NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1304133749|gb|AUC95828|]
View 

oxidoreductase [Bradyrhizobium sp. SK17]

Protein Classification

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-380 8.72e-54

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 179.73  E-value: 8.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749   1 MTTKRLGLImnGiTGRMGlNQHLIrsivAIREQGGVLLSngdrimpdpILVGRDAEKVAGLAKRYNIeRHTTDLDRALAD 80
Cdd:COG0673     1 MDKLRVGII--G-AGGIG-RAHAP----ALAALPGVELV---------AVADRDPERAEAFAEEYGV-RVYTDYEELLAD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  81 KD-DTVFfDAATTQARPSLLTKAINAGKHVYCEKPIATNLEEAVAVVKLANAKGLKHGTVQDKLFLPGLKKLAFLRDSGF 159
Cdd:COG0673    63 PDiDAVV-IATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 160 FGRMLSVRGEFGYWvfeggWQEAQRPSWNYRAEDGGGIILDMVCHWRYVLDNLFG-EVESVVCIGNTDIPERYDekgkky 238
Cdd:COG0673   142 IGEIRSVRARFGHP-----RPAGPADWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDRVE------ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 239 qatADDSAYATFRLKGGVIAHINMSWVTRVYRDDLvTFQVDGTHGSavagltdcmiqarqatprpvwnpdekrmhdfyad 318
Cdd:COG0673   211 ---VDDTAAATLRFANGAVATLEASWVAPGGERDE-RLEVYGTKGT---------------------------------- 252
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304133749 319 wqklpenvvydngfkeqweMFIRHVCEDAPYKYTLLEGAKGVQLAECALKSWKERRWIDVAP 380
Cdd:COG0673   253 -------------------LFVDAIRGGEPPPVSLEDGLRALELAEAAYESARTGRRVELPD 295
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-380 8.72e-54

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 179.73  E-value: 8.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749   1 MTTKRLGLImnGiTGRMGlNQHLIrsivAIREQGGVLLSngdrimpdpILVGRDAEKVAGLAKRYNIeRHTTDLDRALAD 80
Cdd:COG0673     1 MDKLRVGII--G-AGGIG-RAHAP----ALAALPGVELV---------AVADRDPERAEAFAEEYGV-RVYTDYEELLAD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  81 KD-DTVFfDAATTQARPSLLTKAINAGKHVYCEKPIATNLEEAVAVVKLANAKGLKHGTVQDKLFLPGLKKLAFLRDSGF 159
Cdd:COG0673    63 PDiDAVV-IATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 160 FGRMLSVRGEFGYWvfeggWQEAQRPSWNYRAEDGGGIILDMVCHWRYVLDNLFG-EVESVVCIGNTDIPERYDekgkky 238
Cdd:COG0673   142 IGEIRSVRARFGHP-----RPAGPADWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDRVE------ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 239 qatADDSAYATFRLKGGVIAHINMSWVTRVYRDDLvTFQVDGTHGSavagltdcmiqarqatprpvwnpdekrmhdfyad 318
Cdd:COG0673   211 ---VDDTAAATLRFANGAVATLEASWVAPGGERDE-RLEVYGTKGT---------------------------------- 252
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304133749 319 wqklpenvvydngfkeqweMFIRHVCEDAPYKYTLLEGAKGVQLAECALKSWKERRWIDVAP 380
Cdd:COG0673   253 -------------------LFVDAIRGGEPPPVSLEDGLRALELAEAAYESARTGRRVELPD 295
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
54-376 5.50e-23

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: 98.06  E-value: 5.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  54 DAEKVAGLAKRYNIERHTTDLDRALADKD-DTVFFDAAT-TQArpSLLTKAINAGKHVYCEKPIATNLEEAVAVVKLANA 131
Cdd:TIGR04380  36 FADAAAELAEKLGIEPVTQDPEAALADPEiDAVLIASPTdTHA--DLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 132 KGLKhgtVQ---DKLFLPGLKKLAFLRDSGFFGRMLSVRGEFgywvfeggwQEAQRPSWNYrAEDGGGIILDMVCH---- 204
Cdd:TIGR04380 114 AGVK---LQigfNRRFDPNFRRVKQLVEAGKIGKPEILRITS---------RDPAPPPVAY-VKVSGGLFLDMTIHdfdm 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 205 WRYVLDNlfgEVESVVCIGNTDIPERYDEKGkkyqataD-DSAYATFRLKGGVIAHINMSWVTrVYRDDlVTFQVDGTHG 283
Cdd:TIGR04380 181 ARFLLGS---EVEEVYAQGSVLVDPAIGEAG-------DvDTAVITLKFENGAIAVIDNSRRA-AYGYD-QRVEVFGSKG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 284 SAVAGLtdcmiqaRQATPRPVWNPD----EKRMHDFyadWQKlpenvvYDNGFKEQWEMFIRHVCEDAPYKYTLLEGAKG 359
Cdd:TIGR04380 249 MLRAEN-------DTESTVILYDAEgvrgDKPLNFF---LER------YRDAYRAEIQAFVDAILEGRPPPVTGEDGLKA 312
                         330
                  ....*....|....*..
gi 1304133749 360 VQLAECALKSWKERRWI 376
Cdd:TIGR04380 313 LLLALAAKRSLEEGRPV 329
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
50-135 1.22e-11

