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Conserved domains on  [gi|498415214|ref|WP_010723926|]
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Gfo/Idh/MocA family protein [Enterococcus faecium]

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];
1-246 1.46e-69

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 218.25  E-value: 1.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   1 MKKYQWGIVGLGTIAHEFAESFNQ-ETSELTAVASRTSEKAENFARRYNIpKAYGSYQEMLDDAEIDIVYIAVPNRQHID 79
Cdd:COG0673    1 MDKLRVGIIGAGGIGRAHAPALAAlPGVELVAVADRDPERAEAFAEEYGV-RVYTDYEELLADPDIDAVVIATPNHLHAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214  80 HILAALEAGKHVLCEKAITMNKKELADAMRLAEEKNLILAEAMTIFNMPLYQQLRSIMDTGKLGALKMIQAPFGSYKEPD 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214 160 PKNRFFNPELA-GGALLDIGTYAVSFARFFLSSQPEVV---ASTMVPFETGIDEQSVTILRNKENELAAVSLTFQAKMPK 235
Cdd:COG0673  160 PADWRFDPELAgGGALLDLGIHDIDLARWLLGSEPESVsatGGRLVPDRVEVDDTAAATLRFANGAVATLEASWVAPGGE 239

                        250
                 ....*....|....
gi 498415214 236 VG---IVAFENGYV 246
Cdd:COG0673  240 RDerlEVYGTKGTL 253
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-246 1.46e-69

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 218.25  E-value: 1.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   1 MKKYQWGIVGLGTIAHEFAESFNQ-ETSELTAVASRTSEKAENFARRYNIpKAYGSYQEMLDDAEIDIVYIAVPNRQHID 79
Cdd:COG0673    1 MDKLRVGIIGAGGIGRAHAPALAAlPGVELVAVADRDPERAEAFAEEYGV-RVYTDYEELLADPDIDAVVIATPNHLHAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214  80 HILAALEAGKHVLCEKAITMNKKELADAMRLAEEKNLILAEAMTIFNMPLYQQLRSIMDTGKLGALKMIQAPFGSYKEPD 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214 160 PKNRFFNPELA-GGALLDIGTYAVSFARFFLSSQPEVV---ASTMVPFETGIDEQSVTILRNKENELAAVSLTFQAKMPK 235
Cdd:COG0673  160 PADWRFDPELAgGGALLDLGIHDIDLARWLLGSEPESVsatGGRLVPDRVEVDDTAAATLRFANGAVATLEASWVAPGGE 239

                        250
                 ....*....|....
gi 498415214 236 VG---IVAFENGYV 246
Cdd:COG0673  240 RDerlEVYGTKGTL 253
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 6-118 8.86e-32

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: 115.00  E-value: 8.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214    6 WGIVGLGTIAHEFAESFNQETS--ELTAVASRTSEKAENFARRYNIPkAYGSYQEMLDDAEIDIVYIAVPNRQHIDHILA 83
Cdd:pfam01408   3 VGIIGAGKIGSKHARALNASQPgaELVAILDPNSERAEAVAESFGVE-VYSDLEELLNDPEIDAVIVATPNGLHYDLAIA 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 498415214   84 ALEAGKHVLCEKAITMNKKELADAMRLAEEKNLIL 118
Cdd:pfam01408  82 ALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRV 116
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 3-196 1.82e-24

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: 101.14  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214    3 KYQWGIVGLGTIAHEFAES--FNQETSELTAVASRTSEKAENFARRYNIPKAYGSYQEMLDDAEIDIVYIAVPNRQHIDH 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENlaTHVPGARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   81 ILAALEAGKHVLCEKAITMNKKELADAMRLAEEKNLILaeaMTIFNM---PLYQQLRSIMDTGKLGALKMIQapfGSYKE 157
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKL---QIGFNRrfdPNFRRVKQLVEAGKIGKPEILR---ITSRD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 498415214  158 PDPknrffnPELA-----GGALLDIGTYAVSFARFFLSSQPEVV 196
Cdd:TIGR04380 155 PAP------PPVAyvkvsGGLFLDMTIHDFDMARFLLGSEVEEV 192
PRK11579 PRK11579
putative oxidoreductase; Provisional
 7-164 1.57e-09

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 58.19  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   7 GIVGLGTIAHEFAESFNQETS--ELTAVASRTSEKAEnfARRYNIPkAYGSYQEMLDDAEIDIVYIAVPNRQHIDHILAA 84
Cdd:PRK11579   8 GLIGYGYASKTFHAPLIAGTPglELAAVSSSDATKVK--ADWPTVT-VVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214  85 LEAGKHVLCEKAITMNKKELADAMRLAEEKNLILaeamTIFNMPLYQQ----LRSIMDTGKLGALKMIQAPFGSYKePDP 160
Cdd:PRK11579  85 LEAGKHVVVDKPFTVTLSQARELDALAKSAGRVL----SVFHNRRWDSdfltLKALLAEGVLGEVAYFESHFDRFR-PQV 159


