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Conserved domains on  [gi|1184610966|ref|WP_085172969|]
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precorrin-2 C(20)-methyltransferase [Mycobacterium paraense]

Protein Classification

Precorrin_2_C20_MT and Precorrin_3B_C17_MT domain-containing protein( domain architecture ID 10898430)

Precorrin_2_C20_MT and Precorrin_3B_C17_MT domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
250-493 7.59e-108

Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


:

Pssm-ID: 440634  Cd Length: 250  Bit Score: 320.86  E-value: 7.59e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSG 328
Cdd:COG1010     4 GKLYVVGLGPGSAELMTPRARAALAEADVVVGYGTYLDLIpPLLPGKEVHASGMREEVERAREALELAAEGKTVAVVSSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 329 DPGVFAMATAVLEEAKQ---WPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLA 405
Cdd:COG1010    84 DPGVYGMAGLVLEVLEEggaWRDVEVEVVPGITAAQAAAARLGAPLGHDFCVISLSDLLTPWEVIEKRLRAAAEADFVIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 406 IYNPASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYsddfGDRV 485
Cdd:COG1010   164 LYNPRSRKRPWQLERALEILLEHRPPDTPVGIVRNAGRPDESVTVTTLGELDPEEVDMLTTVIIGNSQTRVI----GGWM 239

                  ....*...
gi 1184610966 486 FTPRRYPG 493
Cdd:COG1010   240 ITPRGYPR 247
TP_methylase super family cl00304
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
3-233 6.74e-101

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


The actual alignment was detected with superfamily member PRK05990:

Pssm-ID: 444820  Cd Length: 241  Bit Score: 302.68  E-value: 6.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   3 ARGTLWGVGLGPGDPELVTVKAARLIGEADVVAYHSARHGRSIARGIAEPYLRPGQIEEHLVYPVTTEATDHPGGYAGAL 82
Cdd:PRK05990    1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYFVAKGKKGNAFGIVEAHLSPGQTLLPLVYPVTTEILPPPLCYETVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  83 EDFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTERFNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLPG 162
Cdd:PRK05990   81 ADFYDTSAEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPRYETEVIPGVCSMLGCWSVLGAPLVYRNQSLSVLSG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184610966 163 TLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILPAGEVDETGVPYFSL 233
Cdd:PRK05990  161 VLPEEELRRRLADADAAVIMKLGRNLDKVRRVLAALGLLDRALYVERATMANQRIVPLAEVDPMASPYFSL 231
 
Name Accession Description Interval E-value
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
250-493 7.59e-108

Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440634  Cd Length: 250  Bit Score: 320.86  E-value: 7.59e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSG 328
Cdd:COG1010     4 GKLYVVGLGPGSAELMTPRARAALAEADVVVGYGTYLDLIpPLLPGKEVHASGMREEVERAREALELAAEGKTVAVVSSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 329 DPGVFAMATAVLEEAKQ---WPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLA 405
Cdd:COG1010    84 DPGVYGMAGLVLEVLEEggaWRDVEVEVVPGITAAQAAAARLGAPLGHDFCVISLSDLLTPWEVIEKRLRAAAEADFVIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 406 IYNPASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYsddfGDRV 485
Cdd:COG1010   164 LYNPRSRKRPWQLERALEILLEHRPPDTPVGIVRNAGRPDESVTVTTLGELDPEEVDMLTTVIIGNSQTRVI----GGWM 239

                  ....*...
gi 1184610966 486 FTPRRYPG 493
Cdd:COG1010   240 ITPRGYPR 247
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
3-233 6.74e-101

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 302.68  E-value: 6.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   3 ARGTLWGVGLGPGDPELVTVKAARLIGEADVVAYHSARHGRSIARGIAEPYLRPGQIEEHLVYPVTTEATDHPGGYAGAL 82
Cdd:PRK05990    1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYFVAKGKKGNAFGIVEAHLSPGQTLLPLVYPVTTEILPPPLCYETVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  83 EDFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTERFNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLPG 162
Cdd:PRK05990   81 ADFYDTSAEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPRYETEVIPGVCSMLGCWSVLGAPLVYRNQSLSVLSG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184610966 163 TLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILPAGEVDETGVPYFSL 233
Cdd:PRK05990  161 VLPEEELRRRLADADAAVIMKLGRNLDKVRRVLAALGLLDRALYVERATMANQRIVPLAEVDPMASPYFSL 231
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
252-491 1.36e-91

Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone.


