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Conserved domains on  [gi|2076732937|ref|WP_219968280|]
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Gfo/Idh/MocA family protein [Methanospirillum stamsii]

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];
4-253 6.16e-74

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 229.81  E-value: 6.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLAS--GY-LCAVSDISSERANSLAGKYpGVRVETDWQSVIKDPEIDLVIISTSNNWLAPITL 80
Cdd:COG0673     4 LRVGIIGAGGIGRAHAPALAAlpGVeLVAVADRDPERAEAFAEEY-GVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  81 EAVFAGKHVLVEKPAARHYLEFDPIIEAMEESKSKVTVGYNLRFHPALKKAHSIIERGELGNIMYIRGRYGHgGRPGYEK 160
Cdd:COG0673    83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGH-PRPAGPA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 161 EWRADPEISGGGELLDQGVHLIDLSRWFLG-DFTKIHGSIRTYF-WNMPVEDNGFMYLETAQGQIAWLQVSCTEWKNLF- 237
Cdd:COG0673   162 DWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVpDRVEVDDTAAATLRFANGAVATLEASWVAPGGERd 241

                         250
                  ....*....|....*..
gi 2076732937 238 -SYEIFCEHGKLQIDGI 253
Cdd:COG0673   242 eRLEVYGTKGTLFVDAI 258
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
4-253 6.16e-74

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 229.81  E-value: 6.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLAS--GY-LCAVSDISSERANSLAGKYpGVRVETDWQSVIKDPEIDLVIISTSNNWLAPITL 80
Cdd:COG0673     4 LRVGIIGAGGIGRAHAPALAAlpGVeLVAVADRDPERAEAFAEEY-GVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  81 EAVFAGKHVLVEKPAARHYLEFDPIIEAMEESKSKVTVGYNLRFHPALKKAHSIIERGELGNIMYIRGRYGHgGRPGYEK 160
Cdd:COG0673    83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGH-PRPAGPA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 161 EWRADPEISGGGELLDQGVHLIDLSRWFLG-DFTKIHGSIRTYF-WNMPVEDNGFMYLETAQGQIAWLQVSCTEWKNLF- 237
Cdd:COG0673   162 DWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVpDRVEVDDTAAATLRFANGAVATLEASWVAPGGERd 241

                         250
                  ....*....|....*..
gi 2076732937 238 -SYEIFCEHGKLQIDGI 253
Cdd:COG0673   242 eRLEVYGTKGTLFVDAI 258
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 3-319 3.71e-34

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: 127.34  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   3 IMKVGIIGCGVIGHKRAESLASGY----LCAVSDISSERANSLAGKYPGVRVETDWQSVIKDPEIDLVIISTSNNWLAPI 78
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVpgarLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  79 TLEAVFAGKHVLVEKPAArhyLEFDPIIEAM---EESKSKVTVGYNLRFHPALKKAHSIIERGELGNIMYIRGrYGHGGR 155
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPID---LDLEEIKEALaavEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRI-TSRDPA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 156 PG---YEKewradpeiSGGGELLDQGVHLIDLSRWFLGD-FTKI--HGSIRTYfwnmPV------EDNGFMYLETAQGQI 223
Cdd:TIGR04380 157 PPpvaYVK--------VSGGLFLDMTIHDFDMARFLLGSeVEEVyaQGSVLVD----PAigeagdVDTAVITLKFENGAI 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 224 AWLQVScteWKNLFSY----EIFCEHGKLQIDgiggsygterltcykmlpqmGPPETTIW------------EYPFPD-- 285
Cdd:TIGR04380 225 AVIDNS---RRAAYGYdqrvEVFGSKGMLRAE--------------------NDTESTVIlydaegvrgdkpLNFFLEry 281

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2076732937 286 -NSWKEEFMDFEQKILTNKNPDPGIRDAREALKVV 319
Cdd:TIGR04380 282 rDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLA 316
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 4-120 5.90e-20

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: 83.80  E-value: 5.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESL---ASGY-LCAVSDISSERANSLAgKYPGVRVETDWQSVIKDPEIDLVIISTSNNWLAPIT 79
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALnasQPGAeLVAILDPNSERAEAVA-ESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2076732937  80 LEAVFAGKHVLVEKPAARHYLEFDPIIEAMEESKSKVTVGY 120
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
 4-183 4.52e-17

