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Conserved domains on  [gi|16129276|ref|NP_415831|]
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D-glucoside 3-dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
7-351 3.52e-80

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 246.76  E-value: 3.52e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   7 SSPLRVAIIGAGQVAdKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGnASVWDDPQAMLLAVKPDVVSVCSPNRFHY 86
Cdd:COG0673   1 MDKLRVGIIGAGGIG-RAHAPALAALPGVELVAVADRDPERAEAFAEEYG-VRVYTDYEELLADPDIDAVVIATPNHLHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276  87 EHTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLGEIYVTTARALRRCGV 166
Cdd:COG0673  79 ELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276 167 PGWGVFTNKELQGGGPLIDIGIHMLDAAMYVLGFPaVKSVNAHSfqkigtqkscgqfGEWDPATYSVEDSLFGTIEFHNG 246
Cdd:COG0673 159 GPADWRFDPELAGGGALLDLGIHDIDLARWLLGSE-PESVSATG-------------GRLVPDRVEVDDTAAATLRFANG 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276 247 GILWLETSFALNIREQSiMNVSFCGDKAGatlfpahiytdnngelmtlmqreiaddnrhlrsmeAFINHVQGKPVMIADA 326
Cdd:COG0673 225 AVATLEASWVAPGGERD-ERLEVYGTKGT-----------------------------------LFVDAIRGGEPPPVSL 268

                       330       340
                ....*....|....*....|....*
gi 16129276 327 EQGYIIQQLVAALYQSAETGTRVEL 351
Cdd:COG0673 269 EDGLRALELAEAAYESARTGRRVEL 293
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
7-351 3.52e-80

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 246.76  E-value: 3.52e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   7 SSPLRVAIIGAGQVAdKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGnASVWDDPQAMLLAVKPDVVSVCSPNRFHY 86
Cdd:COG0673   1 MDKLRVGIIGAGGIG-RAHAPALAALPGVELVAVADRDPERAEAFAEEYG-VRVYTDYEELLADPDIDAVVIATPNHLHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276  87 EHTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLGEIYVTTARALRRCGV 166
Cdd:COG0673  79 ELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276 167 PGWGVFTNKELQGGGPLIDIGIHMLDAAMYVLGFPaVKSVNAHSfqkigtqkscgqfGEWDPATYSVEDSLFGTIEFHNG 246
Cdd:COG0673 159 GPADWRFDPELAGGGALLDLGIHDIDLARWLLGSE-PESVSATG-------------GRLVPDRVEVDDTAAATLRFANG 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276 247 GILWLETSFALNIREQSiMNVSFCGDKAGatlfpahiytdnngelmtlmqreiaddnrhlrsmeAFINHVQGKPVMIADA 326
Cdd:COG0673 225 AVATLEASWVAPGGERD-ERLEVYGTKGT-----------------------------------LFVDAIRGGEPPPVSL 268

                       330       340
                ....*....|....*....|....*
gi 16129276 327 EQGYIIQQLVAALYQSAETGTRVEL 351
Cdd:COG0673 269 EDGLRALELAEAAYESARTGRRVEL 293
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 10-130 3.18e-43

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: 145.43  E-value: 3.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276    10 LRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGnASVWDDPQAMLLAVKPDVVSVCSPNRFHYEHT 89
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEAVAESFG-VEVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 16129276    90 LMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDF 130
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 9-242 2.29e-27

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: 109.62  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276     9 PLRVAIIGAGQVAdKVHASYYCTRN-DLELVAVCDSRLSQAQALAEKYGNASVWDDPQAMLLAVKPDVVSVCSPNRFHYE 87
Cdd:TIGR04380   1 KLKVGIIGAGRIG-KVHAENLATHVpGARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276    88 HTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLG--EIYVTTAR------ 159
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGkpEILRITSRdpappp 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   160 --ALRRCGvpgwGVFtnkelqgggplIDIGIHMLDAAMYVLGFP-----AVKSVNAHsfqkigtqKSCGQFGEWDPA--T 230
Cdd:TIGR04380 160 vaYVKVSG----GLF-----------LDMTIHDFDMARFLLGSEveevyAQGSVLVD--------PAIGEAGDVDTAviT 216

