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Conserved domains on  [gi|518633115|ref|WP_019803322|]
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uroporphyrinogen decarboxylase [Streptococcus mutans]

Protein Classification

uroporphyrinogen decarboxylase family protein( domain architecture ID 10131019)

uroporphyrinogen decarboxylase (URO-D) family protein similar to URO-D that decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
URO-D_like cd03465
The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ...
10-333 9.95e-65

The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane.


:

Pssm-ID: 239548  Cd Length: 330  Bit Score: 207.57  E-value: 9.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  10 LKAFKGERVDKVPVGFWYHFLAEEEfgQGLDNPELFKKNLQGHQKFI---KEVDPDFIKLMSDGFFTYP----------- 75
Cdd:cd03465    1 AAALNGEKPDRVPVGPLLHGGAAEF--IGISLKEYYTDPELGAEAQIalyKKFGPDAIKVFSDLFVEAEafgaeiryped 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  76 --NELIHTNVTSIQELANISSIG-ENHPWFDQQMQLVKAIKESFTeDIVAIYNIF-SPVTYLKWQLsgqvahGDDIIARF 151
Cdd:cd03465   79 dtPSVEGPLIEDEEEDDDLLPPDpGDSPRLPELLEAIRLLKEELG-DRVPVIGAVgGPFTLASLLM------GASKFLML 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 152 LQEDAQTLKKVLNVIAGDIATLTRKIIaEAGLEGIYLSVQSIQDSNVTSEDYRNYITPSDLTIIEAAQQVQGLTVLHICG 231
Cdd:cd03465  152 LYTDPELVHKLLEKCTEFIIRYADALI-EAGADGIYISDPWASSSILSPEDFKEFSLPYLKKVFDAIKALGGPVIHHNCG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 232 yeGASNDIKLFKDYPAQVFNWAVGTegiSLAQGRKLFGGK-TVLGGFVNTkdGILYKGSKDDIQTEVKKLLQE----SGT 306
Cdd:cd03465  231 --DTAPILELMADLGADVFSIDVTV---DLAEAKKKVGDKaCLMGNLDPI--DVLLNGSPEEIKEEVKELLEKllkgGGG 303
                        330       340
                 ....*....|....*....|....*..
gi 518633115 307 LATVIGADCTIPSDIaaERIAWVKEAV 333
Cdd:cd03465  304 YILSSGCEIPPDTPI--ENIKAMIDAV 328
 
Name Accession Description Interval E-value
URO-D_like cd03465
The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ...
10-333 9.95e-65

The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane.


Pssm-ID: 239548  Cd Length: 330  Bit Score: 207.57  E-value: 9.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  10 LKAFKGERVDKVPVGFWYHFLAEEEfgQGLDNPELFKKNLQGHQKFI---KEVDPDFIKLMSDGFFTYP----------- 75
Cdd:cd03465    1 AAALNGEKPDRVPVGPLLHGGAAEF--IGISLKEYYTDPELGAEAQIalyKKFGPDAIKVFSDLFVEAEafgaeiryped 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  76 --NELIHTNVTSIQELANISSIG-ENHPWFDQQMQLVKAIKESFTeDIVAIYNIF-SPVTYLKWQLsgqvahGDDIIARF 151
Cdd:cd03465   79 dtPSVEGPLIEDEEEDDDLLPPDpGDSPRLPELLEAIRLLKEELG-DRVPVIGAVgGPFTLASLLM------GASKFLML 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 152 LQEDAQTLKKVLNVIAGDIATLTRKIIaEAGLEGIYLSVQSIQDSNVTSEDYRNYITPSDLTIIEAAQQVQGLTVLHICG 231
Cdd:cd03465  152 LYTDPELVHKLLEKCTEFIIRYADALI-EAGADGIYISDPWASSSILSPEDFKEFSLPYLKKVFDAIKALGGPVIHHNCG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 232 yeGASNDIKLFKDYPAQVFNWAVGTegiSLAQGRKLFGGK-TVLGGFVNTkdGILYKGSKDDIQTEVKKLLQE----SGT 306
Cdd:cd03465  231 --DTAPILELMADLGADVFSIDVTV---DLAEAKKKVGDKaCLMGNLDPI--DVLLNGSPEEIKEEVKELLEKllkgGGG 303
                        330       340
                 ....*....|....*....|....*..
gi 518633115 307 LATVIGADCTIPSDIaaERIAWVKEAV 333
Cdd:cd03465  304 YILSSGCEIPPDTPI--ENIKAMIDAV 328
HemE COG0407
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
4-333 7.12e-19

