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Conserved domains on  [gi|112489859]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
9-350 0e+00

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member cd04736:

Pssm-ID: 419668  Cd Length: 361  Bit Score: 649.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   9 EDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWP 88
Cdd:cd04736    1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  89 KGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRERD 168
Cdd:cd04736   81 NGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVHRELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 169 LHNRFKIP--------------PFLTLKNFEGIDLGK-----MDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLL 229
Cdd:cd04736  161 LRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQLanfasDDAIDVEVQAALMSRQMDASFNWQDLRWLRDLWPHKLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 230 VKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGRA 309
Cdd:cd04736  241 VKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGRA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 112489859 310 TLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSP 350
Cdd:cd04736  321 TLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
 
Name Accession Description Interval E-value
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
9-350 0e+00

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 649.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   9 EDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWP 88
Cdd:cd04736    1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  89 KGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRERD 168
Cdd:cd04736   81 NGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVHRELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 169 LHNRFKIP--------------PFLTLKNFEGIDLGK-----MDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLL 229
Cdd:cd04736  161 LRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQLanfasDDAIDVEVQAALMSRQMDASFNWQDLRWLRDLWPHKLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 230 VKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGRA 309
Cdd:cd04736  241 VKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGRA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 112489859 310 TLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSP 350
Cdd:cd04736  321 TLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
FMN_dh pfam01070
FMN-dependent dehydrogenase.
16-354 7.04e-159

FMN-dependent dehydrogenase.


Pssm-ID: 376451  Cd Length: 348  Bit Score: 449.68  E-value: 7.04e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   16 QKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWPKGDLALA 95
Cdd:pfam01070   1 RKRLPKFAFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   96 RAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVIH-REIAQGMVLKALHTGYTTLVLTTDVAVNGYRERDLHNRFK 174
Cdd:pfam01070  81 RAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRdREITEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGFT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  175 IPPFLTLKNFE------GIDLGKMDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAEGAD 248
Cdd:pfam01070 161 LPPRLTPRNLLdlalhpRWALGVLGGKDASGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  249 GVILSNHGGRQLDCAISPMEVLAQSVAKTGK--PVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEVL 326
Cdd:pfam01070 241 GIVVSNHGGRQLDGAPATIDALPEIVAAVGGriPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHAL 320
                         330       340
                  ....*....|....*....|....*...
gi 112489859  327 TLLKADIDRTLAQIGCPDITSLSPDYLQ 354
Cdd:pfam01070 321 EILRDELERTMALLGCTSIADLTPSLLR 348
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
8-353 8.05e-98

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only];


Pssm-ID: 224223  Cd Length: 360  Bit Score: 294.96  E-value: 8.05e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   8 VEDYRKLAQKRLPKmVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALW 87
Cdd:COG1304    1 VADLRRAAQRRLPK-AFHYIDGGAEDEVTLRRNREAFEDIALRPRVLPEVDDIDLSTTFLGQKLSAPIIIAPMTGGGLAH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  88 PKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDgdlwFQLYV-IHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRE 166
Cdd:COG1304   80 PEGEVINAKLAAAAGEPFILSTVGSQRIEEVAAAPP----FQLYFsKDREFAPNLVDRAANAGAKQLVLTVDSPVGGERE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 167 RDLHNRFKIPPFLTLKNFEGIDLG----KMDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRC 242
Cdd:COG1304  156 RDAVNGISAPALAIHLNVLQEATQpegdRDGKGGLDSIAEYVSALSVPVISKEDGAGISKEWAGPLVLKGILAPEDAAGA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 243 IAEGADGVILSNHGGRQLDCAISPMEVL--AQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGET 320
Cdd:COG1304  236 GGTGADGIEVSNHGGRQLDWGISTADSLpeIVEAVGDRIEVIADGGIRSGLDVAKALALGADAVGIGRPFLYGLAAGGEA 315
                        330       340       350
                 ....*....|....*....|....*....|...
gi 112489859 321 GVDEVLTLLKADIDRTLAQIGCPDITSLSPDYL 353
Cdd:COG1304  316 GVERVLEIIRKELKIAMALTGAKNIEELKRVPL 348
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
7-356 2.65e-97

