnrknhcpvyffs 263
Cdd:cd19100 135 RFIGISGHSPEVLLRaletgefdVVLFP-----INPAGDHIDSFREELLPLAREKGVGVIAMKVLA-------------- 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281366738 264 EGmkRLVKKYKRSASQiVLRYLIDYGVV--PIPKAANPIHIKENL 306
Cdd:cd19100 196 GG--RLLSGDPLDPEQ-ALRYALSLPPVdvVIVGMDSPEELDENL 237
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
39-331 |
4.49e-21 |
|
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: 92.89 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRLS-SGHEMPVLGFGTYKLR-GY-------QCSAAVHCAIETGFRHFDTA-YYYENEKEIGEALrtqiKMGNISREN 108
Cdd:cd19144 2 PTRTLGrNGPSVPALGFGAMGLSaFYgppkpdeERFAVLDAAFELGCTFWDTAdIYGDSEELIGRWF----KQNPGKREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 109 IFLTTKLWN----------THHDPRDVRRICEKQLELLGFSYIDLYLMHFPVGykyvcdeilmpmsgdelqTVEIDylDT 178
Cdd:cd19144 78 IFLATKFGIeknvetgeysVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDG------------------KTPIE--KT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 179 WRAMENLVKLGMVRSIGLSNFNMEQIQRiiqCSSSKPVVN-QVEIWPGFL-----QKDLVDYCRYNGIIVTAFSPLGQ-- 250
Cdd:cd19144 138 VAAMAELVQEGKIKHIGLSECSAETLRR---AHAVHPIAAvQIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGRgf 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 251 -----PNRKNHCPVYF------FSE-----------GMKRLVKKYKRSASQIVLRYLIDYG--VVPIPKAANPIHIKENL 306
Cdd:cd19144 215 ltgaiRSPDDFEEGDFrrmaprFQAenfpknlelvdKIKAIAKKKNVTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENL 294
|
330 340
....*....|....*....|....*
gi 281366738 307 NIFDFKLDEADTRLLRGIKPKSRIV 331
Cdd:cd19144 295 GALKVKLTEEEEKEIREIAEEAEVV 319
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-210 |
8.62e-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: 90.34 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLrGYQCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTqikmgnISRENIFLTTKLWNTHH-- 120
Cdd:cd19105 10 GLKVSRLGFGGGGL-PRESPELLRRALDLGINYFDTAEGYgngNSEEIIGEALKG------LRRDKVFLATKASPRLDkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 DPRDVRRICEKQLELLGFSYIDLYLMHF--PVGYKYVCDEILmpmsgdelqtveidyldtwRAMENLVKLGMVRSIGLS- 197
Cdd:cd19105 83 DKAELLKSVEESLKRLQTDYIDIYQLHGvdTPEERLLNEELL-------------------EALEKLKKEGKVRFIGFSt 143
|
170
....*....|....
gi 281366738 198 NFNM-EQIQRIIQC 210
Cdd:cd19105 144 HDNMaEVLQAAIES 157
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
50-314 |
1.06e-20 |
|
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: 90.35 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRGY----------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTqikmgniSRENIFLTTKL- 115
Cdd:cd19088 2 SRLGYGAMRLTGPgiwgppadreEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALHP-------YPDDVVIATKGg 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 116 --------WNTHHDPRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDelQTVEIDylDTWRAMENLVK 187
Cdd:cd19088 75 lvrtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRI----------------D--PKVPFE--EQLGALAELQD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 188 LGMVRSIGLSNFNMEQI---QRIIQCSSskpVVNQVEIWPgflQKD--LVDYCRYNGIIVTAFSPL-GQPNRKNhcpvyf 261
Cdd:cd19088 135 EGLIRHIGLSNVTVAQIeeaRAIVRIVS---VQNRYNLAN---RDDegVLDYCEAAGIAFIPWFPLgGGDLAQP------ 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 281366738 262 fSEGMKRLVKKYKRSASQIVLRYLIDYG--VVPIPKAANPIHIKENLNIFDFKLD 314
Cdd:cd19088 203 -GGLLAEVAARLGATPAQVALAWLLARSpvMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
50-310 |
1.06e-20 |
|
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: 90.31 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGT--YKLRGY------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmgNISRENIFLTTKL-WN 117
Cdd:cd19096 1 SVLGFGTmrLPESDDdsideeKAIEMIRYAIDAGINYFDTAYGYgggKSEEILGEALK------EGPREKFYLATKLpPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 118 THHDPRDVRRICEKQLELLGFSYIDLYLMHfpvgykyvcdeilMPMSGDELQTVEIdyLDTWRAMENLVKLGMVRSIGLS 197
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLH-------------GLNSPEWLEKARK--GGLLEFLEKAKKEGLIRHIGFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 198 nFNM--EQIQRIIqcsSSKPV-VNQVEI----WPGFLQKDLVDYCRYNGIIVTAFSPL---GQPNRknhcpvyffSEGMK 267
Cdd:cd19096 140 -FHDspELLKEIL---DSYDFdFVQLQYnyldQENQAGRPGIEYAAKKGMGVIIMEPLkggGLANN---------PPEAL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281366738 268 RLVKKYKRSASQIVLRYLIDYGVVP--IPKAANPIHIKENLNIFD 310
Cdd:cd19096 207 AILCGAPLSPAEWALRFLLSHPEVTtvLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
53-324 |
1.15e-20 |
|
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: 91.21 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 53 GFGTYKLRGY--------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmGNISRENIFLTTKL---WNT 118
Cdd:cd19148 8 ALGTWAIGGWmwggtdekEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKALK-----EYGKRDRVVIATKVgleWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 119 HHDP-RD-----VRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELQTVEidylDTWRAMENLVKLGMVR 192
Cdd:cd19148 83 GGEVvRNssparIRKEVEDSLRRLQTDYIDLYQVHWP----------------DPLVPIE----ETAEALKELLDEGKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 193 SIGLSNFN---MEQIQRIIQCSSSKPVVNQVEiwPGFlQKDLVDYCRYNGIIVTAFSPL------GQPNR---------K 254
Cdd:cd19148 143 AIGVSNFSpeqMETFRKVAPLHTVQPPYNLFE--REI-EKDVLPYARKHNIVTLAYGALcrgllsGKMTKdtkfegddlR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 255 NHCPVY---FFS------EGMKRLVKK-YKRSASQIVLRYLIDYGVVPIP--KAANPIHIKENLNIFDFKLDEADTRLLR 322
Cdd:cd19148 220 RTDPKFqepRFSqylaavEELDKLAQErYGKSVIHLAVRWLLDQPGVSIAlwGARKPEQLDAVDEVFGWSLNDEDMKEID 299
|
..