                 ....
gi 498415214 161 KNRF 164
Cdd:PRK11579 160 RQRW 163
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-246 1.46e-69

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 218.25  E-value: 1.46e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   1 MKKYQWGIVGLGTIAHEFAESFNQ-ETSELTAVASRTSEKAENFARRYNIpKAYGSYQEMLDDAEIDIVYIAVPNRQHID 79
Cdd:COG0673    1 MDKLRVGIIGAGGIGRAHAPALAAlPGVELVAVADRDPERAEAFAEEYGV-RVYTDYEELLADPDIDAVVIATPNHLHAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214  80 HILAALEAGKHVLCEKAITMNKKELADAMRLAEEKNLILAEAMTIFNMPLYQQLRSIMDTGKLGALKMIQAPFGSYKEPD 159
Cdd:COG0673   80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214 160 PKNRFFNPELA-GGALLDIGTYAVSFARFFLSSQPEVV---ASTMVPFETGIDEQSVTILRNKENELAAVSLTFQAKMPK 235
Cdd:COG0673  160 PADWRFDPELAgGGALLDLGIHDIDLARWLLGSEPESVsatGGRLVPDRVEVDDTAAATLRFANGAVATLEASWVAPGGE 239

                        250
                 ....*....|....
gi 498415214 236 VG---IVAFENGYV 246
Cdd:COG0673  240 RDerlEVYGTKGTL 253
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 6-118 8.86e-32

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: 115.00  E-value: 8.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214    6 WGIVGLGTIAHEFAESFNQETS--ELTAVASRTSEKAENFARRYNIPkAYGSYQEMLDDAEIDIVYIAVPNRQHIDHILA 83
Cdd:pfam01408   3 VGIIGAGKIGSKHARALNASQPgaELVAILDPNSERAEAVAESFGVE-VYSDLEELLNDPEIDAVIVATPNGLHYDLAIA 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 498415214   84 ALEAGKHVLCEKAITMNKKELADAMRLAEEKNLIL 118
Cdd:pfam01408  82 ALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRV 116
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
 3-196 1.82e-24

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: 101.14  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214    3 KYQWGIVGLGTIAHEFAES--FNQETSELTAVASRTSEKAENFARRYNIPKAYGSYQEMLDDAEIDIVYIAVPNRQHIDH 80
Cdd:TIGR04380   1 KLKVGIIGAGRIGKVHAENlaTHVPGARLKAIVDPFADAAAELAEKLGIEPVTQDPEAALADPEIDAVLIASPTDTHADL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   81 ILAALEAGKHVLCEKAITMNKKELADAMRLAEEKNLILaeaMTIFNM---PLYQQLRSIMDTGKLGALKMIQapfGSYKE 157
Cdd:TIGR04380  81 IIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEKAGVKL---QIGFNRrfdPNFRRVKQLVEAGKIGKPEILR---ITSRD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 498415214  158 PDPknrffnPELA-----GGALLDIGTYAVSFARFFLSSQPEVV 196
Cdd:TIGR04380 155 PAP------PPVAyvkvsGGLFLDMTIHDFDMARFLLGSEVEEV 192
PRK11579 PRK11579
putative oxidoreductase; Provisional
 7-164 1.57e-09

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 58.19  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   7 GIVGLGTIAHEFAESFNQETS--ELTAVASRTSEKAEnfARRYNIPkAYGSYQEMLDDAEIDIVYIAVPNRQHIDHILAA 84
Cdd:PRK11579   8 GLIGYGYASKTFHAPLIAGTPglELAAVSSSDATKVK--ADWPTVT-VVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214  85 LEAGKHVLCEKAITMNKKELADAMRLAEEKNLILaeamTIFNMPLYQQ----LRSIMDTGKLGALKMIQAPFGSYKePDP 160
Cdd:PRK11579  85 LEAGKHVVVDKPFTVTLSQARELDALAKSAGRVL----SVFHNRRWDSdfltLKALLAEGVLGEVAYFESHFDRFR-PQV 159


                 ....
gi 498415214 161 KNRF 164
Cdd:PRK11579 160 RQRW 163
NAD_binding_3 pfam03447
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ...
 10-106 8.56e-09

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: 8.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   10 GLGTIAHEFAESFNQETSELT------AVASRTSEKAENFARRyniPKAYGSYQEMLDDAEIDIVYIAVPNRQHIDHILA 83
Cdd:pfam03447   1 GCGAIGSGVLEQLLRQQSEIPlelvavADRDLLSKDPLALLPD---EPLTLDLDDLIAHPDPDVVVECASSEAVAELVLD 77

                          90       100
                  ....*....|....*....|...
gi 498415214   84 ALEAGKHVlcekaITMNKKELAD 106
Cdd:pfam03447  78 ALKAGKDV-----VTASKGALAD 95
PRK10206 PRK10206
putative oxidoreductase; Provisional
 35-272 9.43e-08