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 85.66  E-value: 7.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115   4 SKKEWVLKAFKGERVDKVPVGFWYHFLAEEEFGQGLD----NPELFKK-NLQGHQKFikevDPDFIKLMSD--------- 69
Cdd:COG0407    2 TPKERLLRALRGEPVDRVPVWPLTTAALMRQAGRYLPeycyDPELAAEvTLQPVRRF----GVDAAILFSDilveaealg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  70 -GFFTYPNE---LIHTNVTSIQELANISSIGENHPWFDQQMQLVKAIKESFTEDIVAIYNIFSPVTylkwqLSGQVAHGD 145
Cdd:COG0407   78 cKVDFGEGEgpvVEEHPIRDAEDVDALEVPDPEDGRLPYVLEAIRLLKEELGDEVPLIGFAGGPFT-----LASYLVEGF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 146 DIIARFLQEDAQTLKKVLNVIAGDIATLTRKIIaEAGLEGIylsvqSIQDSNVTS---EDYRNYITPSDLTIIEAAQQVQ 222
Cdd:COG0407  153 EKLKKLMYRDPELVHALLDKLTDAVIEYLKAQI-EAGADAV-----QIFDSWAGLlspKDFEEFVLPYLKRIVDALKERG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 223 GLTVLHICGyeGASNDIKLFKDYPAQVFN--WAVgtegiSLAQGRKLFGGKTVLGGFVNTkDGILYKGSKDDIQTEVKKL 300
Cdd:COG0407  227 VPVIIHFCG--DGTPLLEDMAETGADALSvdWRV-----DLAEAKERLGDKVALQGNLDP-ALLLLNGTPEEVEAEVKRI 298
                        330       340       350
                 ....*....|....*....|....*....|....
gi 518633115 301 LQESGTLAT-VIGADCTIPSDIAAERIAWVKEAV 333
Cdd:COG0407  299 LDAGGGGPGhIFNLGHGIPPDTPPENVKALVEAV 332
URO-D pfam01208
Uroporphyrinogen decarboxylase (URO-D);
5-333 3.27e-10

Uroporphyrinogen decarboxylase (URO-D);


Pssm-ID: 460112 [Multi-domain]  Cd Length: 341  Bit Score: 60.29  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115    5 KKEWVLKAFKGERVDKVPVGF-----WY--HFLAEEE---FGQGLDNPEL-FKKNLQGHQKFikevDPDFIKLMSD---- 69
Cdd:pfam01208   2 PNERFLRALRGEPVDRPPVWLmrqagRYlpEYRALRAgvsFLEYCKDPELaAEVTLQPYRRF----GLDAAIIFSDilve 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115   70 ------GFFTYPNE--LIHTNVTSIQELANISSIG-ENHPWFDQQMQLVKAIKESFTEDIVAIYNIFSPVT---YLkwql 137
Cdd:pfam01208  78 aeamgcEVEFPEGEgpVVENPVRSPEDVERLEVPDpELEGRLPYVLEAIRLLRKELGGEVPLIGFAGAPFTlasYL---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  138 sgqVAHGDDIIARFLQEDAQTLKKVLNVIAGDIATLTRKIIaEAGlegiylsVQSIQ--DSN---VTSEDYRNYITPSDL 212
Cdd:pfam01208 154 ---VEKGFEKFKKLMYKDPELVHRLLDKLTDACIEYLKAQI-EAG-------ADAIQifDSWaglLSPEDFREFVLPYLK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  213 TIIEAAQQV-QGLTVLHICGyegASNDI-KLFKDYPAQVFNWavgTEGISLAQGRKLFGGKTVLGGFVNTkdGILYkGSK 290
Cdd:pfam01208 223 RIVDAVKGRgPGPVILHICG---NGTPIlEDMADTGADVVSL---DWRVDLAEAARRVGDRVALQGNLDP--AVLL-GSP 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 518633115  291 DDIQTEVKKLLQES--GTLATVIGADCTIPSDIAAERIAWVKEAV 333
Cdd:pfam01208 294 EEIRKEVKEILEKGidGPKGYILNLGHGIPPGTPPENVKALVEAV 338
mtaA_cmuA TIGR01463
methyltransferase, MtaA/CmuA family; This subfamily is closely related to, yet is distinct ...
105-318 1.92e-06