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134  Cd Length: 367  Bit Score: 293.95  E-value: 2.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   7 NVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGAL 86
Cdd:PLN02493   5 NVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  87 WPKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVI-HREIAQGMVLKALHTGYTTLVLTTDVAVNGYR 165
Cdd:PLN02493  85 HPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYkNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 166 ERDLHNRFKIPPFLTLKNFEGIDLGKMDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAE 245
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 246 GADGVILSNHGGRQLDCAISPMEVLAQSVAKT-GK-PVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVD 323
Cdd:PLN02493 245 GAAGIIVSNHGARQLDYVPATISALEEVVKATqGRiPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVR 324
                        330       340       350
                 ....*....|....*....|....*....|...
gi 112489859 324 EVLTLLKADIDRTLAQIGCPDITSLSPDYLQNE 356
Cdd:PLN02493 325 KVLQMLRDEFELTMALSGCRSLKEISRNHITTE 357
actino_HemFlav TIGR03966
heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an ...
8-351 1.63e-59

heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an N-terminal heme-binding domain and C-terminal flavodehydrogenase domain, and share homology to yeast flavocytochrome b2, to E. coli L-lactate dehydrogenase [cytochrome], to (S)-mandelate dehydrogenase, etc. This enzyme appears only in the context of the mycofactocin system. Interestingly, it is absent from the four species detected so far with mycofactocin but without an F420 biosynthesis system.


Pssm-ID: 274885  Cd Length: 385  Bit Score: 197.29  E-value: 1.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859    8 VEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPkRLVDVS-RRSLQAEVLGKRQSMPLLIGPTALNgAL 86
Cdd:TIGR03966   8 VAEAQRRARKRLPRSVYAALIAGTEKGVTLADNVAAFDELGFRP-HVAGLPpKRELSTTVMGQEISFPVLISPTGVQ-AV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   87 WPKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDgDLWFQLY-VIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYR 165
Cdd:TIGR03966  86 HPDGEVAVARAAAARGTAMGLSSFASKPVEEVVAANP-KTFFQIYwVGSRDDILARLERARAAGAKGLILTLDWSFASRR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  166 --------ER-DLHNRFKIPPFLTLKN------FEGIDLGKMDKANLEMQAALMSRQMDASF--------NWEALRWLRD 222
Cdd:TIGR03966 165 dwgspeipEKiDLRTMLRFAPEVLVRPgwllryLRSGRIPDLTVPNLALRGETPPTFFGAYGewmgtpppTWEDVAWLRE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  223 LWPHKLLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGK--PVLIDSGFRRGSDIVKALALG 300
Cdd:TIGR03966 245 QWGGPFMLKGITRPDDARRAVDAGATAISVSNHGGNNLDGTPAAIRALPAIAEAVGDqvEVLLDGGIRRGSDVVKALALG 324
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 112489859  301 AEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPD 351
Cdd:TIGR03966 325 ARAVMIGRAYLWGLAANGEAGVENVLDILRQGIDSALLGLGKASVHELSRE 375
 
Name Accession Description Interval E-value
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
9-350 0e+00

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 649.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   9 EDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWP 88
Cdd:cd04736    1 EDYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  89 KGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRERD 168
Cdd:cd04736   81 NGDLALARAAAKAGIPFVLSTASNMSIEDVARQADGDLWFQLYVVHRELAELLVKRALAAGYTTLVLTTDVAVNGYRERD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 169 LHNRFKIP--------------PFLTLKNFEGIDLGK-----MDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLL 229
Cdd:cd04736  161 LRNGFAIPfrytprvlldgilhPRWLLRFLRNGMPQLanfasDDAIDVEVQAALMSRQMDASFNWQDLRWLRDLWPHKLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 230 VKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGRA 309
Cdd:cd04736  241 VKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGRA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 112489859 310 TLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSP 350
Cdd:cd04736  321 TLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
FMN_dh pfam01070
FMN-dependent dehydrogenase.
16-354 7.04e-159

FMN-dependent dehydrogenase.


Pssm-ID: 376451  Cd Length: 348  Bit Score: 449.68  E-value: 7.04e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   16 QKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWPKGDLALA 95
Cdd:pfam01070   1 RKRLPKFAFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELALA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   96 RAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVIH-REIAQGMVLKALHTGYTTLVLTTDVAVNGYRERDLHNRFK 174
Cdd:pfam01070  81 RAAAAAGIPFVLSTVSSTSLEEVAAAAGGPLWFQLYVPRdREITEDLLERAEAAGYKALVLTVDTPVLGRRERDLRNGFT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  175 IPPFLTLKNFE------GIDLGKMDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAEGAD 248
Cdd:pfam01070 161 LPPRLTPRNLLdlalhpRWALGVLGGKDASGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEAGVD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  249 GVILSNHGGRQLDCAISPMEVLAQSVAKTGK--PVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEVL 326
Cdd:pfam01070 241 GIVVSNHGGRQLDGAPATIDALPEIVAAVGGriPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGGEAGVAHAL 320
                         330       340
                  ....*....|....*....|....*...
gi 112489859  327 TLLKADIDRTLAQIGCPDITSLSPDYLQ 354
Cdd:pfam01070 321 EILRDELERTMALLGCTSIADLTPSLLR 348
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
9-350 3.49e-141

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203  Cd Length: 299  Bit Score: 402.98  E-value: 3.49e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   9 EDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWP 88
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  89 KGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYV-IHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRer 167
Cdd:cd02809   81 DGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPRWFQLYVpRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 168 dlhnrfkippfltlknfegidlgkmdkanlemqaalmsrqmdasFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAEGA 247
Cdd:cd02809  159 --------------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGA 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 248 DGVILSNHGGRQLDCAISPMEVLAQSVAKTGK--PVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEV 325
Cdd:cd02809  195 DGIVVSNHGGRQLDGAPATIDALPEIVAAVGGriEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHV 274
                        330       340
                 ....*....|....*....|....*
gi 112489859 326 LTLLKADIDRTLAQIGCPDITSLSP 350
Cdd:cd02809  275 LEILRDELERAMALLGCASLADLDP 299
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
6-353 5.76e-101

L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.


Pssm-ID: 239448  Cd Length: 383  Bit Score: 303.82  E-value: 5.76e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   6 FNVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGA 85
Cdd:cd03332   19 VDPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQEL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  86 LWPKGDLALARAATKAGIPFVLSTASNMSIEDLARQC-DGDLWFQLY-VIHREIAQGMVLKALHTGYTTLVLTTDVAVNG 163
Cdd:cd03332   99 FHPDAELATARAAAELGVPYILSTASSSSIEDVAAAAgDAPRWFQLYwPKDDDLTESLLRRAEKAGYRVLVVTLDTWSLG 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 164 YRERDLHNRFKipPFLT-------------LKNFEGiDLGKMDKANLEMQAALMSRQM---DASFNWEALRWLRDLWPHK 227
Cdd:cd03332  179 WRPRDLDLGYL--PFLRgigianyfsdpvfRKKLAE-PVGEDPEAPPPMEAAVARFVSvfsGPSLTWEDLAFLREWTDLP 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 228 LLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTG--KPVLIDSGFRRGSDIVKALALGAEAVL 305
Cdd:cd03332  256 IVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGdrLTVLFDSGVRTGADIMKALALGAKAVL 335
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 112489859 306 LGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPDYL 353
Cdd:cd03332  336 IGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
8-353 8.05e-98

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only];


Pssm-ID: 224223  Cd Length: 360  Bit Score: 294.96  E-value: 8.05e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   8 VEDYRKLAQKRLPKmVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALW 87
Cdd:COG1304    1 VADLRRAAQRRLPK-AFHYIDGGAEDEVTLRRNREAFEDIALRPRVLPEVDDIDLSTTFLGQKLSAPIIIAPMTGGGLAH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  88 PKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDgdlwFQLYV-IHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRE 166
Cdd:COG1304   80 PEGEVINAKLAAAAGEPFILSTVGSQRIEEVAAAPP----FQLYFsKDREFAPNLVDRAANAGAKQLVLTVDSPVGGERE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 167 RDLHNRFKIPPFLTLKNFEGIDLG----KMDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRC 242
Cdd:COG1304  156 RDAVNGISAPALAIHLNVLQEATQpegdRDGKGGLDSIAEYVSALSVPVISKEDGAGISKEWAGPLVLKGILAPEDAAGA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 243 IAEGADGVILSNHGGRQLDCAISPMEVL--AQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGET 320
Cdd:COG1304  236 GGTGADGIEVSNHGGRQLDWGISTADSLpeIVEAVGDRIEVIADGGIRSGLDVAKALALGADAVGIGRPFLYGLAAGGEA 315
                        330       340       350
                 ....*....|....*....|....*....|...
gi 112489859 321 GVDEVLTLLKADIDRTLAQIGCPDITSLSPDYL 353
Cdd:COG1304  316 GVERVLEIIRKELKIAMALTGAKNIEELKRVPL 348
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
7-356 2.65e-97

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134  Cd Length: 367  Bit Score: 293.95  E-value: 2.65e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   7 NVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGAL 86
Cdd:PLN02493   5 NVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  87 WPKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVI-HREIAQGMVLKALHTGYTTLVLTTDVAVNGYR 165
Cdd:PLN02493  85 HPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYkNRNVVEQLVRRAERAGFKAIALTVDTPRLGRR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 166 ERDLHNRFKIPPFLTLKNFEGIDLGKMDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAE 245
Cdd:PLN02493 165 ESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 246 GADGVILSNHGGRQLDCAISPMEVLAQSVAKT-GK-PVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVD 323
Cdd:PLN02493 245 GAAGIIVSNHGARQLDYVPATISALEEVVKATqGRiPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVR 324
                        330       340       350
                 ....*....|....*....|....*....|...
gi 112489859 324 EVLTLLKADIDRTLAQIGCPDITSLSPDYLQNE 356
Cdd:PLN02493 325 KVLQMLRDEFELTMALSGCRSLKEISRNHITTE 357
PLN02535 PLN02535
glycolate oxidase
1-356 3.59e-96