Pssm-ID: 381173 [Multi-domain]  Cd Length: 238  Bit Score: 278.53  E-value: 1.36e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 252 VAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGDP 330
Cdd:cd11646     1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIeDLLPGKEVISSGMGEEVERAREALELALEGKRVALVSSGDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 331 GVFAMATAVLEEAKQ-WPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLAIYNP 409
Cdd:cd11646    81 GIYGMAGLVLELLDErWDDIEVEVVPGITAALAAAALLGAPLGHDFAVISLSDLLTPWEVIEKRLRAAAEADFVIALYNP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 410 ASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYsddfGDRVFTPR 489
Cdd:cd11646   161 RSKKRPWQLEKALEILLEHRPPDTPVGIVRNAGREGEEVTITTLGELDPEDVDMFTTVIIGNSQTYII----GGKMITPR 236

                  ..
gi 1184610966 490 RY 491
Cdd:cd11646   237 GY 238
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
5-236 4.80e-86

Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 263.88  E-value: 4.80e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   5 GTLWGVGLGPGDPELVTVKAARLIGEADVVAYH-SARHGRSIARGIAEPYLRPgQIEEHLVYPVTTEAtdhpggyaGALE 83
Cdd:COG2243     3 GKLYGVGVGPGDPELLTLKAVRALREADVIAYPaKGAGKASLAREIVAPYLPP-ARIVELVFPMTTDY--------EALV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  84 DFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLPG 162
Cdd:COG2243    74 AAWDEAAARIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRERgFEVEVIPGITSFSAAAAALGIPLAEGDEPLTVLPG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184610966 163 TLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILP-AGEVDETGVPYFSLAML 236
Cdd:COG2243   154 TLLEEELERALDDFDTVVIMKVGRNFPKVREALEEAGLLDRAWYVERAGMPDERIVPgLAEVDIEEAPYFSLILV 228
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
252-492 6.21e-78

precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273641 [Multi-domain]  Cd Length: 239  Bit Score: 243.75  E-value: 6.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 252 VAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGDP 330
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIeDLIPGKEVVTSGMREEIARAELAIELAAEGRTVALVSSGDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 331 GVFAMATAVLE--EAKQWPgVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLAIYN 408
Cdd:TIGR01466  81 GIYGMAALVFEalEKKGAE-VDIEVIPGITAASAAASLLGAPLGHDFCVISLSDLLTPWPEIEKRLRAAAEADFVIAIYN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 409 PASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYSddfgDRVFTP 488
Cdd:TIGR01466 160 PRSKRRPEQFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAELDEELIDMLTTVIIGNSETYVID----GWMITP 235

                  ....
gi 1184610966 489 RRYP 492
Cdd:TIGR01466 236 RGYA 239
PRK05991 PRK05991
precorrin-3B C17-methyltransferase; Provisional
250-492 1.90e-67

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 180342 [Multi-domain]  Cd Length: 250  Bit Score: 216.92  E-value: 1.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRVPVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGD 329
Cdd:PRK05991    3 GRLFVIGTGPGNPEQMTPEALAAVEAATDFFGYGPYLDRLPLRADQLRHASDNREELDRAGAALAMAAAGANVCVVSGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 330 PGVFAMATAVLEEAK----QWPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLA 405
Cdd:PRK05991   83 PGVFAMAAAVCEAIEngpaAWRAVDLTIVPGVTAMLAVAARIGAPLGHDFCAISLSDNLKPWELIEKRLRLAAEAGFVIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 406 IYNPASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYS-DDFGDR 484
Cdd:PRK05991  163 LYNPISRARPWQLGEAFDLLREHLPATVPVIFGRAAGRPDERIAVAPLAEADASMADMATCVIIGSAETRIVArPGKPDL 242

                  ....*...
gi 1184610966 485 VFTPRRYP 492
Cdd:PRK05991  243 VYTPRSAA 250
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
10-236 9.22e-66

Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.