methyltransferase, MtaA/CmuA family; This subfamily is closely related to, yet is distinct from, uroporphyrinogen decarboxylase (EC 4.1.1.37). It includes two isozymes from Methanosarcina barkeri of methylcobalamin--coenzyme M methyltransferase. It also includes a chloromethane utilization protein, CmuA, which transfers the methyl group of chloromethane to a corrinoid protein.


Pssm-ID: 273639  Cd Length: 336  Bit Score: 49.05  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  105 QMQLVKAIKESFTEDIVAIYNIFSPVTylkwqLSGQVAHGDDIIaRFLQEDAQTLKKVLNvIAGDIATLTRKIIAEAGLE 184
Cdd:TIGR01463 122 VLEAIKILREKYGPDVPIIGGMEGPFT-----VASDLIGVKSFM-KWSITDPDLAEAALD-IATDFVIAYAKAMVEAGAD 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  185 GIYLSVQSIQDSNVTSEDYRNYITPSDLTIieaAQQVQGLTVLHICGyegasNDIKLFKDYPAQVFNWAVGTEGISLAQG 264
Cdd:TIGR01463 195 VIAIADPVASPDLISPETYREFLLPYQKKF---AAEINSVTVLHICG-----NTNPILSDMADCGFEGFSVDEKPGMAHG 266
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 518633115  265 RKLFGGKTVLGGFVNTKDgILYKGSKDDIQTEVKK-LLQESGTLATVIGADCTIP 318
Cdd:TIGR01463 267 KRVIGGRASLVGNLSPPF-TLLNGTPEKIKAEAKEvLEGGIDILAPGCGIAPMTP 320
PRK06252 PRK06252
methylcobalamin:coenzyme M methyltransferase; Validated
109-301 8.84e-06

methylcobalamin:coenzyme M methyltransferase; Validated


Pssm-ID: 235753  Cd Length: 339  Bit Score: 46.80  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 109 VKAIKESFTEDIVAIYNIFSPVT----------YLKWQLSGQvahgdDIIARFLQedaqtlkkvlnvIAGDIATLTRKII 178
Cdd:PRK06252 127 IKILKEKVGEEVPIIAGLTGPISlasslmgpknFLKWLIKKP-----ELAHEFLD------------FVTDFCIEYAKAQ 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 179 AEAGLEGIylsvqSIQDSNVTSE-----DYRNYITPSDLTIIEAaqqVQGL-TVLHICGyegasnDIKLFKDYPAQvfnw 252
Cdd:PRK06252 190 LEAGADVI-----CIADPSASPEllgpkMFEEFVLPYLNKIIDE---VKGLpTILHICG------DLTSILEEMAD---- 251
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518633115 253 aVGTEGIS------LAQGRKLFGGKTVLGGFVNTKDgILYKGSKDDIQTEVKKLL 301
Cdd:PRK06252 252 -CGFDGISidekvdVKTAKENVGDRAALIGNVSTSF-TLLNGTPEKVKAEAKKCL 304
 
Name Accession Description Interval E-value
URO-D_like cd03465
The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ...
10-333 9.95e-65

The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane.