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 80.53  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLASGY----LCAVSdisSERANSLAGKYPGVRVETDWQSVIKDPEIDLVIISTSNNWLAPIT 79
Cdd:PRK11579    5 IRVGLIGYGYASKTFHAPLIAGTpgleLAAVS---SSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  80 LEAVFAGKHVLVEKP------AARHylefdpiIEAMEESKSKV-TVGYNLRFHPALKKAHSIIERGELGNIMYIRG---R 149
Cdd:PRK11579   82 KAALEAGKHVVVDKPftvtlsQARE-------LDALAKSAGRVlSVFHNRRWDSDFLTLKALLAEGVLGEVAYFEShfdR 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2076732937 150 YghggRPGYEKEWRADPEiSGGGELLDQGVHLID 183
Cdd:PRK11579  155 F----RPQVRQRWREQGG-PGSGIWYDLAPHLLD 183
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 4-90 9.05e-05

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: 42.14  E-value: 9.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLAS--GY-LCAVSDISSERANSLAGKY-----PGVRVETDWQSVIKDPEIDLVIISTSnNWL 75
Cdd:cd24146     1 IRVVVWGLGAMGRGIARYLLEkpGLeIVGAVDRDPAKVGKDLGELgggapLGVKVTDDLDAVLAATKPDVVVHATT-SFL 79

                          90
                  ....*....|....*...
gi 2076732937  76 APIT---LEAVFAGKHVL 90
Cdd:cd24146    80 ADVApqiERLLEAGLNVI 97
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
4-253 6.16e-74

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 229.81  E-value: 6.16e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLAS--GY-LCAVSDISSERANSLAGKYpGVRVETDWQSVIKDPEIDLVIISTSNNWLAPITL 80
Cdd:COG0673     4 LRVGIIGAGGIGRAHAPALAAlpGVeLVAVADRDPERAEAFAEEY-GVRVYTDYEELLADPDIDAVVIATPNHLHAELAI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  81 EAVFAGKHVLVEKPAARHYLEFDPIIEAMEESKSKVTVGYNLRFHPALKKAHSIIERGELGNIMYIRGRYGHgGRPGYEK 160
Cdd:COG0673    83 AALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGH-PRPAGPA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 161 EWRADPEISGGGELLDQGVHLIDLSRWFLG-DFTKIHGSIRTYF-WNMPVEDNGFMYLETAQGQIAWLQVSCTEWKNLF- 237
Cdd:COG0673   162 DWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVpDRVEVDDTAAATLRFANGAVATLEASWVAPGGERd 241

                         250
                  ....*....|....*..
gi 2076732937 238 -SYEIFCEHGKLQIDGI 253
Cdd:COG0673   242 eRLEVYGTKGTLFVDAI 258
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 3-319 3.71e-34

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: 127.34  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   3 IMKVGIIGCGVIGHKRAESLASGY----LCAVSDISSERANSLAGKYPGVRVETDWQSVIKDPEIDLVIISTSNNWLAPI 78
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENLATHVpgarLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  79 TLEAVFAGKHVLVEKPAArhyLEFDPIIEAM---EESKSKVTVGYNLRFHPALKKAHSIIERGELGNIMYIRGrYGHGGR 155
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPID---LDLEEIKEALaavEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGKPEILRI-TSRDPA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 156 PG---YEKewradpeiSGGGELLDQGVHLIDLSRWFLGD-FTKI--HGSIRTYfwnmPV------EDNGFMYLETAQGQI 223
Cdd:TIGR04380 157 PPpvaYVK--------VSGGLFLDMTIHDFDMARFLLGSeVEEVyaQGSVLVD----PAigeagdVDTAVITLKFENGAI 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 224 AWLQVScteWKNLFSY----EIFCEHGKLQIDgiggsygterltcykmlpqmGPPETTIW------------EYPFPD-- 285
Cdd:TIGR04380 225 AVIDNS---RRAAYGYdqrvEVFGSKGMLRAE--------------------NDTESTVIlydaegvrgdkpLNFFLEry 281

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2076732937 286 -NSWKEEFMDFEQKILTNKNPDPGIRDAREALKVV 319
Cdd:TIGR04380 282 rDAYRAEIQAFVDAILEGRPPPVTGEDGLKALLLA 316
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 4-120 5.90e-20

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: 83.80  E-value: 5.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESL---ASGY-LCAVSDISSERANSLAgKYPGVRVETDWQSVIKDPEIDLVIISTSNNWLAPIT 79
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALnasQPGAeLVAILDPNSERAEAVA-ESFGVEVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2076732937  80 LEAVFAGKHVLVEKPAARHYLEFDPIIEAMEESKSKVTVGY 120
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
PRK11579 PRK11579
putative oxidoreductase; Provisional
 4-183 4.52e-17