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: 61.07  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  50 LVGRDAEKVAGLAKRYNIErHTTDLDRALADKD-DTVFfdAAT-TQARPSLLTKAINAGKHVYCEKPIATNLEEAVAVVK 127
Cdd:pfam01408  31 ILDPNSERAEAVAESFGVE-VYSDLEELLNDPEiDAVI--VATpNGLHYDLAIAALEAGKHVLCEKPLATTVEEAKELVE 107

                  ....*...
gi 1304133749 128 LANAKGLK 135
Cdd:pfam01408 108 LAKKKGVR 115
PRK10206 PRK10206
putative oxidoreductase; Provisional
62-173 7.82e-06

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 47.51  E-value: 7.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  62 AKRYNIERHTTDLDRALADKDDTVFFDAATTQARPSLLTKAINAGKHVYCEKPIATNLEEAVAVVKLANAKGLKHGTVQ- 140
Cdd:PRK10206   44 APIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQn 123
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1304133749 141 ---DKLFLPGLKKLaflrDSGFFGRMLSVRGEFGYW 173
Cdd:PRK10206  124 rrfDSCFLTAKKAI----ESGKLGEIVEVESHFDYY 155
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-380 8.72e-54

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 179.73  E-value: 8.72e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749   1 MTTKRLGLImnGiTGRMGlNQHLIrsivAIREQGGVLLSngdrimpdpILVGRDAEKVAGLAKRYNIeRHTTDLDRALAD 80
Cdd:COG0673     1 MDKLRVGII--G-AGGIG-RAHAP----ALAALPGVELV---------AVADRDPERAEAFAEEYGV-RVYTDYEELLAD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  81 KD-DTVFfDAATTQARPSLLTKAINAGKHVYCEKPIATNLEEAVAVVKLANAKGLKHGTVQDKLFLPGLKKLAFLRDSGF 159
Cdd:COG0673    63 PDiDAVV-IATPNHLHAELAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 160 FGRMLSVRGEFGYWvfeggWQEAQRPSWNYRAEDGGGIILDMVCHWRYVLDNLFG-EVESVVCIGNTDIPERYDekgkky 238
Cdd:COG0673   142 IGEIRSVRARFGHP-----RPAGPADWRFDPELAGGGALLDLGIHDIDLARWLLGsEPESVSATGGRLVPDRVE------ 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 239 qatADDSAYATFRLKGGVIAHINMSWVTRVYRDDLvTFQVDGTHGSavagltdcmiqarqatprpvwnpdekrmhdfyad 318
Cdd:COG0673   211 ---VDDTAAATLRFANGAVATLEASWVAPGGERDE-RLEVYGTKGT---------------------------------- 252
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304133749 319 wqklpenvvydngfkeqweMFIRHVCEDAPYKYTLLEGAKGVQLAECALKSWKERRWIDVAP 380
Cdd:COG0673   253 -------------------LFVDAIRGGEPPPVSLEDGLRALELAEAAYESARTGRRVELPD 295
myo_inos_iolG TIGR04380
inositol 2-dehydrogenase; All members of the seed alignment for this model are known or ...
54-376 5.50e-23