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 52.90  E-value: 9.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214  35 RTSEKAENFARRYNIPKAYGSYQEMLDDAEIDIVYIAVPNRQHIDHILAALEAGKHVLCEKAITMNKKELADAMRLAEEK 114
Cdd:PRK10206  35 RRHAKPEEQAPIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214 115 NLILAEAMTIFNMPLYQQLRSIMDTGKLGALKMIQAPFGSYKePDPKNRFFNPElaGGALLDIGTYAVSfarfflssqpE 194
Cdd:PRK10206 115 GLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYR-PVAETKPGLPQ--DGAFYGLGVHTMD----------Q 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214 195 VVASTMVPFETGIDEQSvtiLRNKENElaavSLTFQAKM--PKVGIVAFENGYVTIaDYPRadraeiLFTDGTK-EFIES 271
Cdd:PRK10206 182 IISLFGRPDHVAYDIRS---LRNKANP----DDTFEAQLfyGDLKAIVKTSHLVKI-DYPK------FIVHGKKgSFIKY 247


                 .
gi 498415214 272 G 272
Cdd:PRK10206 248 G 248
PRK06349 PRK06349
homoserine dehydrogenase; Provisional
 1-121 1.82e-07

homoserine dehydrogenase; Provisional


Pssm-ID: 235783 [Multi-domain]  Cd Length: 426  Bit Score: 52.00  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   1 MKKYQWGIVGLGTI-----------AHEFAESFNQETsELTAVASRTSEKAenfaRRYNIPKAY--GSYQEMLDDAEIDI 67
Cdd:PRK06349   1 MKPLKVGLLGLGTVgsgvvrileenAEEIAARAGRPI-EIKKVAVRDLEKD----RGVDLPGILltTDPEELVNDPDIDI 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498415214  68 VyIAV-----PNRqhiDHILAALEAGKHVlcekaITMNK-------KELADAmrlAEEKNLILA-EA 121
Cdd:PRK06349  76 V-VELmggiePAR---ELILKALEAGKHV-----VTANKallavhgAELFAA---AEEKGVDLYfEA 130
PRK13304 PRK13304
aspartate dehydrogenase;
7-115 4.72e-06

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 47.29  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214   7 GIVGLGTIAHEFAESFNQET--SELTAVASRTSEKAENFARRYNiPKAYGSYQEMLDDaeIDIVYIAVPNRQHIDHILAA 84
Cdd:PRK13304   5 GIVGCGAIASLITKAILSGRinAELYAFYDRNLEKAENLASKTG-AKACLSIDELVED--VDLVVECASVNAVEEVVPKS 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 498415214  85 LEAGKHVlcekaITMNKKELADA------MRLAEEKN 115
Cdd:PRK13304  82 LENGKDV-----IIMSVGALADKelflklYKLAKENN 113
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-73 8.89e-06

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 46.34  E-value: 8.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498415214   1 MKKYQWGIVGLGTIAHEFAESFNQETSELTAVASRTSEKAENFARRYNIpKAYGSYQEMLDDAeiDIVYIAVP 73
Cdd:COG5495    1 MARMKIGIIGAGRVGTALAAALRAAGHEVVGVYSRSPASAERAAALLGA-VPALDLEELAAEA--DLVLLAVP 70
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
7-86 2.38e-05

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 42.22  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214    7 GIVGLGTIAHEFAESF-NQETSELTAVASRTSEKAENFARRYNIPKAYGSYQEMLDDAeiDIVYIAVPnRQHIDHILAAL 85
Cdd:pfam03807   1 GFIGAGNMGEALARGLvAAGPHEVVVANSRNPEKAEELAEEYGVGATAVDNEEAAEEA--DVVFLAVK-PEDAPDVLSEL 77


                  .
gi 498415214   86 E 86
Cdd:pfam03807  78 S 78
PRK06270 PRK06270
homoserine dehydrogenase; Provisional
 58-128 6.59e-04

homoserine dehydrogenase; Provisional


Pssm-ID: 235763 [Multi-domain]  Cd Length: 341  Bit Score: 41.00  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498415214  58 EMLDDAEIDIVYIAVPNRQH-----IDHILAALEAGKHVlcekaITMNKKELADA----MRLAEEKNLIL------AEAM 122
Cdd:PRK06270  83 EVIRSVDADVVVEATPTNIEtgepaLSHCRKALERGKHV-----VTSNKGPLALAykelKELAKKNGVRFryeatvGGAM 157


                 ....*.
gi 498415214 123 TIFNMP 128
Cdd:PRK06270 158 PIINLA 163
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
 134-197 5.01e-03

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: 37.40  E-value: 5.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498415214  134 RSIMDTGKLGALKMIQ-APFGSYKEPDP-KNRFFNPELAGGALLDIGTYAVSFARFFLSSQPEVVA 197
Cdd:pfam02894   1 KELIENGVLGEVVMVTvHTRDPFRPPQEfKRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVVA 66
 
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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