                         250
                  ....*....|..
gi 16129276   231 YSVEDSLFGTIE 242
Cdd:TIGR04380 217 LKFENGAIAVID 228
PRK11579 PRK11579
putative oxidoreductase; Provisional
 7-201 5.34e-17

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 80.92  E-value: 5.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276    7 SSPLRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQAlaeKYGNASVWDDPQAMLLAVKPDVVSVCSPNRFHY 86
Cdd:PRK11579   2 SDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKA---DWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   87 EHTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYdFHH-RFALDTQQLREQVTNGVLGEI-YVTTARALRRC 164
Cdd:PRK11579  79 PLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSV-FHNrRWDSDFLTLKALLAEGVLGEVaYFESHFDRFRP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 16129276  165 GV-PGWgvftnKELQGGGPLI--DIGIHMLDAAMYVLGFP 201
Cdd:PRK11579 158 QVrQRW-----REQGGPGSGIwyDLAPHLLDQAIQLFGLP 192
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 10-121 1.64e-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: 47.15  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276  10 LRVAIIGAGQVAdKVHASYYCTRNDLELVAVCDSRLSQA-----QALAEKYGNASVWDDPQAMLLAVKPDVVSVCSPNRF 84
Cdd:cd24146   1 IRVVVWGLGAMG-RGIARYLLEKPGLEIVGAVDRDPAKVgkdlgELGGGAPLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 16129276  85 H--YEHTLMALEAGCHVM--CEK---PPAMTPEQAREMCDTARK 121
Cdd:cd24146  80 AdvAPQIERLLEAGLNVIttCEElfyPWARDPELAEELDALAKE 123
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
7-351 3.52e-80

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 246.76  E-value: 3.52e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   7 SSPLRVAIIGAGQVAdKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGnASVWDDPQAMLLAVKPDVVSVCSPNRFHY 86
Cdd:COG0673   1 MDKLRVGIIGAGGIG-RAHAPALAALPGVELVAVADRDPERAEAFAEEYG-VRVYTDYEELLADPDIDAVVIATPNHLHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276  87 EHTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLGEIYVTTARALRRCGV 166
Cdd:COG0673  79 ELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276 167 PGWGVFTNKELQGGGPLIDIGIHMLDAAMYVLGFPaVKSVNAHSfqkigtqkscgqfGEWDPATYSVEDSLFGTIEFHNG 246
Cdd:COG0673 159 GPADWRFDPELAGGGALLDLGIHDIDLARWLLGSE-PESVSATG-------------GRLVPDRVEVDDTAAATLRFANG 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276 247 GILWLETSFALNIREQSiMNVSFCGDKAGatlfpahiytdnngelmtlmqreiaddnrhlrsmeAFINHVQGKPVMIADA 326
Cdd:COG0673 225 AVATLEASWVAPGGERD-ERLEVYGTKGT-----------------------------------LFVDAIRGGEPPPVSL 268

                       330       340
                ....*....|....*....|....*
gi 16129276 327 EQGYIIQQLVAALYQSAETGTRVEL 351
Cdd:COG0673 269 EDGLRALELAEAAYESARTGRRVEL 293
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 10-130 3.18e-43

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: 145.43  E-value: 3.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276    10 LRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGnASVWDDPQAMLLAVKPDVVSVCSPNRFHYEHT 89
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNASQPGAELVAILDPNSERAEAVAESFG-VEVYSDLEELLNDPEIDAVIVATPNGLHYDLA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 16129276    90 LMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDF 130
Cdd:pfam01408  80 IAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVGF 120
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 142-351 1.42e-38