Pssm-ID: 381172 [Multi-domain]  Cd Length: 223  Bit Score: 211.60  E-value: 9.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAYHSARHGR-SIARGIAEPYLRPGQIEEHLVYPVTTEAtdhpggyaGALEDFYAE 88
Cdd:cd11645     1 VGVGPGDPELLTLKAVRILKEADVIFVPVSKGGEgSAALIIAAALLIPDKEIIPLEFPMTKDR--------EELEEAWDE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  89 ATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLPGTLPVA 167
Cdd:cd11645    73 AAEEIAEELKEGKDVAFLTLGDPSLYSTFSYLLERLRAPgVEVEIIPGITSFSAAAARLGIPLAEGDESLAILPATYDEE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 168 ELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILP-AGEVDETGVPYFSLAML 236
Cdd:cd11645   153 ELEKALENFDTVVLMKVGRNLEEIKELLEELGLLDKAVYVERCGMEGERIYTdLEELKEEKLPYFSLIIV 222
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
5-236 2.01e-62

precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273642 [Multi-domain]  Cd Length: 230  Bit Score: 203.31  E-value: 2.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   5 GTLWGVGLGPGDPELVTVKAARLIGEADVVAY-HSARHGRSIARGIAEPYLRPGQIEEH-LVYPVTTEAtdhpggyaGAL 82
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIAVpASKKGRESLARKIVEDYLKPNDTRILeLVFPMTKDR--------DEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  83 EDFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLP 161
Cdd:TIGR01467  73 EKAWDEAAEAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMgIEVEVVPGITSFAACASAAGLPLVEGDESLAILP 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184610966 162 GTLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILPAGEVDETG-VPYFSLAML 236
Cdd:TIGR01467 153 ATAGEAELEKALAEFDTVVLMKVGRNLPQIKEALAKLGRLDAAVVVERATMPDEKIVDLVREAIDDaLPYFSTILV 228
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
6-220 2.10e-30

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 117.44  E-value: 2.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   6 TLWGVGLGPGDPELVTVKAARLIGEADVVAYhsarhGRSIARGIAEPYLRPGQIeehlvypvtteatDHPGGYAGALEDF 85
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLG-----DDSRALEILLDLLPEDLY-------------FPMTEDKEPLEEA 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  86 YAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVL---- 160
Cdd:pfam00590  63 YEEIAEALAAALRAGKDVARLVSGDPLVYGTGSYLVEALRAAgIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLflpg 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184610966 161 PGTLPVAELTRRLADADAAVVLKLGRSYPAVREALSAT-GQLDDAFYVERASTSGQRILPA 220
Cdd:pfam00590 143 LARIELRLLEALLANGDTVVLLYGPRRLAELAELLLELyPDTTPVAVVERAGTPDEKVVRG 203
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
251-457 8.34e-22

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 93.18  E-value: 8.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 251 TVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRT-YLDRVPVREGQRRHPSDNTDEPARARL-------ACALAEEGCAV 322
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSrALEILLDLLPEDLYFPMTEDKEPLEEAyeeiaeaLAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 323 AVVSSGDPGVFAMATAVLEEAKQwPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDrLKPWEVISARLAAAAAADL 402
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRA-AGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLF-LPGLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184610966 403 VLAI--YNPaskartWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLD 457
Cdd:pfam00590 159 DTVVllYGP------RRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
 
Name Accession Description Interval E-value
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
250-493 7.59e-108

Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440634  Cd Length: 250  Bit Score: 320.86  E-value: 7.59e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSG 328
Cdd:COG1010     4 GKLYVVGLGPGSAELMTPRARAALAEADVVVGYGTYLDLIpPLLPGKEVHASGMREEVERAREALELAAEGKTVAVVSSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 329 DPGVFAMATAVLEEAKQ---WPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLA 405
Cdd:COG1010    84 DPGVYGMAGLVLEVLEEggaWRDVEVEVVPGITAAQAAAARLGAPLGHDFCVISLSDLLTPWEVIEKRLRAAAEADFVIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 406 IYNPASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYsddfGDRV 485
Cdd:COG1010   164 LYNPRSRKRPWQLERALEILLEHRPPDTPVGIVRNAGRPDESVTVTTLGELDPEEVDMLTTVIIGNSQTRVI----GGWM 239