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 290.97  E-value: 3.59e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   1 MSQNLFNVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPT 80
Cdd:PLN02535   1 MADEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  81 ALNGALWPKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVI-HREIAQGMVLKALHTGYTTLVLTTDV 159
Cdd:PLN02535  81 AMHKLAHPEGEIATARAAAACNTIMVLSFMASCTVEEVASSCNAVRFLQLYVYkRRDIAAQLVQRAEKNGYKAIVLTADV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 160 AVNGYRERDLHNRFKIPpflTLKNFEGI---DLGKMDKANLEmqaALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSA 236
Cdd:PLN02535 161 PRLGRREADIKNKMISP---QLKNFEGLlstEVVSDKGSGLE---AFASETFDASLSWKDIEWLRSITNLPILIKGVLTR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 237 EDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGK--PVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGL 314
Cdd:PLN02535 235 EDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGrvPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGL 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 112489859 315 AARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPDYLQNE 356
Cdd:PLN02535 315 AAKGEDGVRKVIEMLKDELEITMALSGCPSVKDITRSHVRTE 356
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
10-350 7.22e-95

Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.


Pssm-ID: 239238  Cd Length: 344  Bit Score: 286.80  E-value: 7.22e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  10 DYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWPK 89
Cdd:cd02922    2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  90 GDLALARAATKAGIPFVLSTASNMSIEDL--ARQCDGDLWFQLYV-IHREIAQGMVLKALHTGYTTLVLTTDVAVNGYRE 166
Cdd:cd02922   82 GELNLARAAGKHGILQMISTNASCSLEEIvdARPPDQPLFFQLYVnKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 167 RDLhnRFKippfLTLKNFEGIDlGKMDKANLEMQAALMSRQMDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAEG 246
Cdd:cd02922  162 RDE--RLK----AEEAVSDGPA-GKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 247 ADGVILSNHGGRQLDCAISPMEVLAQsvAKTGKP-------VLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGE 319
Cdd:cd02922  235 VDGIVLSNHGGRQLDTAPAPIEVLLE--IRKHCPevfdkieVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGE 312
                        330       340       350
                 ....*....|....*....|....*....|.
gi 112489859 320 TGVDEVLTLLKADIDRTLAQIGCPDITSLSP 350
Cdd:cd02922  313 EGVEKAIQILKDEIETTMRLLGVTSLDQLGP 343
lldD PRK11197
L-lactate dehydrogenase; Provisional
10-353 1.64e-81

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 253.79  E-value: 1.64e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  10 DYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWPK 89
Cdd:PRK11197   8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  90 GDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWFQLYVIH-REIAQGMVLKALHTGYTTLVLTTDVAVNGYRERD 168
Cdd:PRK11197  88 GEVQAARAADAKGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRdRGFMRNALERAKAAGCSTLVFTVDMPVPGARYRD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 169 LHNRFKIPPFLTLKNFEGI----------------DLGKM-----DKANLEMQAALMSRQMDASFNWEALRWLRDLWPHK 227
Cdd:PRK11197 168 AHSGMSGPNAAMRRYLQAVthpqwawdvglngrphDLGNIsaylgKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDGP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 228 LLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVL---AQSVaKTGKPVLIDSGFRRGSDIVKALALGAEAV 304
Cdd:PRK11197 248 MVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALpaiADAV-KGDITILADSGIRNGLDVVRMIALGADTV 326
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 112489859 305 LLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPDYL 353
Cdd:PRK11197 327 LLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
PLN02979 PLN02979
glycolate oxidase
49-356 3.85e-80

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 250.02  E-value: 3.85e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  49 FKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGALWPKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGDLWF 128
Cdd:PLN02979  46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFF 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 129 QLYVI-HREIAQGMVLKALHTGYTTLVLTTDVAVNGYRERDLHNRFKIPPFLTLKNFEGIDLGKMDKANLEMQAALMSRQ 207
Cdd:PLN02979 126 QLYVYkNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTLPPNLTLKNFEGLDLGKMDEANDSGLASYVAGQ 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 208 MDASFNWEALRWLRDLWPHKLLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKT-GK-PVLIDS 285
Cdd:PLN02979 206 IDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATqGRiPVFLDG 285
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 112489859 286 GFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPDYLQNE 356
Cdd:PLN02979 286 GVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHITTE 356
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
7-349 3.54e-76