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: 98.06  E-value: 5.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  54 DAEKVAGLAKRYNIERHTTDLDRALADKD-DTVFFDAAT-TQArpSLLTKAINAGKHVYCEKPIATNLEEAVAVVKLANA 131
Cdd:TIGR04380  36 FADAAAELAEKLGIEPVTQDPEAALADPEiDAVLIASPTdTHA--DLIIEAAAAGKHIFCEKPIDLDLEEIKEALAAVEK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 132 KGLKhgtVQ---DKLFLPGLKKLAFLRDSGFFGRMLSVRGEFgywvfeggwQEAQRPSWNYrAEDGGGIILDMVCH---- 204
Cdd:TIGR04380 114 AGVK---LQigfNRRFDPNFRRVKQLVEAGKIGKPEILRITS---------RDPAPPPVAY-VKVSGGLFLDMTIHdfdm 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 205 WRYVLDNlfgEVESVVCIGNTDIPERYDEKGkkyqataD-DSAYATFRLKGGVIAHINMSWVTrVYRDDlVTFQVDGTHG 283
Cdd:TIGR04380 181 ARFLLGS---EVEEVYAQGSVLVDPAIGEAG-------DvDTAVITLKFENGAIAVIDNSRRA-AYGYD-QRVEVFGSKG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 284 SAVAGLtdcmiqaRQATPRPVWNPD----EKRMHDFyadWQKlpenvvYDNGFKEQWEMFIRHVCEDAPYKYTLLEGAKG 359
Cdd:TIGR04380 249 MLRAEN-------DTESTVILYDAEgvrgDKPLNFF---LER------YRDAYRAEIQAFVDAILEGRPPPVTGEDGLKA 312
                         330
                  ....*....|....*..
gi 1304133749 360 VQLAECALKSWKERRWI 376
Cdd:TIGR04380 313 LLLALAAKRSLEEGRPV 329
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
50-135 1.22e-11

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: 61.07  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  50 LVGRDAEKVAGLAKRYNIErHTTDLDRALADKD-DTVFfdAAT-TQARPSLLTKAINAGKHVYCEKPIATNLEEAVAVVK 127
Cdd:pfam01408  31 ILDPNSERAEAVAESFGVE-VYSDLEELLNDPEiDAVI--VATpNGLHYDLAIAALEAGKHVLCEKPLATTVEEAKELVE 107

                  ....*...
gi 1304133749 128 LANAKGLK 135
Cdd:pfam01408 108 LAKKKGVR 115
GFO_IDH_MocA_C pfam02894
Oxidoreductase family, C-terminal alpha/beta domain; This family of enzymes utilize NADP or ...
156-378 6.03e-07

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: 49.72  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 156 DSGFFGRMLSVRG-EFGYWVfeggwQEAQRPSWNYRAEDGGGIILDMVCHWRYVLDNLFGEVESVVcigntdiperydek 234
Cdd:pfam02894   5 ENGVLGEVVMVTVhTRDPFR-----PPQEFKRWRVDPEKSGGALYDLGIHTIDLLIYLFGEPPSVV-------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 235 gkkYQATADDSAYATFRLKGGVIAHINMSWvTRVYRDDLVTFQVDGTHGSAVAGLTD-----CMI--QARQATPRPVWNP 307
Cdd:pfam02894  66 ---AVYASEDTAFATLEFKNGAVGTLETSG-GSIVEANGHRISIHGTKGSIELDGIDdgllsVTVvgEPGWATDDPMVRK 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304133749 308 DEKRMHDFYADWQKLpENVVYDNgfkeqwemFIRHVCEDAPYKYTLLEGAKGVQLAECALKSWKERRWIDV 378
Cdd:pfam02894 142 GGDEVPEFLGSFAGG-YLLEYDA--------FLEAVRGGKVVLVDAEDGLYALAVIEAAYESAEEGRPVKL 203
PRK10206 PRK10206
putative oxidoreductase; Provisional
62-173 7.82e-06

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 47.51  E-value: 7.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  62 AKRYNIERHTTDLDRALADKDDTVFFDAATTQARPSLLTKAINAGKHVYCEKPIATNLEEAVAVVKLANAKGLKHGTVQ- 140
Cdd:PRK10206   44 APIYSHIHFTSDLDEVLNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQn 123
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1304133749 141 ---DKLFLPGLKKLaflrDSGFFGRMLSVRGEFGYW 173
Cdd:PRK10206  124 rrfDSCFLTAKKAI----ESGKLGEIVEVESHFDYY 155
PRK11579 PRK11579
putative oxidoreductase; Provisional
98-286 4.52e-04

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 42.01  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749  98 LLTKAINAGKHVYCEKPIATNLEEAVAVVKLANAKGLK----HGTVQDKLFLPgLKKLafLRDsgffGRMlsvrGEFGYw 173
Cdd:PRK11579   80 LAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVlsvfHNRRWDSDFLT-LKAL--LAE----GVL----GEVAY- 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304133749 174 vFEGG---WQEAQRPSWNYRAEDGGGIILDMVCHwryVLD---NLFGEVESVvcigNTDIPERydekgkKYQATADDSAY 247
Cdd:PRK11579  148 -FESHfdrFRPQVRQRWREQGGPGSGIWYDLAPH---LLDqaiQLFGLPVSI----TVDLAQL------RPGAQSTDYFH 213
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1304133749 248 ATFRLKG-GVIAHINMSWVTRVYRddlvtFQVDGTHGSAV 286
Cdd:PRK11579  214 AILSYPQrRVVLHGTMLAAAESAR-----YIVHGSRGSYV 248
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH