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Conserved domains on  [gi|506240185|ref|WP_015759960|]
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MULTISPECIES: molybdopterin-dependent oxidoreductase [Eggerthella]

Protein Classification

molybdopterin-binding protein( domain architecture ID 1861)

molybdopterin-binding protein similar to sulfite oxidase and nitrite reductase that catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate

Gene Ontology:  GO:0043546
PubMed:  9242907

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MsrP super family cl30135
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
114-248 7.02e-24

Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];


The actual alignment was detected with superfamily member COG2041:

Pssm-ID: 441644 [Multi-domain]  Cd Length: 183  Bit Score: 96.76  E-value: 7.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 114 ANFYVNVGGHIKKNFTVDVSELSEDASEEALMACSCATGSPFGQAAVLGVPLASIVEMADLEEGVNTVTAYGAD-GFGQP 192
Cdd:COG2041   33 ADWRLRVDGLVEKPLTLTLDDLLALPLEERIYRLHCVENWSGGVAPWTGVPLRDLLERAGPKPGAKYVLFESADpGYTES 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506240185 193 LPLRYALEHDAMLVYQVNGQELTsATDGSSMQLWMPETVARYFTRNITDIELTRED 248
Cdd:COG2041  113 LPLDEALDPDTLLAYGMNGEPLP-PEHGAPLRLVVPGLYGFKSAKWLVRIEVTDED 167
SO_family_Moco super family cl00199
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
66-354 3.08e-21

Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


The actual alignment was detected with superfamily member cd02114:

Pssm-ID: 469652 [Multi-domain]  Cd Length: 367  Bit Score: 93.35  E-value: 3.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185  66 RVPNVQGSF-VFNQLGTTPNDELFNVFGAALTSMCSKPAVefeaqtggvanFYVNVGGHIKKNFTVDVSELSEDASEE-- 142
Cdd:cd02114   25 RPPHLETPFsVFNEGLITPNDAFFVRYHLAGIPLDIDPDA-----------YTLTIDGKVRTPLTLSLAELKRIEPRFev 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 143 -ALMACS---------------CATGSpFGQAAVLGVPLASIVEMADLEEGVNTVTAYGADG--------FGQPLPLRYA 198
Cdd:cd02114   94 vAVNQCSgnsrgffqprvqgaqLANGA-MGNARWAGVPLKAVLAKAGVQDGARQVAFRGLDQpvldvtpdFVKSLDIDHA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 199 LEHDAMLVYQVNGQELtSATDGSSMQLWMPETVARYFTRNITDIELTreDAEPDVQQVDPCYR----------------- 261
Cdd:cd02114  173 LDGEVMLAWEMNGEPL-PVLNGYPLRLVVPGFYATYWVKHLSHITVL--DKEFDGFWASQAYRipdnadagvepgtapdr 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 262 ----NKIN----IMNYADGCTFVAGDEITFEGVADDLGSPIEAIEFSFDGGATWTScATEGATADKWV--NWQFSTSFED 331
Cdd:cd02114  250 tapiNRFKvrsfITSLENGAIVAPAGELALRGIAFDGGSGIRRVDVSADGGDSWTQ-ATLGPDLGRFSfrGWKLTLDGVK 328
                        330       340
                 ....*....|....*....|...
gi 506240185 332 AGDYRMTVRAKTADGMVSPLAAT 354
Cdd:cd02114  329 KGPLTLMVRATNNDGQTQPLRAP 351
 
Name Accession Description Interval E-value
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
114-248 7.02e-24

Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];


Pssm-ID: 441644 [Multi-domain]  Cd Length: 183  Bit Score: 96.76  E-value: 7.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 114 ANFYVNVGGHIKKNFTVDVSELSEDASEEALMACSCATGSPFGQAAVLGVPLASIVEMADLEEGVNTVTAYGAD-GFGQP 192
Cdd:COG2041   33 ADWRLRVDGLVEKPLTLTLDDLLALPLEERIYRLHCVENWSGGVAPWTGVPLRDLLERAGPKPGAKYVLFESADpGYTES 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506240185 193 LPLRYALEHDAMLVYQVNGQELTsATDGSSMQLWMPETVARYFTRNITDIELTRED 248
Cdd:COG2041  113 LPLDEALDPDTLLAYGMNGEPLP-PEHGAPLRLVVPGLYGFKSAKWLVRIEVTDED 167
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
66-354 3.08e-21

sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SorB, a small c-type heme containing subunit, it forms a hetrodimer. It is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239032 [Multi-domain]  Cd Length: 367  Bit Score: 93.35  E-value: 3.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185  66 RVPNVQGSF-VFNQLGTTPNDELFNVFGAALTSMCSKPAVefeaqtggvanFYVNVGGHIKKNFTVDVSELSEDASEE-- 142
Cdd:cd02114   25 RPPHLETPFsVFNEGLITPNDAFFVRYHLAGIPLDIDPDA-----------YTLTIDGKVRTPLTLSLAELKRIEPRFev 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 143 -ALMACS---------------CATGSpFGQAAVLGVPLASIVEMADLEEGVNTVTAYGADG--------FGQPLPLRYA 198
Cdd:cd02114   94 vAVNQCSgnsrgffqprvqgaqLANGA-MGNARWAGVPLKAVLAKAGVQDGARQVAFRGLDQpvldvtpdFVKSLDIDHA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 199 LEHDAMLVYQVNGQELtSATDGSSMQLWMPETVARYFTRNITDIELTreDAEPDVQQVDPCYR----------------- 261
Cdd:cd02114  173 LDGEVMLAWEMNGEPL-PVLNGYPLRLVVPGFYATYWVKHLSHITVL--DKEFDGFWASQAYRipdnadagvepgtapdr 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 262 ----NKIN----IMNYADGCTFVAGDEITFEGVADDLGSPIEAIEFSFDGGATWTScATEGATADKWV--NWQFSTSFED 331
Cdd:cd02114  250 tapiNRFKvrsfITSLENGAIVAPAGELALRGIAFDGGSGIRRVDVSADGGDSWTQ-ATLGPDLGRFSfrGWKLTLDGVK 328
                        330       340
                 ....*....|....*....|...
gi 506240185 332 AGDYRMTVRAKTADGMVSPLAAT 354
Cdd:cd02114  329 KGPLTLMVRATNNDGQTQPLRAP 351
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
118-355 8.58e-21

Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).


Pssm-ID: 239028 [Multi-domain]  Cd Length: 317  Bit Score: 91.59  E-value: 8.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 118 VNVGGHIKKNFTVDVSELSEDASEEALMACSCA-----------TGSPFGQAAV-----LGVPLASIVEMADLEEGVNTV 181
Cdd:cd02110   20 LEIHGLVERPLTLTLDDLKRLPSVEVVATLECSgngrggfipvrSGAQWGHGAVgnarwTGVPLKDLLEEAGVKPGAKHV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 182 TAYGAD--------GFGQPLPLRYALEHDAMLVYQVNGQELTSAtDGSSMQLWMPetvARYFTRNI---TDIELTREDAE 250
Cdd:cd02110  100 LFEGADvppgekaaDYTRSVPLSKALDDDALLAYEMNGEPLPPD-HGYPLRLVVP---GWYGARSVkwlRRIEVTDQPSD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 251 ------------PDVQQVDPCYRNKINIMNY-------ADGCTFVAGDEITFEGVADDLGSPIEAIEFSFDGGATWTSCA 311
Cdd:cd02110  176 gywqtrdytvppPDVDAVGGKARRPIGEMPVksvitspSPGAELVSGGRVEIGGVAWSGGRGIRRVEVSLDGGRTWQEAR 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 506240185 312 TEGATADK--WVNWQFSTSFEdAGDYRMTVRAKTADGMVSPLAATL 355
Cdd:cd02110  256 LEGPLAGPraWRQWELDWDLP-PGEYELVARATDSTGNVQPERAEW 300
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
118-215 4.00e-11

Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.