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088  Cd Length: 351  Bit Score: 239.27  E-value: 3.54e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   7 NVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALNGAL 86
Cdd:cd04737    7 NLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  87 WPKGDLALARAATKAGIPFVLSTASNMSIEDLAR-QCDGDLWFQLYV-----IHREIAQgmvlKALHTGYTTLVLTTDVA 160
Cdd:cd04737   87 HATGEVATARGMAEVGSLFSISTYSNTSLEEIAKaSNGGPKWFQLYMskddgFNRSLLD----RAKAAGAKAIILTADAT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 161 VNGYRERDLHNRFKIP---PFLTlKNFEGIDLGKMDKanlEMQAALMSRqmdasFNWEALRWLRDLWPHKLLVKGLLSAE 237
Cdd:cd04737  163 VGGNREADIRNKFQFPfgmPNLN-HFSEGTGKGKGIS---EIYAAAKQK-----LSPADIEFIAKISGLPVIVKGIQSPE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 238 DADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGK--PVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLA 315
Cdd:cd04737  234 DADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHrvPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLA 313
                        330       340       350
                 ....*....|....*....|....*....|....
gi 112489859 316 ARGETGVDEVLTLLKADIDRTLAQIGCPDITSLS 349
Cdd:cd04737  314 LGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVK 347
actino_HemFlav TIGR03966
heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an ...
8-351 1.63e-59

heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an N-terminal heme-binding domain and C-terminal flavodehydrogenase domain, and share homology to yeast flavocytochrome b2, to E. coli L-lactate dehydrogenase [cytochrome], to (S)-mandelate dehydrogenase, etc. This enzyme appears only in the context of the mycofactocin system. Interestingly, it is absent from the four species detected so far with mycofactocin but without an F420 biosynthesis system.


Pssm-ID: 274885  Cd Length: 385  Bit Score: 197.29  E-value: 1.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859    8 VEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPkRLVDVS-RRSLQAEVLGKRQSMPLLIGPTALNgAL 86
Cdd:TIGR03966   8 VAEAQRRARKRLPRSVYAALIAGTEKGVTLADNVAAFDELGFRP-HVAGLPpKRELSTTVMGQEISFPVLISPTGVQ-AV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   87 WPKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDgDLWFQLY-VIHREIAQGMVLKALHTGYTTLVLTTDVAVNGYR 165
Cdd:TIGR03966  86 HPDGEVAVARAAAARGTAMGLSSFASKPVEEVVAANP-KTFFQIYwVGSRDDILARLERARAAGAKGLILTLDWSFASRR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  166 --------ER-DLHNRFKIPPFLTLKN------FEGIDLGKMDKANLEMQAALMSRQMDASF--------NWEALRWLRD 222
Cdd:TIGR03966 165 dwgspeipEKiDLRTMLRFAPEVLVRPgwllryLRSGRIPDLTVPNLALRGETPPTFFGAYGewmgtpppTWEDVAWLRE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  223 LWPHKLLVKGLLSAEDADRCIAEGADGVILSNHGGRQLDCAISPMEVLAQSVAKTGK--PVLIDSGFRRGSDIVKALALG 300
Cdd:TIGR03966 245 QWGGPFMLKGITRPDDARRAVDAGATAISVSNHGGNNLDGTPAAIRALPAIAEAVGDqvEVLLDGGIRRGSDVVKALALG 324
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 112489859  301 AEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSLSPD 351
Cdd:TIGR03966 325 ARAVMIGRAYLWGLAANGEAGVENVLDILRQGIDSALLGLGKASVHELSRE 375
L_lactate_ox TIGR02708
L-lactate oxidase; Members of this protein oxidize L-lactate to pyruvate, reducing molecular ...
4-348 7.32e-53

L-lactate oxidase; Members of this protein oxidize L-lactate to pyruvate, reducing molecular oxygen to hydrogen peroxide. The enzyme is known in Aerococcus viridans, Streptococcus iniae, and some strains of Streptococcus pyogenes where it appears to contribute to virulence. [Energy metabolism, Other]