Pssm-ID: 239548  Cd Length: 330  Bit Score: 207.57  E-value: 9.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  10 LKAFKGERVDKVPVGFWYHFLAEEEfgQGLDNPELFKKNLQGHQKFI---KEVDPDFIKLMSDGFFTYP----------- 75
Cdd:cd03465    1 AAALNGEKPDRVPVGPLLHGGAAEF--IGISLKEYYTDPELGAEAQIalyKKFGPDAIKVFSDLFVEAEafgaeiryped 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  76 --NELIHTNVTSIQELANISSIG-ENHPWFDQQMQLVKAIKESFTeDIVAIYNIF-SPVTYLKWQLsgqvahGDDIIARF 151
Cdd:cd03465   79 dtPSVEGPLIEDEEEDDDLLPPDpGDSPRLPELLEAIRLLKEELG-DRVPVIGAVgGPFTLASLLM------GASKFLML 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 152 LQEDAQTLKKVLNVIAGDIATLTRKIIaEAGLEGIYLSVQSIQDSNVTSEDYRNYITPSDLTIIEAAQQVQGLTVLHICG 231
Cdd:cd03465  152 LYTDPELVHKLLEKCTEFIIRYADALI-EAGADGIYISDPWASSSILSPEDFKEFSLPYLKKVFDAIKALGGPVIHHNCG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 232 yeGASNDIKLFKDYPAQVFNWAVGTegiSLAQGRKLFGGK-TVLGGFVNTkdGILYKGSKDDIQTEVKKLLQE----SGT 306
Cdd:cd03465  231 --DTAPILELMADLGADVFSIDVTV---DLAEAKKKVGDKaCLMGNLDPI--DVLLNGSPEEIKEEVKELLEKllkgGGG 303
                        330       340
                 ....*....|....*....|....*..
gi 518633115 307 LATVIGADCTIPSDIaaERIAWVKEAV 333
Cdd:cd03465  304 YILSSGCEIPPDTPI--ENIKAMIDAV 328
HemE COG0407
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
4-333 7.12e-19

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 85.66  E-value: 7.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115   4 SKKEWVLKAFKGERVDKVPVGFWYHFLAEEEFGQGLD----NPELFKK-NLQGHQKFikevDPDFIKLMSD--------- 69
Cdd:COG0407    2 TPKERLLRALRGEPVDRVPVWPLTTAALMRQAGRYLPeycyDPELAAEvTLQPVRRF----GVDAAILFSDilveaealg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  70 -GFFTYPNE---LIHTNVTSIQELANISSIGENHPWFDQQMQLVKAIKESFTEDIVAIYNIFSPVTylkwqLSGQVAHGD 145
Cdd:COG0407   78 cKVDFGEGEgpvVEEHPIRDAEDVDALEVPDPEDGRLPYVLEAIRLLKEELGDEVPLIGFAGGPFT-----LASYLVEGF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 146 DIIARFLQEDAQTLKKVLNVIAGDIATLTRKIIaEAGLEGIylsvqSIQDSNVTS---EDYRNYITPSDLTIIEAAQQVQ 222
Cdd:COG0407  153 EKLKKLMYRDPELVHALLDKLTDAVIEYLKAQI-EAGADAV-----QIFDSWAGLlspKDFEEFVLPYLKRIVDALKERG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 223 GLTVLHICGyeGASNDIKLFKDYPAQVFN--WAVgtegiSLAQGRKLFGGKTVLGGFVNTkDGILYKGSKDDIQTEVKKL 300
Cdd:COG0407  227 VPVIIHFCG--DGTPLLEDMAETGADALSvdWRV-----DLAEAKERLGDKVALQGNLDP-ALLLLNGTPEEVEAEVKRI 298
                        330       340       350
                 ....*....|....*....|....*....|....
gi 518633115 301 LQESGTLAT-VIGADCTIPSDIAAERIAWVKEAV 333
Cdd:COG0407  299 LDAGGGGPGhIFNLGHGIPPDTPPENVKALVEAV 332
URO-D pfam01208
Uroporphyrinogen decarboxylase (URO-D);
5-333 3.27e-10

