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Conserved domains on  [gi|446170855|ref|WP_000248710|]
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MULTISPECIES: Gfo/Idh/MocA family protein [Lactobacillales]

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

CATH:  3.40.50.720|3.30.360.10
Gene Ontology:  GO:0000166|GO:0003824
PubMed:  30945211|31869345|25704928|26749496

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-265 1.05e-69

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.57  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   1 MVNYGIVGAGYFGADLARSMNKIEDAKVVAVFDPN--HGEEVAQELGSDVCASLDELVAREDIDCVIVASPSYLHREPVV 78
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDpeRAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  79 KAAQHGKHVFCEKPIALSYEDCKAMVDACKENNVIFMAGHIMNFFNGVHHAKELITQGKIGKVLYCHAARTGWEEQQPTV 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAGPAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855 159 SWKKLRSQSGGHLY-HHIHELDCIQFIMGGLPEKATMVGGNVYHKGENFgdeDDMLIVNLEYSDDRYAVLEYG--NAFRW 235
Cdd:COG0673  163 WRFDPELAGGGALLdLGIHDIDLARWLLGSEPESVSATGGRLVPDRVEV---DDTAAATLRFANGAVATLEASwvAPGGE 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 446170855 236 GEHYVLIQGTEGAIKLDLFNTGGTLRVKGE 265
Cdd:COG0673  240 RDERLEVYGTKGTLFVDAIRGGEPPPVSLE 269
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-265 1.05e-69

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.57  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   1 MVNYGIVGAGYFGADLARSMNKIEDAKVVAVFDPN--HGEEVAQELGSDVCASLDELVAREDIDCVIVASPSYLHREPVV 78
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDpeRAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  79 KAAQHGKHVFCEKPIALSYEDCKAMVDACKENNVIFMAGHIMNFFNGVHHAKELITQGKIGKVLYCHAARTGWEEQQPTV 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAGPAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855 159 SWKKLRSQSGGHLY-HHIHELDCIQFIMGGLPEKATMVGGNVYHKGENFgdeDDMLIVNLEYSDDRYAVLEYG--NAFRW 235
Cdd:COG0673  163 WRFDPELAGGGALLdLGIHDIDLARWLLGSEPESVSATGGRLVPDRVEV---DDTAAATLRFANGAVATLEASwvAPGGE 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 446170855 236 GEHYVLIQGTEGAIKLDLFNTGGTLRVKGE 265
Cdd:COG0673  240 RDERLEVYGTKGTLFVDAIRGGEPPPVSLE 269
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 130-363 1.32e-39

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: 139.48  E-value: 1.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  130 KELITQGKIGKVLYCHAA-RTGWEEQQPTVSWKKLRSQSGGHLYHH-IHELDCIQFIMGGLPEKATMVGGnvyhkgenfg 207
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHtRDPFRPPQEFKRWRVDPEKSGGALYDLgIHTIDLLIYLFGEPPSVVAVYAS---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  208 deDDMLIVNLEYSDDRYAVLE--YGNAFRWGEHYVLIQGTEGAIKLDLFNTGGtlrvkgegESHFLVHETQEEDDDRTai 285
Cdd:pfam02894  71 --EDTAFATLEFKNGAVGTLEtsGGSIVEANGHRISIHGTKGSIELDGIDDGL--------LSVTVVGEPGWATDDPM-- 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446170855  286 ytgrgmdgaiaYGKPGVRCPLWLQTCIDKEMEYLHDIIKGgeITEEFEKLLNGVAALESIATADACTLSVKEDRKVSL 363
Cdd:pfam02894 139 -----------VRKGGDEVPEFLGSFAGGYLLEYDAFLEA--VRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 1-362 1.99e-39

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: 142.74  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855    1 MVNYGIVGAGYFGADLARS-MNKIEDAKVVAVFDPN--HGEEVAQELG-SDVCASLDELVAREDIDCVIVASPSYLHREP 76
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENlATHVPGARLKAIVDPFadAAAELAEKLGiEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   77 VVKAAQHGKHVFCEKPIALSYEDCKAMVDACKENNVIFMAGHIMNFFNGVHHAKELITQGKIGKVlycHAAR-TGWEEQQ 155
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKP---EILRiTSRDPAP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  156 PTVSWkkLRSQSGGHLYHHIHELDCIQFIMGGLPEKATMVGGNVYHK--GEnFGDEDDMlIVNLEYSDDRYAVLEygNAF 233
Cdd:TIGR04380 158 PPVAY--VKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPaiGE-AGDVDTA-VITLKFENGAIAVID--NSR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  234 RWGEHYvliqgtegAIKLDLFNTGGTLRVKGEGESHflvhetqeedddrtaiytgrgmdgAIAYGKPGVRCPLWLQTCID 313
Cdd:TIGR04380 232 RAAYGY--------DQRVEVFGSKGMLRAENDTEST------------------------VILYDAEGVRGDKPLNFFLE 279