Pssm-ID: 131755  Cd Length: 367  Bit Score: 179.34  E-value: 7.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859    4 NLFNVEDYRKLAQKRLPKMVYDYLEGGAEDEYGVKHNRDVFQQWRFKPKRLVDVSRRSLQAEVLGKRQSMPLLIGPTALN 83
Cdd:TIGR02708  12 DFINTYDLEEMAQQVIPKGAFGYIASGAGDTFTLRENIRAFNHKLIVPHLLQDVENPSTEIEFLGHKLKSPFIMAPVAAH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   84 GALWPKGDLALARAATKAGIPFVLSTASNMSIEDLARQCDGD-LWFQLYV-----IHREIAQgmvlKALHTGYTTLVLTT 157
Cdd:TIGR02708  92 KLANEQGEVATARGVSEFGSIYTTSSYSTADLPEISEALNGTpHWFQFYMskddgINRDIMD----RVKADGAKAIVLTA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  158 DVAVNGYRERDLHNRFKIP---PFLT--LKNFEGIDLGKMDKANlemQAALMSRQMDASFNWEALrwlrdlwphKLLVKG 232
Cdd:TIGR02708 168 DATVGGNREVDVRNGFVFPvgmPIVQeyLPTGAGKSMDNVYKSA---KQKLSPRDIEEIAGYSGL---------PVYVKG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  233 LLSAEDADRCIAEGADGVILSNHGGRQLD---CAISPMEVLAQSVAKTgKPVLIDSGFRRGSDIVKALALGAEAVLLGRA 309
Cdd:TIGR02708 236 PQCPEDADRALKAGASGIWVTNHGGRQLDggpAAFDSLQEVAEAVDKR-VPIVFDSGVRRGQHVFKALASGADLVALGRP 314
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 112489859  310 TLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSL 348
Cdd:TIGR02708 315 VIYGLALGGSQGARQVFEYLNKELKRVMQLTGTQTIEDV 353
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
75-308 5.31e-17

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 78.40  E-value: 5.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  75 LLIGPTALNGAlwpKGDLALARAATKAG-IPFVLSTASNMSIED----------LARQCDGDLWFQLYVIHREIAQGM-V 142
Cdd:cd04722    1 VILALLAGGPS---GDPVELAKAAAEAGaDAIIVGTRSSDPEEAetddkevlkeVAAETDLPLGVQLAINDAAAAVDIaA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 143 LKALHTGYTTLVLTTDVAVNgyrerdlhnrfkippfltlknfegidlgkmdkanlemqaalmsrqmdASFNWEALRWLRD 222
Cdd:cd04722   78 AAARAAGADGVEIHGAVGYL-----------------------------------------------AREDLELIRELRE 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 223 LWPH-KLLVKGLLSAEDADR-CIAEGADGVILSNHGGRQLDCAISP--MEVLAQSVAKTGKPVLIDSGFRRGSDIVKALA 298
Cdd:cd04722  111 AVPDvKVVVKLSPTGELAAAaAEEAGVDEVGLGNGGGGGGGRDAVPiaDLLLILAKRGSKVPVIAGGGINDPEDAAEALA 190
                        250
                 ....*....|
gi 112489859 299 LGAEAVLLGR 308
Cdd:cd04722  191 LGADGVIVGS 200
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
215-307 1.79e-08

inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273546 [Multi-domain]  Cd Length: 450  Bit Score: 55.82  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  215 EALRWLRDLWPHKLLVKG-LLSAEDADRCIAEGADGVILSNHGGR----QLDCA-----ISPMEVLAQSVAKTGKPVLID 284
Cdd:TIGR01302 254 DSIKEIKKTYPDLDIIAGnVATAEQAKALIDAGADGLRVGIGPGSicttRIVAGvgvpqITAVYDVAEYAAQSGIPVIAD 333
                          90       100
                  ....*....|....*....|...
gi 112489859  285 SGFRRGSDIVKALALGAEAVLLG 307
Cdd:TIGR01302 334 GGIRYSGDIVKALAAGADAVMLG 356
PRK05437 PRK05437
isopentenyl pyrophosphate isomerase; Provisional
234-348 4.70e-08

isopentenyl pyrophosphate isomerase; Provisional


Pssm-ID: 235465  Cd Length: 352  Bit Score: 54.00  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 234 LSAEDADRCIAEGADGVILSNHGG---------RQ---------LDCAISPMEVLAQSVAKTGKPVLIDSG-FRRGSDIV 294
Cdd:PRK05437 198 ISKETAKRLADAGVKAIDVAGAGGtswaaienyRArddrlasyfADWGIPTAQSLLEARSLLPDLPIIASGgIRNGLDIA 277
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 112489859 295 KALALGAEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSL 348
Cdd:PRK05437 278 KALALGADAVGMAGPFLKAALEGGEEAVIELIEQWIEELKIAMFLTGAKNIAEL 331
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
235-336 5.62e-08