                  ....*...
gi 1184610966 486 FTPRRYPG 493
Cdd:COG1010   240 ITPRGYPR 247
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
3-233 6.74e-101

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 302.68  E-value: 6.74e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   3 ARGTLWGVGLGPGDPELVTVKAARLIGEADVVAYHSARHGRSIARGIAEPYLRPGQIEEHLVYPVTTEATDHPGGYAGAL 82
Cdd:PRK05990    1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYFVAKGKKGNAFGIVEAHLSPGQTLLPLVYPVTTEILPPPLCYETVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  83 EDFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTERFNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLPG 162
Cdd:PRK05990   81 ADFYDTSAEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPRYETEVIPGVCSMLGCWSVLGAPLVYRNQSLSVLSG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184610966 163 TLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILPAGEVDETGVPYFSL 233
Cdd:PRK05990  161 VLPEEELRRRLADADAAVIMKLGRNLDKVRRVLAALGLLDRALYVERATMANQRIVPLAEVDPMASPYFSL 231
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
252-491 1.36e-91

Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone.


Pssm-ID: 381173 [Multi-domain]  Cd Length: 238  Bit Score: 278.53  E-value: 1.36e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 252 VAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGDP 330
Cdd:cd11646     1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIeDLLPGKEVISSGMGEEVERAREALELALEGKRVALVSSGDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 331 GVFAMATAVLEEAKQ-WPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLAIYNP 409
Cdd:cd11646    81 GIYGMAGLVLELLDErWDDIEVEVVPGITAALAAAALLGAPLGHDFAVISLSDLLTPWEVIEKRLRAAAEADFVIALYNP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 410 ASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYsddfGDRVFTPR 489
Cdd:cd11646   161 RSKKRPWQLEKALEILLEHRPPDTPVGIVRNAGREGEEVTITTLGELDPEDVDMFTTVIIGNSQTYII----GGKMITPR 236

                  ..
gi 1184610966 490 RY 491
Cdd:cd11646   237 GY 238
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
5-236 4.80e-86

Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 263.88  E-value: 4.80e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   5 GTLWGVGLGPGDPELVTVKAARLIGEADVVAYH-SARHGRSIARGIAEPYLRPgQIEEHLVYPVTTEAtdhpggyaGALE 83
Cdd:COG2243     3 GKLYGVGVGPGDPELLTLKAVRALREADVIAYPaKGAGKASLAREIVAPYLPP-ARIVELVFPMTTDY--------EALV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  84 DFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLPG 162
Cdd:COG2243    74 AAWDEAAARIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRERgFEVEVIPGITSFSAAAAALGIPLAEGDEPLTVLPG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184610966 163 TLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILP-AGEVDETGVPYFSLAML 236
Cdd:COG2243   154 TLLEEELERALDDFDTVVIMKVGRNFPKVREALEEAGLLDRAWYVERAGMPDERIVPgLAEVDIEEAPYFSLILV 228
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
252-492 6.21e-78

precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273641 [Multi-domain]  Cd Length: 239  Bit Score: 243.75  E-value: 6.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 252 VAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGDP 330
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIeDLIPGKEVVTSGMREEIARAELAIELAAEGRTVALVSSGDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 331 GVFAMATAVLE--EAKQWPgVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLAIYN 408
Cdd:TIGR01466  81 GIYGMAALVFEalEKKGAE-VDIEVIPGITAASAAASLLGAPLGHDFCVISLSDLLTPWPEIEKRLRAAAEADFVIAIYN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 409 PASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYSddfgDRVFTP 488
Cdd:TIGR01466 160 PRSKRRPEQFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAELDEELIDMLTTVIIGNSETYVID----GWMITP 235

                  ....
gi 1184610966 489 RRYP 492
Cdd:TIGR01466 236 RGYA 239
PRK05991 PRK05991
precorrin-3B C17-methyltransferase; Provisional
250-492 1.90e-67