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446170855  314 K-------EMEYLHDIIKGGEITEefeklLNGVAALESIATADACTLSVKEDRKVS 362
Cdd:TIGR04380 280 RyrdayraEIQAFVDAILEGRPPP-----VTGEDGLKALLLALAAKRSLEEGRPVK 330
PRK13304 PRK13304
aspartate dehydrogenase;
1-111 2.79e-08

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 54.23  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   1 MVNYGIVGAGYFGADLARS-MNKIEDAKVVAVFDPN--HGEEVAQELGSDVCASLDELVarEDIDCVI-VASPSYLhREP 76
Cdd:PRK13304   1 MLKIGIVGCGAIASLITKAiLSGRINAELYAFYDRNleKAENLASKTGAKACLSIDELV--EDVDLVVeCASVNAV-EEV 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446170855  77 VVKAAQHGKHVFCEKPIALSYEDCKAMV-DACKENN 111
Cdd:PRK13304  78 VPKSLENGKDVIIMSVGALADKELFLKLyKLAKENN 113
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 6-116 3.08e-06

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: 46.77  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   6 IVGAGYFGADLARSMNKIEDAKVVAVFDPNH------GEEVAQE--LGSDVCASLDELVAREDIDCVIVASPSYLHR--E 75
Cdd:cd24146    5 VWGLGAMGRGIARYLLEKPGLEIVGAVDRDPakvgkdLGELGGGapLGVKVTDDLDAVLAATKPDVVVHATTSFLADvaP 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446170855  76 PVVKAAQHGKHVF--CEkpiALSY------EDCKAMVDACKENNVIFMA 116
Cdd:cd24146   85 QIERLLEAGLNVIttCE---ELFYpwardpELAEELDALAKENGVTVLG 130
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-265 1.05e-69

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 220.57  E-value: 1.05e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   1 MVNYGIVGAGYFGADLARSMNKIEDAKVVAVFDPN--HGEEVAQELGSDVCASLDELVAREDIDCVIVASPSYLHREPVV 78
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDpeRAEAFAEEYGVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  79 KAAQHGKHVFCEKPIALSYEDCKAMVDACKENNVIFMAGHIMNFFNGVHHAKELITQGKIGKVLYCHAARTGWEEQQPTV 158
Cdd:COG0673   83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAGPAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855 159 SWKKLRSQSGGHLY-HHIHELDCIQFIMGGLPEKATMVGGNVYHKGENFgdeDDMLIVNLEYSDDRYAVLEYG--NAFRW 235
Cdd:COG0673  163 WRFDPELAGGGALLdLGIHDIDLARWLLGSEPESVSATGGRLVPDRVEV---DDTAAATLRFANGAVATLEASwvAPGGE 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 446170855 236 GEHYVLIQGTEGAIKLDLFNTGGTLRVKGE 265
Cdd:COG0673  240 RDERLEVYGTKGTLFVDAIRGGEPPPVSLE 269
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 130-363 1.32e-39

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: 139.48  E-value: 1.32e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  130 KELITQGKIGKVLYCHAA-RTGWEEQQPTVSWKKLRSQSGGHLYHH-IHELDCIQFIMGGLPEKATMVGGnvyhkgenfg 207
Cdd:pfam02894   1 KELIENGVLGEVVMVTVHtRDPFRPPQEFKRWRVDPEKSGGALYDLgIHTIDLLIYLFGEPPSVVAVYAS---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  208 deDDMLIVNLEYSDDRYAVLE--YGNAFRWGEHYVLIQGTEGAIKLDLFNTGGtlrvkgegESHFLVHETQEEDDDRTai 285
Cdd:pfam02894  71 --EDTAFATLEFKNGAVGTLEtsGGSIVEANGHRISIHGTKGSIELDGIDDGL--------LSVTVVGEPGWATDDPM-- 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446170855  286 ytgrgmdgaiaYGKPGVRCPLWLQTCIDKEMEYLHDIIKGgeITEEFEKLLNGVAALESIATADACTLSVKEDRKVSL 363
Cdd:pfam02894 139 -----------VRKGGDEVPEFLGSFAGGYLLEYDAFLEA--VRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 1-362 1.99e-39