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: 136.39  E-value: 1.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   142 REQVTNGVLGEIYVTTARaLRRCGVP-----GWGVftnKELQGGGPLIDIGIHMLDAAMYVLG-FPAVKSVNAHsfqkig 215
Cdd:pfam02894   1 KELIENGVLGEVVMVTVH-TRDPFRPpqefkRWRV---DPEKSGGALYDLGIHTIDLLIYLFGePPSVVAVYAS------ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   216 tqkscgqfgewdpatysvEDSLFGTIEFHNGGILWLETSfALNIREQSIMNVSFCGDKAGATLFPAHiytDNNGELMTLM 295
Cdd:pfam02894  71 ------------------EDTAFATLEFKNGAVGTLETS-GGSIVEANGHRISIHGTKGSIELDGID---DGLLSVTVVG 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129276   296 QREIADDNR-------------------HLRSMEAFINHVQGKPVMIADAEQGYIIQQLVAALYQSAETGTRVEL 351
Cdd:pfam02894 129 EPGWATDDPmvrkggdevpeflgsfaggYLLEYDAFLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 9-242 2.29e-27

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: 109.62  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276     9 PLRVAIIGAGQVAdKVHASYYCTRN-DLELVAVCDSRLSQAQALAEKYGNASVWDDPQAMLLAVKPDVVSVCSPNRFHYE 87
Cdd:TIGR04380   1 KLKVGIIGAGRIG-KVHAENLATHVpGARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276    88 HTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLG--EIYVTTAR------ 159
Cdd:TIGR04380  80 LIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKLQIGFNRRFDPNFRRVKQLVEAGKIGkpEILRITSRdpappp 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   160 --ALRRCGvpgwGVFtnkelqgggplIDIGIHMLDAAMYVLGFP-----AVKSVNAHsfqkigtqKSCGQFGEWDPA--T 230
Cdd:TIGR04380 160 vaYVKVSG----GLF-----------LDMTIHDFDMARFLLGSEveevyAQGSVLVD--------PAIGEAGDVDTAviT 216

                         250
                  ....*....|..
gi 16129276   231 YSVEDSLFGTIE 242
Cdd:TIGR04380 217 LKFENGAIAVID 228
PRK11579 PRK11579
putative oxidoreductase; Provisional
 7-201 5.34e-17

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 80.92  E-value: 5.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276    7 SSPLRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQAlaeKYGNASVWDDPQAMLLAVKPDVVSVCSPNRFHY 86
Cdd:PRK11579   2 SDKIRVGLIGYGYASKTFHAPLIAGTPGLELAAVSSSDATKVKA---DWPTVTVVSEPQHLFNDPNIDLIVIPTPNDTHF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   87 EHTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYdFHH-RFALDTQQLREQVTNGVLGEI-YVTTARALRRC 164
Cdd:PRK11579  79 PLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSV-FHNrRWDSDFLTLKALLAEGVLGEVaYFESHFDRFRP 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 16129276  165 GV-PGWgvftnKELQGGGPLI--DIGIHMLDAAMYVLGFP 201
Cdd:PRK11579 158 QVrQRW-----REQGGPGSGIwyDLAPHLLDQAIQLFGLP 192
PRK10206 PRK10206
putative oxidoreductase; Provisional
 10-201 3.45e-11