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 52.87  E-value: 5.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 235 SAEDADRCIAEGADGVILSN-----HGGRQLdcaISPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGra 309
Cdd:cd04730  111 SVEEARKAEAAGADALVAQGaeaggHRGTFD---IGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMG-- 185
                         90       100
                 ....*....|....*....|....*....
gi 112489859 310 TLYgLAARgETGVDEVL--TLLKADIDRT 336
Cdd:cd04730  186 TRF-LATE-ESGASPAYkqALLAATAEDT 212
PRK05567 PRK05567
inosine 5'-monophosphate dehydrogenase; Reviewed
215-307 6.18e-07

inosine 5'-monophosphate dehydrogenase; Reviewed


Pssm-ID: 235507 [Multi-domain]  Cd Length: 486  Bit Score: 50.96  E-value: 6.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 215 EALRWLRDLWPHKLLVKG-LLSAEDADRCIAEGADGV-------------ILSNHGGRQLDcAIspMEVlAQSVAKTGKP 280
Cdd:PRK05567 258 DRVREIKAKYPDVQIIAGnVATAEAARALIEAGADAVkvgigpgsicttrIVAGVGVPQIT-AI--ADA-AEAAKKYGIP 333
                         90       100
                 ....*....|....*....|....*..
gi 112489859 281 VLIDSGFRRGSDIVKALALGAEAVLLG 307
Cdd:PRK05567 334 VIADGGIRYSGDIAKALAAGASAVMLG 360
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
205-320 5.77e-06

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 48.04  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 205 SRQMDASFNWEALRWLRDLWPHKLLVKG-LLSAEDADRCIAEGADGVILSNHGGR----QLDCAI------SPMEVlAQS 273
Cdd:PTZ00314 261 SSQGNSIYQIDMIKKLKSNYPHVDIIAGnVVTADQAKNLIDAGADGLRIGMGSGSicitQEVCAVgrpqasAVYHV-ARY 339
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 112489859 274 VAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGRatlyGLAARGET 320
Cdd:PTZ00314 340 ARERGVPCIADGGIKNSGDICKALALGADCVMLGS----LLAGTEEA 382
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain. This family is involved in biosynthesis of ...
215-308 9.42e-06

IMP dehydrogenase / GMP reductase domain. This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 376340  Cd Length: 462  Bit Score: 47.38  E-value: 9.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  215 EALRWLRDLWPHKLLVKG-LLSAEDADRCIAEGADGV-------------ILSNHGGRQLDcAIspMEVlAQSVAKTGKP 280
Cdd:pfam00478 250 DTVKWIKKKYPDVQVIAGnVATAEGAKALIDAGADAVkvgigpgsicttrVVAGVGVPQLT-AI--YDV-AEAAKKYGVP 325
                          90       100
                  ....*....|....*....|....*...
gi 112489859  281 VLIDSGFRRGSDIVKALALGAEAVLLGR 308
Cdd:pfam00478 326 VIADGGIKYSGDIVKALAAGADAVMLGS 353
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
215-308 1.63e-05

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 45.97  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 215 EALRWLRDLWPH-KLLVKGLLSAEDADRCIAEGADGVILSNHGGR----QLDCAIS-PM-----EVlAQSVAKTGKPVLI 283
Cdd:cd00381  124 EMIKFIKKKYPNvDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSicttRIVTGVGvPQatavaDV-AAAARDYGVPVIA 202
                         90       100
                 ....*....|....*....|....*
gi 112489859 284 DSGFRRGSDIVKALALGAEAVLLGR 308
Cdd:cd00381  203 DGGIRTSGDIVKALAAGADAVMLGS 227
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
234-348 2.10e-05

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205  Cd Length: 326  Bit Score: 45.95  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 234 LSAEDADRCIAEGADGVILSNHGG---------RQLDCAISPMEVL-------AQSV-----AKTGKPVLIDSGFRRGSD 292
Cdd:cd02811  190 ISRETAKRLADAGVKAIDVAGAGGtswarvenyRAKDSDQRLAEYFadwgiptAASLlevrsALPDLPLIASGGIRNGLD 269
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 112489859 293 IVKALALGAEAVLLGRATLyGLAARGETGVDEVLTLLKADIDRTLAQIGCPDITSL 348
Cdd:cd02811  270 IAKALALGADLVGMAGPFL-KAALEGEEAVIETIEQIIEELRTAMFLTGAKNLAEL 324
IPP_isom_2 TIGR02151
isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP ...
55-348 3.25e-05