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 80.53  E-value: 4.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLASGY----LCAVSdisSERANSLAGKYPGVRVETDWQSVIKDPEIDLVIISTSNNWLAPIT 79
Cdd:PRK11579    5 IRVGLIGYGYASKTFHAPLIAGTpgleLAAVS---SSDATKVKADWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHFPLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  80 LEAVFAGKHVLVEKP------AARHylefdpiIEAMEESKSKV-TVGYNLRFHPALKKAHSIIERGELGNIMYIRG---R 149
Cdd:PRK11579   82 KAALEAGKHVVVDKPftvtlsQARE-------LDALAKSAGRVlSVFHNRRWDSDFLTLKALLAEGVLGEVAYFEShfdR 154

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2076732937 150 YghggRPGYEKEWRADPEiSGGGELLDQGVHLID 183
Cdd:PRK11579  155 F----RPQVRQRWREQGG-PGSGIWYDLAPHLLD 183
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 135-324 1.14e-15

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: 74.38  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 135 IERGELGNIMYIRGRYGHGGRP-GYEKEWRADPEISGGgELLDQGVHLIDLSRWFLGDFtKIHGSIRTYfwnmpvEDNGF 213
Cdd:pfam02894   4 IENGVLGEVVMVTVHTRDPFRPpQEFKRWRVDPEKSGG-ALYDLGIHTIDLLIYLFGEP-PSVVAVYAS------EDTAF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937 214 MYLETAQGQIAWLQVSCTEW--KNLFSYEIFCEHGKLQIDGIGGSYGT-----ERLTCYKM-LPQMGPPETTIWEYPFPD 285
Cdd:pfam02894  76 ATLEFKNGAVGTLETSGGSIveANGHRISIHGTKGSIELDGIDDGLLSvtvvgEPGWATDDpMVRKGGDEVPEFLGSFAG 155

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2076732937 286 NSWKeEFMDFEQKILTNKNPDPGIRDAREALKVVSTIYK 324
Cdd:pfam02894 156 GYLL-EYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYE 193
PRK10206 PRK10206
putative oxidoreductase; Provisional
 42-183 5.00e-09

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 56.76  E-value: 5.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  42 AGKYPGVRVETDWQSVIKDPEIDLVIIST---SNNWLAPITLEavfAGKHVLVEKPaarhyleFDPIIEAMEE----SKS 114
Cdd:PRK10206   44 APIYSHIHFTSDLDEVLNDPDVKLVVVCThadSHFEYAKRALE---AGKNVLVEKP-------FTPTLAEAKElfalAKS 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2076732937 115 K---VTVGYNLRFHPALKKAHSIIERGELGNIMYIRGRYGHggrpgYEKEWRADPEISGGGELLDQGVHLID 183
Cdd:PRK10206  114 KgltVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDY-----YRPVAETKPGLPQDGAFYGLGVHTMD 180
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 10-116 1.03e-08

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: 52.69  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  10 GCGVIGHKRAESLASG--------YLCAVSDISSERANSLAgkyPGVRVETDWQSVIKDPEIDLVIISTSNNWLAPITLE 81
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQqseiplelVAVADRDLLSKDPLALL---PDEPLTLDLDDLIAHPDPDVVVECASSEAVAELVLD 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2076732937  82 AVFAGKHVLVEKPAA----RHYLEfdpIIEAMEESKSKV 116
Cdd:pfam03447  78 ALKAGKDVVTASKGAladlALYEE---LREAAEANGARI 113
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 4-69 3.52e-07

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 50.83  E-value: 3.52e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076732937   4 MKVGIIGCGVIGhkraESLASGyLCA---------VSDISSERANSLAGKYpGVRVETDWQSVIKDPeiDLVIIS 69
Cdd:COG0345     3 MKIGFIGAGNMG----SAIIKG-LLKsgvppediiVSDRSPERLEALAERY-GVRVTTDNAEAAAQA--DVVVLA 69
PRK13304 PRK13304
aspartate dehydrogenase;
4-91 1.05e-06

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 49.22  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLASGY----LCAVSDISSERANSLAGKYPGVRVETdwqsvIKD--PEIDLVIISTSNNWLAP 77
Cdd:PRK13304    2 LKIGIVGCGAIASLITKAILSGRinaeLYAFYDRNLEKAENLASKTGAKACLS-----IDElvEDVDLVVECASVNAVEE 76

                          90
                  ....*....|....
gi 2076732937  78 ITLEAVFAGKHVLV 91
Cdd:PRK13304   77 VVPKSLENGKDVII 90
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 4-112 6.09e-06