gi 281366738 323 GI 324
Cdd:cd19148 300 AI 301
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
71-321 |
1.23e-20 |
|
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: 91.11 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 71 AIETGFRHFDTAYYYEN---EKEIGEALRtqikmGNISRENIFLTTKLWN-THHDPRD-------VRRICEKQLELLGFS 139
Cdd:cd19079 44 ALDLGINFFDTANVYSGgasEEILGRALK-----EFAPRDEVVIATKVYFpMGDGPNGrglsrkhIMAEVDASLKRLGTD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 140 YIDLYLMHfpvgykyvcdeilmpmsgdelqtvEIDY----LDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCSS--- 212
Cdd:cd19079 119 YIDLYQIH------------------------RWDYetpiEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEkng 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 213 -SKPVVNQV-------EIwpgflQKDLVDYCRYNGIIVTAFSPLGQ--------PNRKNHCPVYFFSEGMKR-------- 268
Cdd:cd19079 175 wTKFVSMQNhynllyrEE-----EREMIPLCEEEGIGVIPWSPLARgrlarpwgDTTERRRSTTDTAKLKYDyfteadke 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366738 269 -------LVKKYKRSASQIVLRYLIDYGVV--PIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19079 250 ivdrveeVAKERGVSMAQVALAWLLSKPGVtaPIVGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
44-317 |
2.61e-20 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 90.21 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 44 SSGHEMPVLGFGTYKLRGYQCSAA-----VHCAIETGFRHFDTA-YY--YENEKEIGEALrtqiKMGNISRENIFLTTK- 114
Cdd:COG4989 8 ASGLSVSRIVLGCMRLGEWDLSPAeaaalIEAALELGITTFDHAdIYggYTCEALFGEAL----KLSPSLREKIELQTKc 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 ---LWNTHHDPRD---------VRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELqtVEIDylDTWRAM 182
Cdd:COG4989 84 girLPSEARDNRVkhydtskehIIASVEGSLRRLGTDYLDLLLLHRP----------------DPL--MDPE--EVAEAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 183 ENLVKLGMVRSIGLSNFNMEQIQrIIQCSSSKP-VVNQVEIWP---GFLQKDLVDYCRYNGIIVTAFSPLGQPnrknhcp 258
Cdd:COG4989 144 DELKASGKVRHFGVSNFTPSQFE-LLQSALDQPlVTNQIELSLlhtDAFDDGTLDYCQLNGITPMAWSPLAGG------- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281366738 259 vYFFSEG----------MKRLVKKYKRSASQIVLRYLIDY--GVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:COG4989 216 -RLFGGFdeqfprlraaLDELAEKYGVSPEAIALAWLLRHpaGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
50-306 |
6.88e-20 |
|
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: 88.06 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRGY-------QCSAAVHCAIETGFRHFDTAYYYEN-EKEIGEALRTQIkmgnisRENIFLTTKLWNTHHD 121
Cdd:cd19095 1 SVLGLGTSGIGRVwgvpseaEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAGLR------RDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 PRD--------VRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmSGDELQTVEIDYLDTWRAMenlvklGMVRS 193
Cdd:cd19095 75 GRDrkdfspaaIRASIERSLRRLGTDYIDLLQLHGP--------------SDDELTGEVLETLEDLKAA------GKVRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 194 IGLSNFNMEqIQRIIQcssSKPV------VNQVEIWpgflQKDLVDYCRYNGIIVTAFSPLGQ---PNRKNHCPVYFFSE 264
Cdd:cd19095 135 IGVSGDGEE-LEAAIA---SGVFdvvqlpYNVLDRE----EEELLPLAAEAGLGVIVNRPLANgrlRRRVRRRPLYADYA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281366738 265 GMKRLVKKYK-RSASQIVLRYLIDYGVVP--IPKAANPIHIKENL 306
Cdd:cd19095 207 RRPEFAAEIGgATWAQAALRFVLSHPGVSsaIVGTTNPEHLEENL 251
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
51-315 |
9.42e-20 |
|
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: 88.42 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 51 VLGFGTYKLRGYQ-----CSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRTqikmgnISRENIFLTTKL-WNTHHD 121
Cdd:cd19074 6 ELSLGTWLTFGGQvddedAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALKG------WPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 PRD-------VRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELQTVEidylDTWRAMENLVKLGMVRSI 194
Cdd:cd19074 80 PNDrglsrkhIFESIHASLKRLQLDYVDIYYCHRY----------------DPETPLE----ETVRAMDDLIRQGKILYW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 195 GLSNFNMEQIQR----IIQCSSSKPVVNQVEIwpGFLQKDLVDY----CRYNGIIVTAFSPL-----------GQPN--- 252
Cdd:cd19074 140 GTSEWSAEQIAEahdlARQFGLIPPVVEQPQY--NMLWREIEEEviplCEKNGIGLVVWSPLaqglltgkyrdGIPPpsr 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366738 253 -RKNHCPVYFFS------------EGMKRLVKKYKRSASQIVLRYLI--DYGVVPIPKAANPIHIKENLNIFDFKLDE 315
