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Conserved domains on  [gi|1681689858|dbj|GEC38552|]
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oxidoreductase [Sinorhizobium meliloti]

Protein Classification

Gfo/Idh/MocA family protein( domain architecture ID 11430574)

Gfo/Idh/MocA family protein belonging to the NAD(P)(+)-binding Rossmann-fold superfamily, may function as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
7-354 1.67e-53

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 178.19  E-value: 1.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   7 PIRVLSAGLGNMGRSHALAYHQNPGFEIAGLVNRSKVALPEALAGYEIL--PSFPEALAELEPELCSINTYSDTHADYAV 84
Cdd:COG0673     3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRvyTDYEELLADPDIDAVVIATPNHLHAELAI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858  85 MAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVVGYILRHHPSWMRLIA--EARKLGGPYVFRMNLNQQSSGP--A 160
Cdd:COG0673    83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAREliDSGAIGEIRSVRARFGHPRPAGpaD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 161 WATHKSLmQTTPPIVDCGVHYVDVMCQITDANPVEVRGMGLRLSNEiAADMYNYGHLQVIFEDGSVGWYEAGWgpmiset 240
Cdd:COG0673   163 WRFDPEL-AGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPD-RVEVDDTAAATLRFANGAVATLEASW------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 241 affvkdvmspngsvsiVMDQNAKSDDIDVHtktsvirvhsaatGPDGRFLksdedlvmegepghqelcdreqafvLKAIR 320
Cdd:COG0673   234 ----------------VAPGGERDERLEVY-------------GTKGTLF-------------------------VDAIR 259
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1681689858 321 EDIDLGRHMDDAVQSLKICLAADDSVRTGKPVKL 354
Cdd:COG0673   260 GGEPPPVSLEDGLRALELAEAAYESARTGRRVEL 293
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
7-354 1.67e-53

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 178.19  E-value: 1.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   7 PIRVLSAGLGNMGRSHALAYHQNPGFEIAGLVNRSKVALPEALAGYEIL--PSFPEALAELEPELCSINTYSDTHADYAV 84
Cdd:COG0673     3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRvyTDYEELLADPDIDAVVIATPNHLHAELAI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858  85 MAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVVGYILRHHPSWMRLIA--EARKLGGPYVFRMNLNQQSSGP--A 160
Cdd:COG0673    83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAREliDSGAIGEIRSVRARFGHPRPAGpaD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 161 WATHKSLmQTTPPIVDCGVHYVDVMCQITDANPVEVRGMGLRLSNEiAADMYNYGHLQVIFEDGSVGWYEAGWgpmiset 240
Cdd:COG0673   163 WRFDPEL-AGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPD-RVEVDDTAAATLRFANGAVATLEASW------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 241 affvkdvmspngsvsiVMDQNAKSDDIDVHtktsvirvhsaatGPDGRFLksdedlvmegepghqelcdreqafvLKAIR 320
Cdd:COG0673   234 ----------------VAPGGERDERLEVY-------------GTKGTLF-------------------------VDAIR 259
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1681689858 321 EDIDLGRHMDDAVQSLKICLAADDSVRTGKPVKL 354
Cdd:COG0673   260 GGEPPPVSLEDGLRALELAEAAYESARTGRRVEL 293
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
8-124 1.61e-24

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 96.51  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   8 IRVLSAGLGNMGRSHALAYHQN-PGFEIAGLVNRSKVALpEALA---GYEILPSFPEALAELEPELCSINTYSDTHADYA 83
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASqPGAELVAILDPNSERA-EAVAesfGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1681689858  84 VMAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVVGY 124
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
7-353 3.02e-22

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 95.75  E-value: 3.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   7 PIRVLSAGLGNMGRSHA--LAYHQnPGFEIAGLVNRSKVALPEALAGYEILP---SFPEALAELEPELCSINTYSDTHAD 81
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAenLATHV-PGARLKAIVDPFADAAAELAEKLGIEPvtqDPEAALADPEIDAVLIASPTDTHAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858  82 YAVMAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVVGYILRHHPSWMRL--IAEARKLGGPYVFRmnlnQQSSGP 159
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVkqLVEAGKIGKPEILR----ITSRDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 160 AwathkslmqtTPPI----------VDCGVHYVDVMCQITDANPVEVRGMGLRLSN-EIA-ADMYNYGHLQVIFEDGSVG 227
Cdd:TIGR04380 156 A----------PPPVayvkvsgglfLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDpAIGeAGDVDTAVITLKFENGAIA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 228 WYEAGWgpmiseTAFFVKD----VMSPNGSVSIVMDqnaksddidvhTKTSVIrvHSAATG-----PDGRFLksdedlvm 298
Cdd:TIGR04380 226 VIDNSR------RAAYGYDqrveVFGSKGMLRAEND-----------TESTVI--LYDAEGvrgdkPLNFFL-------- 278
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1681689858 299 egEPGHQELCDREQAFVlKAIREDIDLGRHMDDAVQSLKICLAADDSVRTGKPVK 353
Cdd:TIGR04380 279 --ERYRDAYRAEIQAFV-DAILEGRPPPVTGEDGLKALLLALAAKRSLEEGRPVK 330
PRK10206 PRK10206
putative oxidoreductase; Provisional
60-117 1.25e-08

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 55.99  E-value: 1.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1681689858  60 EALAELEPELCSINTYSDTHADYAVMAIEAGAHVFVEKPLATTVADAERVVACARANG 117
Cdd:PRK10206   58 EVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
8-117 2.02e-07

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 49.85  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   8 IRVLSAGLGNMGRSHALAYHQNPGFEIAGLVNRSK--------VALPEALAGYEILPSFPEALAELEPELCSINTYSDTH 79
Cdd:cd24146     1 IRVVVWGLGAMGRGIARYLLEKPGLEIVGAVDRDPakvgkdlgELGGGAPLGVKVTDDLDAVLAATKPDVVVHATTSFLA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1681689858  80 ADYAVM--AIEAGAHV-------FVekPLATTVADAERVVACARANG 117
Cdd:cd24146    81 DVAPQIerLLEAGLNVittceelFY--PWARDPELAEELDALAKENG 125
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
7-354 1.67e-53

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 178.19  E-value: 1.67e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   7 PIRVLSAGLGNMGRSHALAYHQNPGFEIAGLVNRSKVALPEALAGYEIL--PSFPEALAELEPELCSINTYSDTHADYAV 84
Cdd:COG0673     3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRvyTDYEELLADPDIDAVVIATPNHLHAELAI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858  85 MAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVVGYILRHHPSWMRLIA--EARKLGGPYVFRMNLNQQSSGP--A 160
Cdd:COG0673    83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAAREliDSGAIGEIRSVRARFGHPRPAGpaD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 161 WATHKSLmQTTPPIVDCGVHYVDVMCQITDANPVEVRGMGLRLSNEiAADMYNYGHLQVIFEDGSVGWYEAGWgpmiset 240
Cdd:COG0673   163 WRFDPEL-AGGGALLDLGIHDIDLARWLLGSEPESVSATGGRLVPD-RVEVDDTAAATLRFANGAVATLEASW------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 241 affvkdvmspngsvsiVMDQNAKSDDIDVHtktsvirvhsaatGPDGRFLksdedlvmegepghqelcdreqafvLKAIR 320
Cdd:COG0673   234 ----------------VAPGGERDERLEVY-------------GTKGTLF-------------------------VDAIR 259
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1681689858 321 EDIDLGRHMDDAVQSLKICLAADDSVRTGKPVKL 354
Cdd:COG0673   260 GGEPPPVSLEDGLRALELAEAAYESARTGRRVEL 293
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
8-124 1.61e-24

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 96.51  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   8 IRVLSAGLGNMGRSHALAYHQN-PGFEIAGLVNRSKVALpEALA---GYEILPSFPEALAELEPELCSINTYSDTHADYA 83
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASqPGAELVAILDPNSERA-EAVAesfGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1681689858  84 VMAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVVGY 124
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
7-353 3.02e-22

inositol 2-dehydrogenase; All members of the seed alignment for this model are known or predicted inositol 2-dehydrogenase sequences co-clustered with other enzymes for catabolism of myo-inositol or closely related compounds. Inositol 2-dehydrogenase catalyzes the first step in inositol catabolism. Members of this family may vary somewhat in their ranges of acceptable substrates and some may act on analogs to myo-inositol rather than myo-inositol per se. [Energy metabolism, Sugars]


Pssm-ID: 275173 [Multi-domain]  Cd Length: 330  Bit Score: 95.75  E-value: 3.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   7 PIRVLSAGLGNMGRSHA--LAYHQnPGFEIAGLVNRSKVALPEALAGYEILP---SFPEALAELEPELCSINTYSDTHAD 81
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAenLATHV-PGARLKAIVDPFADAAAELAEKLGIEPvtqDPEAALADPEIDAVLIASPTDTHAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858  82 YAVMAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVVGYILRHHPSWMRL--IAEARKLGGPYVFRmnlnQQSSGP 159
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVkqLVEAGKIGKPEILR----ITSRDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 160 AwathkslmqtTPPI----------VDCGVHYVDVMCQITDANPVEVRGMGLRLSN-EIA-ADMYNYGHLQVIFEDGSVG 227
Cdd:TIGR04380 156 A----------PPPVayvkvsgglfLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDpAIGeAGDVDTAVITLKFENGAIA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 228 WYEAGWgpmiseTAFFVKD----VMSPNGSVSIVMDqnaksddidvhTKTSVIrvHSAATG-----PDGRFLksdedlvm 298
Cdd:TIGR04380 226 VIDNSR------RAAYGYDqrveVFGSKGMLRAEND-----------TESTVI--LYDAEGvrgdkPLNFFL-------- 278
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1681689858 299 egEPGHQELCDREQAFVlKAIREDIDLGRHMDDAVQSLKICLAADDSVRTGKPVK 353
Cdd:TIGR04380 279 --ERYRDAYRAEIQAFV-DAILEGRPPPVTGEDGLKALLLALAAKRSLEEGRPVK 330
PRK10206 PRK10206
putative oxidoreductase; Provisional
60-117 1.25e-08

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 55.99  E-value: 1.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1681689858  60 EALAELEPELCSINTYSDTHADYAVMAIEAGAHVFVEKPLATTVADAERVVACARANG 117
Cdd:PRK10206   58 EVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKG 115
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
8-117 2.02e-07

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 49.85  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   8 IRVLSAGLGNMGRSHALAYHQNPGFEIAGLVNRSK--------VALPEALAGYEILPSFPEALAELEPELCSINTYSDTH 79
Cdd:cd24146     1 IRVVVWGLGAMGRGIARYLLEKPGLEIVGAVDRDPakvgkdlgELGGGAPLGVKVTDDLDAVLAATKPDVVVHATTSFLA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1681689858  80 ADYAVM--AIEAGAHV-------FVekPLATTVADAERVVACARANG 117
Cdd:cd24146    81 DVAPQIerLLEAGLNVittceelFY--PWARDPELAEELDALAKENG 125
PRK11579 PRK11579
putative oxidoreductase; Provisional
57-122 6.26e-06

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 47.41  E-value: 6.26e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681689858  57 SFPEALAElEP--ELCSINTYSDTHADYAVMAIEAGAHVFVEKPLATTVADAERVVACARANGRKLVV 122
Cdd:PRK11579   54 SEPQHLFN-DPniDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSV 120
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
169-354 1.99e-04

Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 427044  Cd Length: 203  Bit Score: 42.02  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 169 QTTPPIVDCGVHYVDVMCQITDANPVEVRGmglrlsneIAADmyNYGHLQVIFEDGSVGWYEAGwGPMISETaffvkdvm 248
Cdd:pfam02894  38 KSGGALYDLGIHTIDLLIYLFGEPPSVVAV--------YASE--DTAFATLEFKNGAVGTLETS-GGSIVEA-------- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858 249 sPNGSVSIVMDQ-NAKSDDIDvHTKTSVIRVHSAATGPDGRFLKSDEDLVMEGEPGHQELCDREQAFVLKAIREDIDLGR 327
Cdd:pfam02894  99 -NGHRISIHGTKgSIELDGID-DGLLSVTVVGEPGWATDDPMVRKGGDEVPEFLGSFAGGYLLEYDAFLEAVRGGKVVLV 176
                         170       180
                  ....*....|....*....|....*..
gi 1681689858 328 HMDDAVQSLKICLAADDSVRTGKPVKL 354
Cdd:pfam02894 177 DAEDGLYALAVIEAAYESAEEGRPVKL 203
COG3804 COG3804
Uncharacterized conserved protein [Function unknown];
7-93 2.04e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443017 [Multi-domain]  Cd Length: 338  Bit Score: 42.86  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681689858   7 PIRVLSAGLGNMGRsHALAY-HQNPGFEIAGLVNRSkvalPE-------ALAGYE-----ILPSFPEALAELEPELCSIN 73
Cdd:COG3804     1 KIRVVQWGTGNMGR-GAIRAiLAHPGLELVGAIDHS----PAkvgkdagELAGLGrplgvKATDDADAVLALDADVVVYA 75
                          90       100
                  ....*....|....*....|..
gi 1681689858  74 TYSDTHADYA--VMAIEAGAHV 93
Cdd:COG3804    76 TDSRLEEAVDdlERLLEAGVNV 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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