Uroporphyrinogen decarboxylase (URO-D);


Pssm-ID: 460112 [Multi-domain]  Cd Length: 341  Bit Score: 60.29  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115    5 KKEWVLKAFKGERVDKVPVGF-----WY--HFLAEEE---FGQGLDNPEL-FKKNLQGHQKFikevDPDFIKLMSD---- 69
Cdd:pfam01208   2 PNERFLRALRGEPVDRPPVWLmrqagRYlpEYRALRAgvsFLEYCKDPELaAEVTLQPYRRF----GLDAAIIFSDilve 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115   70 ------GFFTYPNE--LIHTNVTSIQELANISSIG-ENHPWFDQQMQLVKAIKESFTEDIVAIYNIFSPVT---YLkwql 137
Cdd:pfam01208  78 aeamgcEVEFPEGEgpVVENPVRSPEDVERLEVPDpELEGRLPYVLEAIRLLRKELGGEVPLIGFAGAPFTlasYL---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  138 sgqVAHGDDIIARFLQEDAQTLKKVLNVIAGDIATLTRKIIaEAGlegiylsVQSIQ--DSN---VTSEDYRNYITPSDL 212
Cdd:pfam01208 154 ---VEKGFEKFKKLMYKDPELVHRLLDKLTDACIEYLKAQI-EAG-------ADAIQifDSWaglLSPEDFREFVLPYLK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  213 TIIEAAQQV-QGLTVLHICGyegASNDI-KLFKDYPAQVFNWavgTEGISLAQGRKLFGGKTVLGGFVNTkdGILYkGSK 290
Cdd:pfam01208 223 RIVDAVKGRgPGPVILHICG---NGTPIlEDMADTGADVVSL---DWRVDLAEAARRVGDRVALQGNLDP--AVLL-GSP 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 518633115  291 DDIQTEVKKLLQES--GTLATVIGADCTIPSDIAAERIAWVKEAV 333
Cdd:pfam01208 294 EEIRKEVKEILEKGidGPKGYILNLGHGIPPGTPPENVKALVEAV 338
Mta_CmuA_like cd03307
MtaA_CmuA_like family. MtaA/CmuA, also MtsA, or methyltransferase 2 (MT2) MT2-A and MT2-M ...
109-330 2.74e-08

MtaA_CmuA_like family. MtaA/CmuA, also MtsA, or methyltransferase 2 (MT2) MT2-A and MT2-M isozymes, are methylcobamide:Coenzyme M methyltransferases, which play a role in metabolic pathways of methane formation from various substrates, such as methylated amines and methanol. Coenzyme M, 2-mercaptoethylsulfonate or CoM, is methylated during methanogenesis in a reaction catalyzed by three proteins. A methyltransferase methylates the corrinoid cofactor, which is bound to a second polypeptide, a corrinoid protein. The methylated corrinoid protein then serves as a substrate for MT2-A and related enzymes, which methylate CoM.