Cdd:cd19074 218 sRATDEDNRDKKrrlltdenlekvKKLKPIADELGLTLAQLALAWCLrnPAVSSAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
69-249 |
3.70e-19 |
|
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: 86.86 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 69 HCAIETGFRHFDTAYYY---ENEKEIGEALRTQikmgnisRENIFLTTKLW-NTHHDP-------RDVRRICEKQLELLG 137
Cdd:cd19087 37 DRALDAGINFFDTADVYgggRSEEIIGRWIAGR-------RDDIVLATKVFgPMGDDPndrglsrRHIRRAVEASLRRLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 138 FSYIDLYLMHfpvgykyvcdEILMPMSGDElqtveidyldTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCS------ 211
Cdd:cd19087 110 TDYIDLYQMH----------HFDRDTPLEE----------TLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAarrgll 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 281366738 212 ---SSKPVVN------QVEIWPGflqkdlvdyCRYNGIIVTAFSPLG 249
Cdd:cd19087 170 rfvSEQPMYNllkrqaELEILPA---------ARAYGLGVIPYSPLA 207
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
51-307 |
2.22e-17 |
|
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: 80.60 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 51 VLGFGTYKLRG--------YQCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQikmgnisRENIFLTTKLWNTH 119
Cdd:cd19086 5 EIGFGTWGLGGdwwgdvddAEAIRALRAALDLGINFFDTADVYgdgHSERLLGKALKGR-------RDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 120 H---------DPRDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgdelqTVEIDYLD-TWRAMENLVKLG 189
Cdd:cd19086 78 DggperpqdfSPEYIREAVEASLKRLGTDYIDLYQLHNP--------------------PDEVLDNDeLFEALEKLKQEG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 190 MVRSIGLSNFNMEQIQRIIQcsSSKPVVNQV-----EIWPGflqKDLVDYCRYNGIIVTAFSPLgqpnrknhcpvyffSE 264
Cdd:cd19086 138 KIRAYGVSVGDPEEALAALR--RGGIDVVQViynllDQRPE---EELFPLAEEHGVGVIARVPL--------------AS 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 281366738 265 GMkrLVKKykrsASQIVLRYLIDYGVV--PIPKAANPIHIKENLN 307
Cdd:cd19086 199 GL--LTGK----LAQAALRFILSHPAVstVIPGARSPEQVEENAA 237
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
72-306 |
3.01e-17 |
|
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: 81.06 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 72 IETGFRHFDTAYYY-------ENEKEIGEALRTQIKmgnisRENIFLTTK-----LWNTHH---DPRDVRRICEKQLELL 136
Cdd:cd19082 27 VELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-----RDKVVIATKgghpdLEDMSRsrlSPEDIRADLEESLERL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 137 GFSYIDLYLMH-----FPVGykyvcdEILmpmsgdelqtveidyldtwRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCS 211
Cdd:cd19082 102 GTDYIDLYFLHrddpsVPVG------EIV-------------------DTLNELVRAGKIRAFGASNWSTERIAEANAYA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 212 SSK----PVVNQV---------EIWPG----FLQKDLVDYCRYNGIIVTAFSPLGQ-------------PNRKNHCpvyF 261
Cdd:cd19082 157 KAHglpgFAASSPqwslarpnePPWPGptlvAMDEEMRAWHEENQLPVFAYSSQARgffskraaggaedDSELRRV---Y 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 281366738 262 FSEG-------MKRLVKKYKRSASQIVLRYLI--DYGVVPIPKAANPIHIKENL 306
Cdd:cd19082 234 YSEEnferlerAKELAEEKGVSPTQIALAYVLnqPFPTVPIIGPRTPEQLRDSL 287
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
39-317 |
5.56e-17 |
|
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: 80.55 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 39 PKVRL-SSGHEMPVLGFGTYKLRGY--------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQIkmgnisR 106
Cdd:cd19145 1 PRVKLgSQGLEVSAQGLGCMGLSGDygapkpeeEGIALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGP------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 107 ENIFLTTKLWNT---------HHDPRDVRRICEKQLELLGFSYIDLYlmhfpvgYKYVCDeilmpmsgdelQTVEIDylD 177
Cdd:cd19145 75 EKVQLATKFGIHeiggsgvevRGDPAYVRAACEASLKRLDVDYIDLY-------YQHRID-----------TTVPIE--I 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 178 TWRAMENLVKLGMVRSIGLSNFNMEQIQRiiqCSSSKPVVN-QVE--IWPGFLQKDLVDYCRYNGIIVTAFSPLG----- 249
Cdd:cd19145 135 TMGELKKLVEEGKIKYIGLSEASADTIRR---AHAVHPITAvQLEwsLWTRDIEEEIIPTCRELGIGIVPYSPLGrgffa 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 250 -----------QPNRKNHcPvYFFSEGMKR----------LVKKYKRSASQIVLRYLIDYG--VVPIPKAANPIHIKENL 306
Cdd:cd19145 212 gkakleellenSDVRKSH-P-RFQGENLEKnkvlyerveaLAKKKGCTPAQLALAWVLHQGedVVPIPGTTKIKNLNQNI 289
|
330
....*....|.
gi 281366738 307 NIFDFKLDEAD 317
Cdd:cd19145 290 GALSVKLTKED 300
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
66-319 |
3.15e-16 |
|
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: 78.43 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 66 AAVHCAIETGFRHFDTA--Y-YYENEKEIGEALRTQikmgnisRENIFLTTKL-WNTHHD----------PRDVRRICEK 131
Cdd:cd19078 29 ELIRKAVELGITFFDTAevYgPYTNEELVGEALKPF-------RDQVVIATKFgFKIDGGkpgplgldsrPEHIRKAVEG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 132 QLELLGFSYIDLYlmhfpvgYKYVCDEilmpmsgdelqTVEIDylDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCS 211
Cdd:cd19078 102 SLKRLQTDYIDLY-------YQHRVDP-----------NVPIE--EVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 212 SSKPVVNQVEIWPGFLQKDLVDYCRYNGIIVTAFSPLGQ--------PNRK-----NHCPVYFFS-EGMK---RLVKKYK 274
Cdd:cd19078 162 PVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKgfltgkidENTKfdegdDRASLPRFTpEALEanqALVDLLK 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 281366738 275 RSA-------SQIVLRYLIDYG--VVPIPKAANPIHIKENLNIFDFKLDEADTR 319
Cdd:cd19078 242 EFAeekgatpAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEELR 295
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
66-321 |
3.21e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 78.53 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 66 AAVHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmgNISRENIFLTTKLWNTHHDPRD--VRRICEKQLELLGFSY 140
Cdd:cd19103 36 AVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLK------RYPREDYIISTKFTPQIAGQSAdpVADMLEGSLARLGTDY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 141 IDLYLMHFPVGYKYVCDEIlmpmsgdelqtveIDyldtwramenLVKLGMVRSIGLSNFNMEQIQR---IIQCS--SSKP 215
Cdd:cd19103 110 IDIYWIHNPADVERWTPEL-------------IP----------LLKSGKVKHVGVSNHNLAEIKRaneILAKAgvSLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 216 VVNQVE-IWPGFLQKDLVDYCRYNGIIVTAFSPL------GQPNRKNHCPVYF---------------FSEGMKRLVKKY 273
Cdd:cd19103 167 VQNHYSlLYRSSEEAGILDYCKENGITFFAYMVLeqgalsGKYDTKHPLPEGSgraetynpllpqleeLTAVMAEIGAKH 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 281366738 274 KRSASQIVLRYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19103 247 GASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKEL 294
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
68-321 |
5.28e-16 |
|
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: 77.84 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 68 VHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmgNISRENIFLTTK---LWNTH-----HDPRDVRRICEKQLELL 136
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLK------EYNRNEVVIATKgahKFGGDgsvlnNSPEFLRSAVEKSLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 137 GFSYIDLYLMHFPVGykyvcdeilmpmsgdelqtvEIDYLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRiiqcSSSKPV 216
Cdd:cd19083 113 NTDYIDLYYIHFPDG--------------------ETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE----ANKDGY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 217 VNQVEIWPGFLQ----KDLVDYCRYNGIIV------------------TAFSPLGQPNRKNHCPVYFFSEGMKRlVKKYK 274
Cdd:cd19083 169 VDVLQGEYNLLQreaeEDILPYCVENNISFipyfplasgllagkytkdTKFPDNDLRNDKPLFKGERFSENLDK-VDKLK 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 281366738 275 RSA-------SQIVLRYL-----IDygvVPIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19083 248 SIAdekgvtvAHLALAWYltrpaID---VVIPGAKRAEQVIDNLKALDVTLTEEEIAFI 303
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
71-321 |
8.75e-16 |
|
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: 77.27 E-value: 8.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 71 AIETGFRHFDTAYYY---ENEKEIGEALRTqikmgniSRENIFLTTKLWN-THHDPRDV----RRI---CEKQLELLGFS 139
Cdd:cd19091 48 ALDAGINFFDTADVYsegESEEILGKALKG-------RRDDVLIATKVRGrMGEGPNDVglsrHHIiraVEASLKRLGTD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 140 YIDLYLMHfpvGYkyvcdeilmpmsgDELQTVEidylDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCSS----SKP 215
Cdd:cd19091 121 YIDLYQLH---GF-------------DALTPLE----ETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISErrglARF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 216 VVNQV-------EiwpgfLQKDLVDYCRYNGIIVTAFSPL-----------GQPN-------RKNHCPVYFFSEG----- 265
Cdd:cd19091 181 VALQAyysllgrD-----LEHELMPLALDQGVGLLVWSPLaggllsgkyrrGQPApegsrlrRTGFDFPPVDRERgydvv 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 266 --MKRLVKKYKRSASQIVLRYLIDYGVVP--IPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19091 256 daLREIAKETGATPAQVALAWLLSRPTVSsvIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
50-316 |
1.34e-15 |
|
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: 76.05 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGT------YKLRGYQCS-AAVHCAIETGFRHFDTA-YYYENEKEIGEALRTqikmgnISRENIFLTTKLwNTHHD 121
Cdd:cd19090 1 SALGLGTaglggvFGGVDDDEAvATIRAALDLGINYIDTApAYGDSEERLGLALAE------LPREPLVLSTKV-GRLPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 PRD------VRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELQTVEIDYLDtwRAMENLVKL---GMVR 192
Cdd:cd19090 74 DTAdysadrVRRSVEESLERLGRDRIDLLMIHDP----------------ERVPWVDILAPG--GALEALLELkeeGLIK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 193 SIGLSNFNMEQIQRIIQ----------CSSSkpVVNQVEiwpgflQKDLVDYCRYNGIIVTAFSPLGQ-------PNRKN 255
Cdd:cd19090 136 HIGLGGGPPDLLRRAIEtgdfdvvltaNRYT--LLDQSA------ADELLPAAARHGVGVINASPLGMgllagrpPERVR 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281366738 256 HCPVYFF------SEGMKRLVKKYKRSASQIVLRYLI-DYGV-VPIPKAANPIHIKENLNIFDFKLDEA 316
Cdd:cd19090 208 YTYRWLSpelldrAKRLYELCDEHGVPLPALALRFLLrDPRIsTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
72-321 |
3.13e-15 |
|
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: 75.71 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 72 IETGFRHFDTAYYY----------ENEKEIGEALRTQIKmgnisRENIFLTTKL-WNTHHD-----PRDVRRICEKQLEL 135
Cdd:cd19081 36 VDAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRGK-----RDRVVIATKVgFPMGPNgpglsRKHIRRAVEASLRR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 136 LGFSYIDLYLMHFPvgykyvcDEilmpmsgdelqtvEIDYLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCSS--- 212
Cdd:cd19081 111 LQTDYIDLYQAHWD-------DP-------------ATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRqhg 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 213 -SKPVVNQVE---IWPGFLQKDLVDYCRYNGIIVTAFSPL------GQPNRKNHCPV---------YFFSEG-------M 266
Cdd:cd19081 171 lPRYVSLQPEynlVDRESFEGELLPLCREEGIGVIPYSPLaggfltGKYRSEADLPGstrrgeaakRYLNERglrildaL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 281366738 267 KRLVKKYKRSASQIVLRYLIDYGVV--PIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19081 251 DEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
67-324 |
2.50e-14 |
|
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: 73.01 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 67 AVHCAIETGFRHFDTAYYYENEKEIGEALRTQIKMGNISRENIFLTTKL----WNTHHDPRDVRRICEKQLELLGFSYID 142
Cdd:cd19101 28 AMAAYVDAGLTTFDCADIYGPAEELIGEFRKRLRRERDAADDVQIHTKWvpdpGELTMTRAYVEAAIDRSLKRLGVDRLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 143 LYLMHFpvgYKYvcdeilmpmsGDElqtveiDYLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIiqCSSSKPVV-NQVe 221
Cdd:cd19101 108 LVQFHW---WDY----------SDP------GYLDAAKHLAELQEEGKIRHLGLTNFDTERLREI--LDAGVPIVsNQV- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 222 iwpgflQ---------KDLVDYCRYNGIIVTAFSP----------LGQP----NRKNHCPVY-------------FFSE- 264
Cdd:cd19101 166 ------QyslldrrpeNGMAALCEDHGIKLLAYGTlaggllsekyLGVPeptgPALETRSLQkyklmidewggwdLFQEl 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281366738 265 --GMKRLVKKYKRSASQIVLRYLIDYGVV--PIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:cd19101 240 lrTLKAIADKHGVSIANVAVRWVLDQPGVagVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAV 303
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-306 |
4.40e-14 |
|
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: 72.35 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 52 LGFGTYKL-----RGYQCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQIKMGNISRENIFLTTK--LWNTHHD 121
Cdd:cd19099 6 LGLGTYRGdsddeTDEEYREALKAALDSGINVIDTAINYrggRSERLIGKALRELIEKGGIKRDEVVIVTKagYIPGDGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 122 PRDVRRI-------------------------------CEKQLELLGFSYIDLYLMHFPVGYkyvcdeiLMPMSGDEL-Q 169
Cdd:cd19099 86 EPLRPLKyleeklgrglidvadsaglrhcispayledqIERSLKRLGLDTIDLYLLHNPEEQ-------LLELGEEEFyD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 170 TVEidylDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCSSSKPVVN----------------QVEIWPGFLQ----- 228
Cdd:cd19099 159 RLE----EAFEALEEAVAEGKIRYYGISTWDGFRAPPALPGHLSLEKLVaaaeevggdnhhfkviQLPLNLLEPEaltek 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 229 -------KDLVDYCRYNGIIVTAFSPLGQPNRKnhcpvyffseGMKRLV----KKYKRSASQIVLRYLIDygvVPIPKAA 297
Cdd:cd19099 235 ntvkgeaLSLLEAAKELGLGVIASRPLNQGQLL----------GELRLAdllaLPGGATLAQRALQFARS---TPGVDSA 301
|
330
....*....|....
gi 281366738 298 -----NPIHIKENL 306
Cdd:cd19099 302 lvgmrRPEHVDENL 315
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
71-250 |
1.47e-12 |
|
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: 67.98 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 71 AIETGFRHFDTA----------YYYENEKEIGEALRTQikmGNisRENIFLTTK-----LWNTH-------HDPRDVRRI 128
Cdd:cd19094 27 AFDEGVNFIDTAemypvppspeTQGRTEEIIGSWLKKK---GN--RDKVVLATKvagpgEGITWprgggtrLDRENIREA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 129 CEKQLELLGFSYIDLYLMHFPVGYkyvcdeilMPMSG-------DELQTvEIDYLDTWRAMENLVKLGMVRSIGLSN--- 198
Cdd:cd19094 102 VEGSLKRLGTDYIDLYQLHWPDRY--------TPLFGggyytepSEEED-SVSFEEQLEALGELVKAGKIRHIGLSNetp 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366738 199 -----FNMEQIQ----RIIQCSSSKPVVNQ-VEIwpgflqkDLVDYCRYNGIIVTAFSPLGQ 250
Cdd:cd19094 173 wgvmkFLELAEQlglpRIVSIQNPYSLLNRnFEE-------GLAEACHRENVGLLAYSPLAG 227
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
63-248 |
2.21e-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: 67.29 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 63 QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQikmgnisRENIFLTTKLWNTHHDPRD----VRRICEKQLEL 135
Cdd:cd19104 33 EQIAAVRRALDLGINFFDTAPSYgdgKSEENLGRALKGL-------PAGPYITTKVRLDPDDLGDiggqIERSVEKSLKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 136 LGFSYIDLYLMHfpvgykyvcDEILMPMSGDELQTVEI-DYL---DTWRAMENLVKLGMVRSIGLSNFNMEQ-IQRIIQc 210
Cdd:cd19104 106 LKRDSVDLLQLH---------NRIGDERDKPVGGTLSTtDVLglgGVADAFERLRSEGKIRFIGITGLGNPPaIRELLD- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 281366738 211 sSSKPVVNQV--------------EIWPGFLQKDLVDYCRYNGIIVTAFSPL 248
Cdd:cd19104 176 -SGKFDAVQVyynllnpsaaearpRGWSAQDYGGIIDAAAEHGVGVMGIRVL 226
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
72-306 |
4.48e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 66.20 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 72 IETGFRHFDTAYYY----------ENEKEIGEALRTQikmGNisRENIFLTTKLW----NTHHDPRD--------VRRIC 129
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDR---GN--RDDVVIATKVGagprDPDGGPESpeglsaetIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 130 EKQLELLGFSYIDLYLMHfpvgykyvCDEILMPMSgdelqtveidylDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQ 209
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAH--------VDDRDTPLE------------ETLEAFNELVKAGKVRAIGASNFAAWRLERARQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 210 CSSSkpvvnqvEIWPGF--LQK---------------------DLVDYCRYNGII-VTAFSPL-----GQPNRKnhCPVY 260
Cdd:cd19752 162 IARQ-------QGWAEFsaIQQrhsylrprpgadfgvqrivtdELLDYASSRPDLtLLAYSPLlsgayTRPDRP--LPEQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 281366738 261 FFSEG-------MKRLVKKYKRSASQIVLRYLID--YGVVPIPKAANPIHIKENL 306
Cdd:cd19752 233 YDGPDsdarlavLEEVAGELGATPNQVVLAWLLHrtPAIIPLLGASTVEQLEENL 287
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
66-317 |
5.57e-12 |
|
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: 65.72 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 66 AAVHCAIETGFRHFDTAYYY------ENEKEIGEALRTQIKmgniSRENIFLTTK------LWNTHHDPRDVRRICEKQL 133
Cdd:cd19077 29 ETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPE----YADKVVLSVKggldpdTLRPDGSPEAVRKSIENIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 134 ELLGFS-YIDLYlmhfpvgykyVCDEIlmpmsgDELQTVEidylDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIiqcSS 212
Cdd:cd19077 105 RALGGTkKIDIF----------EPARV------DPNVPIE----ETIKALKELVKEGKIRGIGLSEVSAETIRRA---HA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 213 SKPVV-NQVEIWPGF---LQKDLVDYCRYNGIIVTAFSPLGQ-------------PNRKNHcpVYF--FSEG-------- 265
Cdd:cd19077 162 VHPIAaVEVEYSLFSreiEENGVLETCAELGIPIIAYSPLGRglltgriksladiPEGDFR--RHLdrFNGEnfeknlkl 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 281366738 266 ---MKRLVKKYKRSASQIVL---RYLIDYGVVPIPKAANPIHIKENLNIFDFKLDEAD 317
Cdd:cd19077 240 vdaLQELAEKKGCTPAQLALawiLAQSGPKIIPIPGSTTLERVEENLKAANVELTDEE 297
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
46-315 |
2.41e-11 |
|
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: 63.72 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 46 GHEMPVLGFGTYKLRGY-------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRtqikmgNISRENIFLTTK- 114
Cdd:cd19163 10 GLKVSKLGFGASPLGGVfgpvdeeEAIRTVHEALDSGINYIDTAPWYgqgRSETVLGKALK------GIPRDSYYLATKv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 -----LWNTHHD--PRDVRRICEKQLELLGFSYIDLYLMHfPVGYKYVCDEILmpmsgDElqtveidyldTWRAMENLVK 187
Cdd:cd19163 84 gryglDPDKMFDfsAERITKSVEESLKRLGLDYIDIIQVH-DIEFAPSLDQIL-----NE----------TLPALQKLKE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 188 LGMVRSIGLSNFNMEQIQRIIQCSSSKpvVNQVEIW-PGFLQ----KDLVDYCRYNGIIVTAFSPLG------QPNRKNH 256
Cdd:cd19163 148 EGKVRFIGITGYPLDVLKEVLERSPVK--IDTVLSYcHYTLNdtslLELLPFFKEKGVGVINASPLSmgllteRGPPDWH 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281366738 257 cPVyffSEGMKRLVKK---YKRSA----SQIVLRYLIDYGVVP--IPKAANPIHIKENLNIFDFKLDE 315
Cdd:cd19163 226 -PA---SPEIKEACAKaaaYCKSRgvdiSKLALQFALSNPDIAttLVGTASPENLRKNLEAAEEPLDA 289
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
50-209 |
1.29e-10 |
|
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: 61.86 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRG-------YQCSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRTQikmgniSRENIFLTTKL---- 115
Cdd:cd19152 1 PKLGFGTAPLGNlyeavsdEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALREL------GREDYVISTKVgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 116 --------------WNT-HHDPR-D-----VRRICEKQLELLGFSYIDLYLMHFPvgykyvcDEilmPMSGDE-LQTVEI 173
Cdd:cd19152 75 vplqeveptfepgfWNPlPFDAVfDysydgILRSIEDSLQRLGLSRIDLLSIHDP-------DE---DLAGAEsDEHFAQ 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 281366738 174 DYLDTWRAMENLVKLGMVRSIGL-SNFnMEQIQRIIQ 209
Cdd:cd19152 145 AIKGAFRALEELREEGVIKAIGLgVND-WEVILRILE 180
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
75-249 |
1.31e-10 |
|
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: 61.80 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 75 GFRHFDTAYYY---ENEKEIGEALRTQikmgnisrENIFLTTK---LWNTHHDPRDVRRICEKQLELLGFSYIDLYLMHF 148
Cdd:cd19075 33 GHTEIDTARVYpdgTSEELLGELGLGE--------RGFKIDTKanpGVGGGLSPENVRKQLETSLKRLKVDKVDVFYLHA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 149 PvgykyvcdeilmpmsgDELQTVEidylDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQ-CSSS---KPVVNQ----- 219
Cdd:cd19075 105 P----------------DRSTPLE----ETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEiCKENgwvLPTVYQgmyna 164
|
170 180 190
....*....|....*....|....*....|....