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 47.37  E-value: 6.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIG-------HKRAESLA--SGY---LCAVS--DISSERANSLagkyPGVRVETDWQSVIKDPEIDLVI-- 67
Cdd:PRK06349    4 LKVGLLGLGTVGsgvvrilEENAEEIAarAGRpieIKKVAvrDLEKDRGVDL----PGILLTTDPEELVNDPDIDIVVel 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937  68 ---ISTSNNWLapitLEAVFAGKHV--------------LVEKPAARH-YLEFD-------PIIEAMEES 112
Cdd:PRK06349   80 mggIEPARELI----LKALEAGKHVvtankallavhgaeLFAAAEEKGvDLYFEaavaggiPIIKALREG 145
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
4-91 1.27e-05

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 45.95  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHK--RAESLASGYLCAVSDISSERANSLAGKyPGVRVETDWQSVIKDPeIDLVIISTSNNWLAPITLE 81
Cdd:COG1712     1 MRIGLIGCGAIGSEvaEALADAGVELVAVYDRDPERAEALLAS-LGARVVSDVDELLAAD-PDLVVEAASQAAVREHGPA 78

                          90
                  ....*....|
gi 2076732937  82 AVFAGKHVLV 91
Cdd:COG1712    79 VLEAGKDLMI 88
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 4-90 9.05e-05

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: 42.14  E-value: 9.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESLAS--GY-LCAVSDISSERANSLAGKY-----PGVRVETDWQSVIKDPEIDLVIISTSnNWL 75
Cdd:cd24146     1 IRVVVWGLGAMGRGIARYLLEkpGLeIVGAVDRDPAKVGKDLGELgggapLGVKVTDDLDAVLAATKPDVVVHATT-SFL 79

                          90
                  ....*....|....*...
gi 2076732937  76 APIT---LEAVFAGKHVL 90
Cdd:cd24146    80 ADVApqiERLLEAGLNVI 97
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-71 1.34e-04

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 42.88  E-value: 1.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2076732937   1 MIIMKVGIIGCGVIGHKRAESL-ASGY-LCAVSDISSERANSLAGKYPGVRVeTDWQSVIKDpeIDLVIISTS 71
Cdd:COG5495     1 MARMKIGIIGAGRVGTALAAALrAAGHeVVGVYSRSPASAERAAALLGAVPA-LDLEELAAE--ADLVLLAVP 70
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 4-92 3.73e-04

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 41.64  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2076732937   4 MKVGIIGCGVIGHKRAESL-ASGYLCAVSDISSERANSLAGKypGVRVETDWQSVIKDpeIDLVIISTSNnwlaPITLEA 82
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLlKAGHEVTVWNRTPAKAEALVAA--GARVAASPAEAAAA--ADVVITMLPD----DAAVEE 73

                          90
                  ....*....|
gi 2076732937  83 VFAGKHVLVE 92
Cdd:COG2084    74 VLLGEDGLLA 83
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 4-69 6.49e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 40.90  E-value: 6.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2076732937   4 MKVGIIGCGVIghkrAESLASGYLCA--------VSDISSERANSLAGKYpGVRVETDWQSVIKDPeiDLVIIS 69
Cdd:PRK11880    3 KKIGFIGGGNM----ASAIIGGLLASgvpakdiiVSDPSPEKRAALAEEY-GVRAATDNQEAAQEA--DVVVLA 69
PRK13303 PRK13303
aspartate dehydrogenase;
4-67 4.38e-03

aspartate dehydrogenase;


Pssm-ID: 237342 [Multi-domain]  Cd Length: 265  Bit Score: 37.99  E-value: 4.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2076732937   4 MKVGIIGCGVIGHKRAESLASGYLCAVSDI-----SSERANSLAGkyPGVRVETDWQSVIKDPeiDLVI 67
Cdd:PRK13303    2 MKVAMIGFGAIGAAVLELLEHDPDLRVDWVivpehSIDAVRRALG--EAVRVVSSVDALPQRP--DLVV 66
PRK07680 PRK07680
late competence protein ComER; Validated
 4-63 5.90e-03

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 37.64  E-value: 5.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2076732937   4 MKVGIIGCGVIGHKRAES-LASGYLCA----VSDISSERANSLAGKYPGVRVETDWQSVIKDPEI 63
Cdd:PRK07680    1 MNIGFIGTGNMGTILIEAfLESGAVKPsqltITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDL 65
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 4-53 7.95e-03

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 36.80  E-value: 7.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2076732937   4 MKVGIIGCGVIGHKRAESL-ASGYLCAVSDISSERANSLAGKYPGVRVETD 53
Cdd:cd01075    29 KTVAVQGLGKVGYKLAEHLlEEGAKLIVADINEEAVARAAELFGATVVAPE 79
 
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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