Pssm-ID: 459699 [Multi-domain]  Cd Length: 168  Bit Score: 60.98  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185  118 VNVGGHIKKNFTVDVSELSEDASEEALMACSCAT----------GSPFGQAAVL-----GVPLASIVEMADLEEGVNTVT 182
Cdd:pfam00174  14 LRVDGLVEKPLTLTLDDLKAFPQVTVTATLQCVGnrrkemnrvkGVQWGGGAIGnaewtGVPLRDLLERAGVKPGAKHVL 93
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 506240185  183 AYGAD-----GFGQPLPLRYALEHDAMLVYQVNGQELT 215
Cdd:pfam00174  94 FEGADtlgdgGYTTSLPLEKALDDDVLLAYEMNGEPLP 131
 
Name Accession Description Interval E-value
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
114-248 7.02e-24

Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];


Pssm-ID: 441644 [Multi-domain]  Cd Length: 183  Bit Score: 96.76  E-value: 7.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 114 ANFYVNVGGHIKKNFTVDVSELSEDASEEALMACSCATGSPFGQAAVLGVPLASIVEMADLEEGVNTVTAYGAD-GFGQP 192
Cdd:COG2041   33 ADWRLRVDGLVEKPLTLTLDDLLALPLEERIYRLHCVENWSGGVAPWTGVPLRDLLERAGPKPGAKYVLFESADpGYTES 112
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506240185 193 LPLRYALEHDAMLVYQVNGQELTsATDGSSMQLWMPETVARYFTRNITDIELTRED 248
Cdd:COG2041  113 LPLDEALDPDTLLAYGMNGEPLP-PEHGAPLRLVVPGLYGFKSAKWLVRIEVTDED 167
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
66-354 3.08e-21

sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SorB, a small c-type heme containing subunit, it forms a hetrodimer. It is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239032 [Multi-domain]  Cd Length: 367  Bit Score: 93.35  E-value: 3.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185  66 RVPNVQGSF-VFNQLGTTPNDELFNVFGAALTSMCSKPAVefeaqtggvanFYVNVGGHIKKNFTVDVSELSEDASEE-- 142
Cdd:cd02114   25 RPPHLETPFsVFNEGLITPNDAFFVRYHLAGIPLDIDPDA-----------YTLTIDGKVRTPLTLSLAELKRIEPRFev 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 143 -ALMACS---------------CATGSpFGQAAVLGVPLASIVEMADLEEGVNTVTAYGADG--------FGQPLPLRYA 198
Cdd:cd02114   94 vAVNQCSgnsrgffqprvqgaqLANGA-MGNARWAGVPLKAVLAKAGVQDGARQVAFRGLDQpvldvtpdFVKSLDIDHA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 199 LEHDAMLVYQVNGQELtSATDGSSMQLWMPETVARYFTRNITDIELTreDAEPDVQQVDPCYR----------------- 261
Cdd:cd02114  173 LDGEVMLAWEMNGEPL-PVLNGYPLRLVVPGFYATYWVKHLSHITVL--DKEFDGFWASQAYRipdnadagvepgtapdr 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 262 ----NKIN----IMNYADGCTFVAGDEITFEGVADDLGSPIEAIEFSFDGGATWTScATEGATADKWV--NWQFSTSFED 331
Cdd:cd02114  250 tapiNRFKvrsfITSLENGAIVAPAGELALRGIAFDGGSGIRRVDVSADGGDSWTQ-ATLGPDLGRFSfrGWKLTLDGVK 328
                        330       340
                 ....*....|....*....|...
gi 506240185 332 AGDYRMTVRAKTADGMVSPLAAT 354
Cdd:cd02114  329 KGPLTLMVRATNNDGQTQPLRAP 351
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
118-355 8.58e-21

Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).


Pssm-ID: 239028 [Multi-domain]  Cd Length: 317  Bit Score: 91.59  E-value: 8.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 118 VNVGGHIKKNFTVDVSELSEDASEEALMACSCA-----------TGSPFGQAAV-----LGVPLASIVEMADLEEGVNTV 181
Cdd:cd02110   20 LEIHGLVERPLTLTLDDLKRLPSVEVVATLECSgngrggfipvrSGAQWGHGAVgnarwTGVPLKDLLEEAGVKPGAKHV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 182 TAYGAD--------GFGQPLPLRYALEHDAMLVYQVNGQELTSAtDGSSMQLWMPetvARYFTRNI---TDIELTREDAE 250
Cdd:cd02110  100 LFEGADvppgekaaDYTRSVPLSKALDDDALLAYEMNGEPLPPD-HGYPLRLVVP---GWYGARSVkwlRRIEVTDQPSD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 251 ------------PDVQQVDPCYRNKINIMNY-------ADGCTFVAGDEITFEGVADDLGSPIEAIEFSFDGGATWTSCA 311
Cdd:cd02110  176 gywqtrdytvppPDVDAVGGKARRPIGEMPVksvitspSPGAELVSGGRVEIGGVAWSGGRGIRRVEVSLDGGRTWQEAR 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 506240185 312 TEGATADK--WVNWQFSTSFEdAGDYRMTVRAKTADGMVSPLAATL 355
Cdd:cd02110  256 LEGPLAGPraWRQWELDWDLP-PGEYELVARATDSTGNVQPERAEW 300
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
120-247 4.43e-13

Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 238198 [Multi-domain]  Cd Length: 156  Bit Score: 66.05  E-value: 4.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 120 VGGHIKKNFTVDVSELSEDASEEALMACSCAtGSPFGQAAVL-----GVPLASIVEMADLEEGVNTVTAYGAD-----GF 189
Cdd:cd00321   21 VDGLVEKPLSLTLDDLKALPQVEVIATLHCV-GNRWGGGAVSnaewtGVPLRDLLEEAGPKPGARYVVFEGADdpggdGY 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506240185 190 GQPLPLRYALEHDAMLVYQVNGQELTSAtDGSSMQLWMPetvARYFTRN---ITDIELTRE 247
Cdd:cd00321  100 TTSLPLEKALDPDVLLAYEMNGEPLPPD-HGFPLRLVVP---GLYGWKSvkwLRRIEVTDE 156
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
118-215 4.00e-11

Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.


Pssm-ID: 459699 [Multi-domain]  Cd Length: 168  Bit Score: 60.98  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185  118 VNVGGHIKKNFTVDVSELSEDASEEALMACSCAT----------GSPFGQAAVL-----GVPLASIVEMADLEEGVNTVT 182
Cdd:pfam00174  14 LRVDGLVEKPLTLTLDDLKAFPQVTVTATLQCVGnrrkemnrvkGVQWGGGAIGnaewtGVPLRDLLERAGVKPGAKHVL 93
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 506240185  183 AYGAD-----GFGQPLPLRYALEHDAMLVYQVNGQELT 215
Cdd:pfam00174  94 FEGADtlgdgGYTTSLPLEKALDDDVLLAYEMNGEPLP 131
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
162-249 1.37e-07

bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown.


Pssm-ID: 239027 [Multi-domain]  Cd Length: 180  Bit Score: 51.09  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 162 GVPLASIVEMADLEEGVNTVTAYGADGFGQPLPLRYALEHDAMLVYQVNGQELTsATDGSSMQLWMPetvARYFTRN--- 238
Cdd:cd02109   73 GVSLKDLLEAARPDPEATFVMAHSYDGYTTNLPLEDLLREDSLLATKMDGEPLP-PEHGGPARLVVP---HLYFWKSakw 148
                         90
                 ....*....|.
gi 506240185 239 ITDIELTREDA 249
Cdd:cd02109  149 LRGIEFLDEDE 159
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
162-356 1.52e-06

bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. SoxC is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SoxD, a small c-type heme containing subunit, it forms a hetrotetrameric sulfite dehydrogenase. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239031 [Multi-domain]  Cd Length: 326  Bit Score: 49.32  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 162 GVPLASIVEMADLEEGVNTVTAYGADGFG--QPLPLRYALEhDAMLVYQVNGQELtSATDGSSMQLWMP----ETVARYF 235
Cdd:cd02113   94 GVPLSTLLEEAGVKPGAKWLLAEGADAAAmtRSIPLEKALD-DALVAYAQNGEAL-RPENGYPLRLVVPgwegNTNVKWL 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506240185 236 TR-NITDIEL-TRE------DAEPD--VQQVDPCYRNKINIMNYADGCTFVAGDEITFEGVADDLGSPIEAIEFSFDGGA 305
Cdd:cd02113  172 RRiEVGDQPWmTREetskytDLLPDgrARQFSFVMEAKSVITSPSGGQRLREPGFHEISGLAWSGRGRIRRVDVSFDGGR 251
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506240185 306 TWTSCATEGATADK-----WVNWQFstsfeDAGDYRMTVRAKTADGMVSPLAATLL 356
Cdd:cd02113  252 TWQDARLEGPVLPKaltrfRLPWKW-----DGRPAVLQSRATDETGYVQPTRAELR 302
 
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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