gi 281366738 220 ----VEiwpgflqKDLVDYCRYNGIIVTAFSPLG 249
Cdd:cd19075 165 itrqVE-------TELFPCLRKLGIRFYAYSPLA 191
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
79-321 |
3.78e-10 |
|
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: 60.31 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 79 FDTAYYYEN---EKEIGEALRTqikmgniSRENIFLTTKL-WNTHH-DP-------RDVRRICEKQLELLGFSYIDLYLM 146
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKYtMNRRPgDPnaggnhrKNLRRSVEASLRRLQTDYIDLLYV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 147 HFPvgykyvcdeilmpmsgDELQTVEidylDTWRAMENLVKLGMVRSIGLSNF---NMEQIQRIIQCSSSKPVVN-QVE- 221
Cdd:cd19080 121 HAW----------------DFTTPVE----EVMRALDDLVRAGKVLYVGISDTpawVVARANTLAELRGWSPFVAlQIEy 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 222 --IWPGFlQKDLVDYCRYNGIIVTAFSPLG------------QPNRKNHCPVYF----FSEGMKRLVKKYK-------RS 276
Cdd:cd19080 181 slLERTP-ERELLPMARALGLGVTPWSPLGgglltgkyqrgeEGRAGEAKGVTVgfgkLTERNWAIVDVVAavaeelgRS 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 281366738 277 ASQIVLRYLID-YGVV-PIPKAANPIHIKENLNIFDFKLDEADTRLL 321
Cdd:cd19080 260 AAQVALAWVRQkPGVViPIIGARTLEQLKDNLGALDLTLSPEQLARL 306
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
45-250 |
1.15e-09 |
|
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: 58.81 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 45 SGHEMPVLGFGTYKLRGYQ-----CSAAVHCAIETGFRHFDTAYYY-----ENEKEIGEALRTQIKMgniSRENIFLTTK 114
Cdd:cd19089 7 SGLHLPAISLGLWHNFGDYtspeeARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVISTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 LWNTHHDP--------RDVRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmsgDELQTVEidylDTWRAMENLV 186
Cdd:cd19089 84 AGYGMWPGpygdggsrKYLLASLDQSLKRMGLDYVDIFYHHRY----------------DPDTPLE----ETMTALADAV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366738 187 KLGMVRSIGLSNFNMEQIQRIIQCSSS---KPVVNQVEI-----WPgflQKDLVDYCRYNGIIVTAFSPLGQ 250
Cdd:cd19089 144 RSGKALYVGISNYPGAKARRAIALLRElgvPLIIHQPRYslldrWA---EDGLLEVLEEAGIGFIAFSPLAQ 212
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
71-310 |
1.32e-09 |
|
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: 58.31 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 71 AIETGFRHFDTAYYYEN-EKEIGEALrtqikmgnISRENIFLTTKL----WNTHHDPRDVRRICEKQLELLGFSYIDLYL 145
Cdd:cd19097 35 ALKAGINTLDTAPAYGDsEKVLGKFL--------KRLDKFKIITKLpplkEDKKEDEAAIEASVEASLKRLKVDSLDGLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 146 MHfpvgykyvcDEILMPMSGDELqtveidyldtWRAMENLVKLGMVRSIGLSNFNMEQIQRIIqcSSSKPVVNQVE---- 221
Cdd:cd19097 107 LH---------NPDDLLKHGGKL----------VEALLELKKEGLIRKIGVSVYSPEELEKAL--ESFKIDIIQLPfnil 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 222 ----IWPGFLQKdLVDycryNGIIVTAFSPLGQP---NRKNHCPVYF--FSEGMKRL---VKKYKRSASQIVLRYL---- 285
Cdd:cd19097 166 dqrfLKSGLLAK-LKK----KGIEIHARSVFLQGlllMEPDKLPAKFapAKPLLKKLhelAKKLGLSPLELALGFVlslp 240
|
250 260
....*....|....*....|....*.
gi 281366738 286 -IDYGVVPIpkaANPIHIKENLNIFD 310
Cdd:cd19097 241 eIDKIVVGV---DSLEQLKEIIAAFK 263
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
50-248 |
5.66e-09 |
|
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: 56.60 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRGY------QCSAAVHCAIETGFRHFDTAYYY---ENEKEIGEALRTQikmgniSRENIFLTTKLWNTHH 120
Cdd:cd19162 1 PRLGLGAASLGNLaragedEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARH------PRAEYVVSTKVGRLLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 121 DPRD----------------VRRICEKQLELLGFSYIDLYLMHFPvgykyvcdeilmpmSGDELQTVEidylDTWRAMEN 184
Cdd:cd19162 75 PGAAgrpagadrrfdfsadgIRRSIEASLERLGLDRLDLVFLHDP--------------DRHLLQALT----DAFPALEE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 185 LVKLGMVRSIGLSNFNMEQIQRIIQCSsskpVVNQVEIWPGFL------QKDLVDYCRYNGIIVTAFSPL 248
Cdd:cd19162 137 LRAEGVVGAIGVGVTDWAALLRAARRA----DVDVVMVAGRYTlldrraATELLPLCAAKGVAVVAAGVF 202
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
67-207 |
1.27e-07 |
|
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: 52.66 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 67 AVHCAIETGFRHFDTA-YYYENEKEIGEALrtQIKMGNISRENIFLTTK-----LWNTHHDPRDVRRICEKQLELLGFSY 140
Cdd:cd19164 39 IVRRALELGIRAFDTSpYYGPSEIILGRAL--KALRDEFPRDTYFIITKvgrygPDDFDYSPEWIRASVERSLRRLHTDY 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 141 IDLYLMHfpvGYKYVCDEilmpmsgdelqtveidylDTWRAMENLVKL---GMVRSIGLSNFNMEQIQRI 207
Cdd:cd19164 117 LDLVYLH---DVEFVADE------------------EVLEALKELFKLkdeGKIRNVGISGYPLPVLLRL 165
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
45-249 |
4.53e-06 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 48.31 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 45 SGHEMPVLGFGTYKLrGYQCSAA-VHC----AIETGFRHFDTAYYYE----------NEKEIGEALRtqiKMGNisRENI 109
Cdd:PRK10625 9 SSLEVSTLGLGTMTF-GEQNSEAdAHAqldyAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLA---KRGS--REKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 110 FLTTKLW------------NTHHDPRDVRRICEKQLELLGFSYIDLYLMHFP---------VGYKYVcdeilmpmsgDEL 168
Cdd:PRK10625 83 IIASKVSgpsrnndkgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptncfgkLGYSWT----------DSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 169 QTVEIdyLDTWRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCSSSKPVVNQVEIWPGF------LQKDLVDYCRYNGIIV 242
Cdd:PRK10625 153 PAVSL--LETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYsllnrsFEVGLAEVSQYEGVEL 230
|
....*..
gi 281366738 243 TAFSPLG 249
Cdd:PRK10625 231 LAYSCLA 237
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
52-249 |
1.55e-05 |
|
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: 46.37 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 52 LGFGTYKLRG-YQCSAAVHCAIET-------GFRHFDTAYYYEN---EKEIGEALRTQikmgNISRENIFLTTKLW---- 116
Cdd:cd19153 15 VGLGTAALGGvYGDGLEQDEAVAIvaeafaaGINHFDTSPYYGAessEAVLGKALAAL----QVPRSSYTVATKVGryrd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 117 NTHHDPRD-VRRICEKQLELLGFSYIDLYLMH---FpVGYKYVCDEIlmpmsgdelqtveIDYLDTWRAMenlvklGMVR 192
Cdd:cd19153 91 SEFDYSAErVRASVATSLERLHTTYLDVVYLHdieF-VDYDTLVDEA-------------LPALRTLKDE------GVIK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366738 193 SIGLSNFNMEQIQRIIQ-CSSSKPVVNQVEIWPGFLQKDLVDYCRY----NGIIVTAFSPLG 249
Cdd:cd19153 151 RIGIAGYPLDTLTRATRrCSPGSLDAVLSYCHLTLQDARLESDAPGlvrgAGPHVINASPLS 212
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
45-250 |
4.52e-05 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 44.98 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 45 SGHEMPVLGFGTYKLRGYQCS-----AAVHCAIETGFRHFDTAYYY-----ENEKEIGEALRTQIKMgniSRENIFLTTK 114
Cdd:PRK09912 21 SGLRLPALSLGLWHNFGHVNAlesqrAILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAA---YRDELIISTK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 ----LWNTHHDPRDVRRIC----EKQLELLGFSYIDLYlmhfpvgYKYVCDEIlMPMSgdelqtveidylDTWRAMENLV 186
Cdd:PRK09912 98 agydMWPGPYGSGGSRKYLlaslDQSLKRMGLEYVDIF-------YSHRVDEN-TPME------------ETASALAHAV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281366738 187 KLGMVRSIGLSNFNMEQIQRIIQCSSS--------KPVVNQVEIWPGflQKDLVDYCRYNGIIVTAFSPLGQ 250
Cdd:PRK09912 158 QSGKALYVGISSYSPERTQKMVELLREwkipllihQPSYNLLNRWVD--KSGLLDTLQNNGVGCIAFTPLAQ 227
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
44-237 |
3.20e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 42.07 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 44 SSGHEMPVLGFGTYKLR---GY----QCSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRTQikmgNISRENIFLTT 113
Cdd:PLN02587 6 STGLKVSSVGFGASPLGsvfGPvseeDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKAL----GIPREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 114 KLwNTHHDPRD-----VRRICEKQLELLGFSYIDLYLMHfpvgykyvcdeilmpmsgdelqTVEIDYLD-----TWRAME 183
Cdd:PLN02587 82 KC-GRYGEGFDfsaerVTKSVDESLARLQLDYVDILHCH----------------------DIEFGSLDqivneTIPALQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 281366738 184 NLVKLGMVRSIGLSNFNMeqiqriiqcSSSKPVVNQVEiwPGFLqkDLV-DYCRY 237
Cdd:PLN02587 139 KLKESGKVRFIGITGLPL---------AIFTYVLDRVP--PGTV--DVIlSYCHY 180
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
50-196 |
5.32e-04 |
|
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: 41.54 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 50 PVLGFGTYKLRGY-------QCSAAVHCAIETGFRHFDTAYYYEN---EKEIGEALRtqikmgNISRENIFLTTK----- 114
Cdd:cd19161 1 SELGLGTAGLGNLytavsnaDADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLR------EKPRDEFVLSTKvgrll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 115 ---------LWNTHHDP----------RD-VRRICEKQLELLGFSYIDLYLMHfPVGYKYvcdeilmpmSGDELQTVEiD 174
Cdd:cd19161 75 kparegsvpDPNGFVDPlpfeivydysYDgIMRSFEDSLQRLGLNRIDILYVH-DIGVYT---------HGDRKERHH-F 143
|
170 180
....*....|....*....|....*
gi 281366738 175 YLDT---WRAMENLVKLGMVRSIGL 196
Cdd:cd19161 144 AQLMsggFKALEELKKAGVIKAFGL 168
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
71-324 |
1.09e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 40.34 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 71 AIETGFRHFDTAYYY----ENEKeIGEALRTQikmgnisRENIFLTTKL---------WNTHHDPRDVRRICEKQLELLG 137
Cdd:PRK10376 49 AVALGVNHIDTSDFYgphvTNQL-IREALHPY-------PDDLTIVTKVgarrgedgsWLPAFSPAELRRAVHDNLRNLG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 138 FSYID---LYLMHFPVGykyvcdeilmPMSGdelqTVEidyldtwRAMENLVKL---GMVRSIGLSNFNMEQI---QRI- 207
Cdd:PRK10376 121 LDVLDvvnLRLMGDGHG----------PAEG----SIE-------EPLTVLAELqrqGLVRHIGLSNVTPTQVaeaRKIa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 208 -IQCssskpVVNQVEIwpgfLQKD---LVDYCRYNGIIVTAFSPLG-----QpnrknhcpvyffSEGMKRLVKKYKRSAS 278
Cdd:PRK10376 180 eIVC-----VQNHYNL----AHRAddaLIDALARDGIAYVPFFPLGgftplQ------------SSTLSDVAASLGATPM 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 281366738 279 QIVLRYLIDYG--VVPIPKAANPIHIKENLNIFDFKLDEADTRLLRGI 324
Cdd:PRK10376 239 QVALAWLLQRSpnILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGI 286
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
70-221 |
6.54e-03 |
|
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: 38.35 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 70 CAIETGFRHFDTAYYYEN---EKEIGEAlrtqIKMGNISRENIFLTTKL-WNTHHDPRDVRRI--------CEKQLELLG 137
Cdd:cd19143 39 AAYDAGVNFFDNAEVYANgqsEEIMGQA----IKELGWPRSDYVVSTKIfWGGGGPPPNDRGLsrkhivegTKASLKRLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281366738 138 FSYIDLYLMHFPvgykyvcdEILMPMSgdelQTVeidyldtwRAMENLVKLGMVRSIGLSNFNMEQIQRIIQCSSS---- 213
Cdd:cd19143 115 LDYVDLVFCHRP--------DPATPIE----ETV--------RAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRlgli 174
|
....*...
gi 281366738 214 KPVVNQVE 221
Cdd:cd19143 175 PPVMEQPQ 182
|
|
| |