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: 142.74  E-value: 1.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855    1 MVNYGIVGAGYFGADLARS-MNKIEDAKVVAVFDPN--HGEEVAQELG-SDVCASLDELVAREDIDCVIVASPSYLHREP 76
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENlATHVPGARLKAIVDPFadAAAELAEKLGiEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   77 VVKAAQHGKHVFCEKPIALSYEDCKAMVDACKENNVIFMAGHIMNFFNGVHHAKELITQGKIGKVlycHAAR-TGWEEQQ 155
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKP---EILRiTSRDPAP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  156 PTVSWkkLRSQSGGHLYHHIHELDCIQFIMGGLPEKATMVGGNVYHK--GEnFGDEDDMlIVNLEYSDDRYAVLEygNAF 233
Cdd:TIGR04380 158 PPVAY--VKVSGGLFLDMTIHDFDMARFLLGSEVEEVYAQGSVLVDPaiGE-AGDVDTA-VITLKFENGAIAVID--NSR 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  234 RWGEHYvliqgtegAIKLDLFNTGGTLRVKGEGESHflvhetqeedddrtaiytgrgmdgAIAYGKPGVRCPLWLQTCID 313
Cdd:TIGR04380 232 RAAYGY--------DQRVEVFGSKGMLRAENDTEST------------------------VILYDAEGVRGDKPLNFFLE 279

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446170855  314 K-------EMEYLHDIIKGGEITEefeklLNGVAALESIATADACTLSVKEDRKVS 362
Cdd:TIGR04380 280 RyrdayraEIQAFVDAILEGRPPP-----VTGEDGLKALLLALAAKRSLEEGRPVK 330
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 2-118 1.40e-38

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: 133.87  E-value: 1.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855    2 VNYGIVGAGYFGADLARSMNKIED-AKVVAVFDPN--HGEEVAQELGSDVCASLDELVAREDIDCVIVASPSYLHREPVV 78
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPgAELVAILDPNseRAEAVAESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446170855   79 KAAQHGKHVFCEKPIALSYEDCKAMVDACKENNVIFMAGH 118
Cdd:pfam01408  81 AALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK13304 PRK13304
aspartate dehydrogenase;
1-111 2.79e-08

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 54.23  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   1 MVNYGIVGAGYFGADLARS-MNKIEDAKVVAVFDPN--HGEEVAQELGSDVCASLDELVarEDIDCVI-VASPSYLhREP 76
Cdd:PRK13304   1 MLKIGIVGCGAIASLITKAiLSGRINAELYAFYDRNleKAENLASKTGAKACLSIDELV--EDVDLVVeCASVNAV-EEV 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446170855  77 VVKAAQHGKHVFCEKPIALSYEDCKAMV-DACKENN 111
Cdd:PRK13304  78 VPKSLENGKDVIIMSVGALADKELFLKLyKLAKENN 113
FlaA1 COG1086
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ...
 6-70 2.34e-06

NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440703 [Multi-domain]  Cd Length: 121  Bit Score: 46.07  E-value: 2.34e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   6 IVGAGYFGADLARSMNKIEDA--KVVAVFDPNHGEEVAQELGSDV---CASLDELVAREDIDCVIVASPS 70
Cdd:COG1086   26 IVGAGEAGRQLARALRRNPDLgyRVVGFVDDDPDKRGRRIEGVPVlgtLDDLPELVRRLGVDEVIIALPS 95
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 6-116 3.08e-06

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: 46.77  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   6 IVGAGYFGADLARSMNKIEDAKVVAVFDPNH------GEEVAQE--LGSDVCASLDELVAREDIDCVIVASPSYLHR--E 75
Cdd:cd24146    5 VWGLGAMGRGIARYLLEKPGLEIVGAVDRDPakvgkdLGELGGGapLGVKVTDDLDAVLAATKPDVVVHATTSFLADvaP 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446170855  76 PVVKAAQHGKHVF--CEkpiALSY------EDCKAMVDACKENNVIFMA 116
Cdd:cd24146   85 QIERLLEAGLNVIttCE---ELFYpwardpELAEELDALAKENGVTVLG 130
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 4-114 5.32e-05

Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.


Pssm-ID: 281446 [Multi-domain]  Cd Length: 116  Bit Score: 42.29  E-value: 5.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855    4 YGIVGAGYFGAdLARSMNKIeDAKVVAVFDPNHGEEVAQEL--GSDVCASLDELVAREDIDCVI-VASPSYLhREPVVKA 80
Cdd:pfam03447   2 CGAIGSGVLEQ-LLRQQSEI-PLELVAVADRDLLSKDPLALlpDEPLTLDLDDLIAHPDPDVVVeCASSEAV-AELVLDA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 446170855   81 AQHGKHVFCEKPIALSYEDC-KAMVDACKENNVIF 114
Cdd:pfam03447  79 LKAGKDVVTASKGALADLALyEELREAAEANGARI 113
PRK10206 PRK10206
putative oxidoreductase; Provisional
 20-142 5.87e-04

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 41.35  E-value: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855  20 MNKIEDAKVVAVFDPNHGEEVAQELGSDVC--ASLDELVAREDIDCVIVASPSYLHREPVVKAAQHGKHVFCEKPIALSY 97
Cdd:PRK10206  22 LNRKDSWHVAHIFRRHAKPEEQAPIYSHIHftSDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTL 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446170855  98 EDCKAMVDACKENNVIFMAGHIMNFFNGVHHAKELITQGKIGKVL 142
Cdd:PRK10206 102 AEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIV 146
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 5-89 9.39e-04

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 39.08  E-value: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   5 GIVGA-GYFGADLARSMNKIEDAKVVAVFDPNHGEEVAQELG------SDVCASLDELVAREDIDCVI---VASPSYLHr 74
Cdd:cd02274    4 AVAGAtGRMGRELVKAILEAPDLELVGAVDRPGSGLLGGDAGglagigTGVIVSLDLELAAADADVVIdftTPEATLEN- 82

                         90
                 ....*....|....*
gi 446170855  75 epVVKAAQHGKHVFC 89
Cdd:cd02274   83 --LEAAAKAGVPLVI 95
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 5-69 2.28e-03

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 39.41  E-value: 2.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446170855   5 GIVGAGYFG---ADLARSMnkieDAKVVAvFDPNHGEEVAQELGSDVCASLDELVAREDIdcVIVASP 69
Cdd:COG0111  144 GIVGLGRIGravARRLRAF----GMRVLA-YDPSPKPEEAADLGVGLVDSLDELLAEADV--VSLHLP 204
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 5-61 4.65e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 38.70  E-value: 4.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855   5 GIVGAGYFG---ADLARSMnkieDAKVVaVFDPNHGEEVAQELGSdVCASLDELVAREDI 61
Cdd:cd12167  154 GIVGFGRIGravVELLRPF----GLRVL-VYDPYLPAAEAAALGV-ELVSLDELLARSDV 207
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 6-115 5.87e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 36.41  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446170855    6 IVGAGYFGA----DLARSMNkiEDAKVVAVFDPNHGEEVAQELG-----------SDVCASLDELVAREDIdcVIVASPS 70
Cdd:pfam03435   3 IIGAGSVGQgvapLLARHFD--VDRITVADRTLEKAQALAAKLGgvrfiavavdaDNYEAVLAALLKEGDL--VVNLSPP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446170855   71 YLHRePVVKAA-QHGKHVFCekpIALSYEDCKAMVDACKENNVIFM 115
Cdd:pfam03435  79 TLSL-DVLKACiETGVHYVD---TSYLREAVLALHEKAKDAGVTAV 120
formate_dh_like cd05198
Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase ...
 5-75 5.94e-03

Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxy acid dehydrogenase family; Formate dehydrogenase, D-specific 2-hydroxy acid dehydrogenase, Phosphoglycerate Dehydrogenase, Lactate dehydrogenase, Thermostable Phosphite Dehydrogenase, and Hydroxy(phenyl)pyruvate reductase, among others, share a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase, among others. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240622 [Multi-domain]  Cd Length: 302  Bit Score: 37.99  E-value: 5.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446170855   5 GIVGAGYFG---ADLARSMnkieDAKVVAvFDPNHGEEVAQELGSDVcASLDELVAREDIdcVIVASPsyLHRE 75
Cdd:cd05198  144 GIVGLGRIGqrvAKRLQAF----GMKVLY-YDRTRKPEPEEDLGFRV-VSLDELLAQSDV--VVLHLP--LTPE 207
 
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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