Pssm-ID: 239423  Cd Length: 326  Bit Score: 54.60  E-value: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 109 VKAIKESFTEDIVAIYNIFSPVTyLKWQLSGqvahgddiIARFLQE---DAQTLKKVLNvIAGDIATLTRKIIAEAGLEG 185
Cdd:cd03307  118 IKILKEKYGEEVPVIGGMTGPAS-LASHLAG--------VENFLKWlikKPEKVREFLE-FLTEACIEYAKAQLEAGADI 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 186 IYLSVQSIQDSNVTSEDYRNYITPSDLTIIEAAQQVqgLTVLHICGyegasnDIKLFKDYPAQvfnwaVGTEGIS----- 260
Cdd:cd03307  188 ITIADPTASPELISPEFYEEFALPYHKKIVKELHGC--PTILHICG------NTTPILEYIAQ-----CGFDGISvdekv 254
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518633115 261 -LAQGRKLFGGKTVLGGFVNTKDgILYKGSKDDIQTEVKKLLqESGtlATVIGADCTIPSDIAAERI-AWVK 330
Cdd:cd03307  255 dVKTAKEIVGGRAALIGNVSPSQ-TLLNGTPEDVKAEARKCL-EDG--VDILAPGCGIAPRTPLANLkAMVE 322
mtaA_cmuA TIGR01463
methyltransferase, MtaA/CmuA family; This subfamily is closely related to, yet is distinct ...
105-318 1.92e-06

methyltransferase, MtaA/CmuA family; This subfamily is closely related to, yet is distinct from, uroporphyrinogen decarboxylase (EC 4.1.1.37). It includes two isozymes from Methanosarcina barkeri of methylcobalamin--coenzyme M methyltransferase. It also includes a chloromethane utilization protein, CmuA, which transfers the methyl group of chloromethane to a corrinoid protein.


Pssm-ID: 273639  Cd Length: 336  Bit Score: 49.05  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  105 QMQLVKAIKESFTEDIVAIYNIFSPVTylkwqLSGQVAHGDDIIaRFLQEDAQTLKKVLNvIAGDIATLTRKIIAEAGLE 184
Cdd:TIGR01463 122 VLEAIKILREKYGPDVPIIGGMEGPFT-----VASDLIGVKSFM-KWSITDPDLAEAALD-IATDFVIAYAKAMVEAGAD 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115  185 GIYLSVQSIQDSNVTSEDYRNYITPSDLTIieaAQQVQGLTVLHICGyegasNDIKLFKDYPAQVFNWAVGTEGISLAQG 264
Cdd:TIGR01463 195 VIAIADPVASPDLISPETYREFLLPYQKKF---AAEINSVTVLHICG-----NTNPILSDMADCGFEGFSVDEKPGMAHG 266
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 518633115  265 RKLFGGKTVLGGFVNTKDgILYKGSKDDIQTEVKK-LLQESGTLATVIGADCTIP 318
Cdd:TIGR01463 267 KRVIGGRASLVGNLSPPF-TLLNGTPEKIKAEAKEvLEGGIDILAPGCGIAPMTP 320
PRK06252 PRK06252
methylcobalamin:coenzyme M methyltransferase; Validated
109-301 8.84e-06

methylcobalamin:coenzyme M methyltransferase; Validated


Pssm-ID: 235753  Cd Length: 339  Bit Score: 46.80  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 109 VKAIKESFTEDIVAIYNIFSPVT----------YLKWQLSGQvahgdDIIARFLQedaqtlkkvlnvIAGDIATLTRKII 178
Cdd:PRK06252 127 IKILKEKVGEEVPIIAGLTGPISlasslmgpknFLKWLIKKP-----ELAHEFLD------------FVTDFCIEYAKAQ 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518633115 179 AEAGLEGIylsvqSIQDSNVTSE-----DYRNYITPSDLTIIEAaqqVQGL-TVLHICGyegasnDIKLFKDYPAQvfnw 252
Cdd:PRK06252 190 LEAGADVI-----CIADPSASPEllgpkMFEEFVLPYLNKIIDE---VKGLpTILHICG------DLTSILEEMAD---- 251
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518633115 253 aVGTEGIS------LAQGRKLFGGKTVLGGFVNTKDgILYKGSKDDIQTEVKKLL 301
Cdd:PRK06252 252 -CGFDGISidekvdVKTAKENVGDRAALIGNVSTSF-TLLNGTPEKVKAEAKKCL 304
 
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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