isopentenyl-diphosphate delta-isomerase, type 2; Isopentenyl-diphosphate delta-isomerase (IPP isomerase) interconverts isopentenyl diphosphate and dimethylallyl diphosphate. This model represents the type 2 enzyme. FMN, NADPH, and Mg2+ are required by this form, which lacks homology to the type 1 enzyme (TIGR02150). IPP is precursor to many compounds, including enzyme cofactors, sterols, and isoprenoids. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273999  Cd Length: 333  Bit Score: 45.33  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859   55 VDVSRRSLQAEVLGKRQSMPLLIgpTALNGALWPKGDL--ALARAATKAGIPFVLSTASNMsIEDlarqcdGDLWFQLYV 132
Cdd:TIGR02151  36 INLDDIDLTTEFLGKRLKAPFYI--NAMTGGSEEAGKInrNLARAARELGIPMGVGSQRAA-LKD------PETADTFEV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  133 IHREIAQGMVLKALhtgyttlvlTTDVAVNGYRERDLhnrfkippfltlknfEGIDLGKMDKANLEMQAA--LMSRQMDA 210
Cdd:TIGR02151 107 VREEAPNGPLIANI---------GAPQLVEGGPEEAQ---------------EAIDMIEADALAIHLNVLqeLVQPEGDR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  211 SF-NW-EALRWLRDLWPHKLLVK----GLlSAEDADRCIAEGADGVILSNHGGRQ------------------LDCAISP 266
Cdd:TIGR02151 163 NFkGWlEKIAEICSQLSVPVIVKevgfGI-SKEVAKLLADAGVSAIDVAGAGGTSwaqvenyrakgsnlasffNDWGIPT 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  267 MEVL--AQSVAKtGKPVLIDSGFRRGSDIVKALALGAEAVLLGRATLYGLAARGETGVDEVLTLLKADIDRTLAQIGCPD 344
Cdd:TIGR02151 242 AASLleVRSDAP-DAPIIASGGLRTGLDVAKAIALGADAVGMARPFLKAALDEGEEAVIEEIELIIEELKVAMFLTGAKT 320

                  ....
gi 112489859  345 ITSL 348
Cdd:TIGR02151 321 IAEL 324
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
278-309 5.50e-05

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202  Cd Length: 392  Bit Score: 44.84  E-value: 5.50e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 112489859 278 GKPVLI-DSGFRRGSDIVKALALGAEAVLLGRA 309
Cdd:cd02808  284 DRVSLIaSGGLRTGADVAKALALGADAVGIGTA 316
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
193-307 1.23e-04

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 43.89  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 193 DKANLEMQAA-------LMSRQMDASFNWEALRWLRDLWPHKLLVKG-LLSAEDADRCIAEGADGVILSNHGGR----QL 260
Cdd:PLN02274 249 DKERLEHLVKagvdvvvLDSSQGDSIYQLEMIKYIKKTYPELDVIGGnVVTMYQAQNLIQAGVDGLRVGMGSGSicttQE 328
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 112489859 261 DCAI-----SPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLG 307
Cdd:PLN02274 329 VCAVgrgqaTAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMG 380
Glu_synthase pfam01645
Conserved region in glutamate synthase. This family represents a region of the glutamate ...
281-314 3.25e-04

Conserved region in glutamate synthase. This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organisms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 366740  Cd Length: 367  Bit Score: 42.32  E-value: 3.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 112489859  281 VLIDSGFRRGSDIVKALALGAEAVLLGRATLYGL 314
Cdd:pfam01645 276 LIADGGLRTGADVAKAAALGADAVYIGTAALIAL 309
PRK08649 PRK08649
GuaB3 family IMP dehydrogenase-related protein;
280-307 7.00e-04

GuaB3 family IMP dehydrogenase-related protein;


Pssm-ID: 236322 [Multi-domain]  Cd Length: 368  Bit Score: 41.34  E-value: 7.00e-04
                         10        20
                 ....*....|....*....|....*...
gi 112489859 280 PVLIDSGFRRGSDIVKALALGAEAVLLG 307
Cdd:PRK08649 258 HVIADGGIGTSGDIAKAIACGADAVMLG 285
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism];
246-311 1.05e-03

Glutamate synthase domain 2 [Amino acid transport and metabolism];


Pssm-ID: 223147  Cd Length: 485  Bit Score: 40.70  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859 246 GADGVILSNHGG-------RQLDCAISPMEV-LA---QSVAKTG---KPVLI-DSGFRRGSDIVKALALGAEAVLLGRAT 310
Cdd:COG0069  327 GADVITIDGADGgtgasplTSIDHAGIPWELgLAethQTLVLNGlrdKVKLIaDGGLRTGADVAKAAALGADAVGFGTAA 406

                 .
gi 112489859 311 L 311
Cdd:COG0069  407 L 407
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
235-337 3.27e-03

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 39.03  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112489859  235 SAEDADRCIAEGADGVIL--SNHGGRQLDCAI---SPMEVLAQSVAKTGKPVLIDSGFRRGSDIVKALALGAEAVLLGRA 309
Cdd:pfam03060 145 SAKEARIAEARGADALIVqgPEAGGHQGTPEYgdkGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTR 224
                          90       100       110
                  ....*....|....*....|....*....|
gi 112489859  310 TLyglaARGETGVDEV--LTLLKADIDRTL 337
Cdd:pfam03060 225 FL----LTKESGAHDAhkQKITEAGEDDTL 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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