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 63.69  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   10 LRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGNASVWDDPQAMLLAVKPDVVSVCSPNRFHYEHT 89
Cdd:PRK10206   2 INCAFIGFGKSTTRYHLPYVLNRKDSWHVAHIFRRHAKPEEQAPIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   90 LMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLGEIYVTTAR-------ALR 162
Cdd:PRK10206  82 KRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHfdyyrpvAET 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16129276  163 RCGVPGWGVFTNkelqgggplidIGIHMLDAAMYVLGFP 201
Cdd:PRK10206 162 KPGLPQDGAFYG-----------LGVHTMDQIISLFGRP 189
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 10-121 1.64e-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: 47.15  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276  10 LRVAIIGAGQVAdKVHASYYCTRNDLELVAVCDSRLSQA-----QALAEKYGNASVWDDPQAMLLAVKPDVVSVCSPNRF 84
Cdd:cd24146   1 IRVVVWGLGAMG-RGIARYLLEKPGLEIVGAVDRDPAKVgkdlgELGGGAPLGVKVTDDLDAVLAATKPDVVVHATTSFL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 16129276  85 H--YEHTLMALEAGCHVM--CEK---PPAMTPEQAREMCDTARK 121
Cdd:cd24146  80 AdvAPQIERLLEAGLNVIttCEElfyPWARDPELAEELDALAKE 123
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 34-129 2.16e-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: 43.06  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276    34 DLELVAVCDSRLSQAQALAEKyGNASVWDDPQAMLLAVKPDVVSVCSPNRFHYEHTLMALEAGCHVMCEKPPAMTPEQAR 113
Cdd:pfam03447  21 PLELVAVADRDLLSKDPLALL-PDEPLTLDLDDLIAHPDPDVVVECASSEAVAELVLDALKAGKDVVTASKGALADLALY 99

                          90
                  ....*....|....*..
gi 16129276   114 EMC-DTARKLGKVLAYD 129
Cdd:pfam03447 100 EELrEAAEANGARIYVE 116
PRK13304 PRK13304
aspartate dehydrogenase;
10-100 1.02e-03

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 40.36  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   10 LRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQALAEKyGNASVWDDPQAMLLAVkpDVVSVCSPNRFHYEHT 89
Cdd:PRK13304   2 LKIGIVGCGAIASLITKAILSGRINAELYAFYDRNLEKAENLASK-TGAKACLSIDELVEDV--DLVVECASVNAVEEVV 78

                         90
                 ....*....|.
gi 16129276   90 LMALEAGCHVM 100
Cdd:PRK13304  79 PKSLENGKDVI 89
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 11-96 5.32e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 38.20  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   11 RVAIIGAGQ---------VADKVHASYyctrndlelVAVCDSRLSQAQALAEKYG------NASVWDDPQAMLLAVKPDV 75
Cdd:PRK11880   4 KIGFIGGGNmasaiigglLASGVPAKD---------IIVSDPSPEKRAALAEEYGvraatdNQEAAQEADVVVLAVKPQV 74

                         90       100
                 ....*....|....*....|..
gi 16129276   76 V-SVCSPNRFHYEHTLMALEAG 96
Cdd:PRK11880  75 MeEVLSELKGQLDKLVVSIAAG 96
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 8-81 8.06e-03

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: 37.35  E-value: 8.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276   8 SPLRVAIIGAGQ---------VADKVHAsyyctrndlELVAVCDSRLSQAQALAEKYG------NASVWDDPQAMLLAVK 72
Cdd:COG0345   1 MSMKIGFIGAGNmgsaiikglLKSGVPP---------EDIIVSDRSPERLEALAERYGvrvttdNAEAAAQADVVVLAVK 71

                        90
                ....*....|
gi 16129276  73 P-DVVSVCSP 81
Cdd:COG0345  72 PqDLAEVLEE 81
OCDMu COG2423
Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid ...
 11-106 8.20e-03

Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family [Amino acid transport and metabolism]; Ornithine cyclodeaminase/archaeal alanine dehydrogenase, mu-crystallin family is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 441972 [Multi-domain]  Cd Length: 322  Bit Score: 37.82  E-value: 8.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129276  11 RVAIIGAGQVAdKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYG----NASVWDDPQAMLLAVkpDVVSVCSPNR--- 83
Cdd:COG2423 129 TLGIIGAGVQA-RTQLRALAAVRPIERVRVWGRDPEKAEAFAARLAaeglPVEAADDLEEAVADA--DIIVTATPSRepv 205

                        90       100       110
                ....*....|....*....|....*....|..
gi 16129276  84 FHYEHtlmaLEAGCHV---------MCEKPPA 106
Cdd:COG2423 206 LRGEW----LRPGTHInavgadtpgKRELDPA 233
 
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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