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 180342 [Multi-domain]  Cd Length: 250  Bit Score: 216.92  E-value: 1.90e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRVPVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGD 329
Cdd:PRK05991    3 GRLFVIGTGPGNPEQMTPEALAAVEAATDFFGYGPYLDRLPLRADQLRHASDNREELDRAGAALAMAAAGANVCVVSGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 330 PGVFAMATAVLEEAK----QWPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLA 405
Cdd:PRK05991   83 PGVFAMAAAVCEAIEngpaAWRAVDLTIVPGVTAMLAVAARIGAPLGHDFCAISLSDNLKPWELIEKRLRLAAEAGFVIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 406 IYNPASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTQWYS-DDFGDR 484
Cdd:PRK05991  163 LYNPISRARPWQLGEAFDLLREHLPATVPVIFGRAAGRPDERIAVAPLAEADASMADMATCVIIGSAETRIVArPGKPDL 242

                  ....*...
gi 1184610966 485 VFTPRRYP 492
Cdd:PRK05991  243 VYTPRSAA 250
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
10-236 9.22e-66

Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.


Pssm-ID: 381172 [Multi-domain]  Cd Length: 223  Bit Score: 211.60  E-value: 9.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAYHSARHGR-SIARGIAEPYLRPGQIEEHLVYPVTTEAtdhpggyaGALEDFYAE 88
Cdd:cd11645     1 VGVGPGDPELLTLKAVRILKEADVIFVPVSKGGEgSAALIIAAALLIPDKEIIPLEFPMTKDR--------EELEEAWDE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  89 ATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLPGTLPVA 167
Cdd:cd11645    73 AAEEIAEELKEGKDVAFLTLGDPSLYSTFSYLLERLRAPgVEVEIIPGITSFSAAAARLGIPLAEGDESLAILPATYDEE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 168 ELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILP-AGEVDETGVPYFSLAML 236
Cdd:cd11645   153 ELEKALENFDTVVLMKVGRNLEEIKELLEELGLLDKAVYVERCGMEGERIYTdLEELKEEKLPYFSLIIV 222
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
5-236 2.01e-62

precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273642 [Multi-domain]  Cd Length: 230  Bit Score: 203.31  E-value: 2.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   5 GTLWGVGLGPGDPELVTVKAARLIGEADVVAY-HSARHGRSIARGIAEPYLRPGQIEEH-LVYPVTTEAtdhpggyaGAL 82
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIAVpASKKGRESLARKIVEDYLKPNDTRILeLVFPMTKDR--------DEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  83 EDFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVLP 161
Cdd:TIGR01467  73 EKAWDEAAEAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMgIEVEVVPGITSFAACASAAGLPLVEGDESLAILP 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184610966 162 GTLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILPAGEVDETG-VPYFSLAML 236
Cdd:TIGR01467 153 ATAGEAELEKALAEFDTVVLMKVGRNLPQIKEALAKLGRLDAAVVVERATMPDEKIVDLVREAIDDaLPYFSTILV 228
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
5-236 3.02e-44

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 155.57  E-value: 3.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   5 GTLWGVGLGPGDPELVTVKAARLIGEADVVAYHSARHGRS-IARGIAEPYLRPGQIEEHLVYPVTTEATdhpggyagALE 83
Cdd:PRK05948    4 GTLYGISVGPGDPELITLKGLRLLQSAPVVAFPAGLAGQPgLAEQIIAPWLSPQQIKLPLYFPYVQDEE--------QLE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  84 DFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTERFNAV---IVPGVTSVSAASAAIATPLVAGDEVLSVL 160
Cdd:PRK05948   76 QAWQAAADQVWHYLEQGEDVAFACEGDVSFYSTFTYLAQTLQELYPQVaiqTIPGVCSPLAAAAALGIPLTLGSQRLAIL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184610966 161 PGTLPVAELTRRLADADAAVVLKLGRSYPAVREALSATGQLDDAFYVERASTSGQRILPA-GEVDETGVPYFSLAML 236
Cdd:PRK05948  156 PALYHLEELEQALTWADVVVLMKVSSVYPQVWQWLKARNLLEQASLVERATTPEQVIYRNlEDYPDLRLPYFSLLII 232
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
5-234 4.95e-39

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 141.59  E-value: 4.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   5 GTLWGVGLGPGDPELVTVKAARLIGEADVV-AYHSARHGRSIARGIAEPYLRPGQIEEHLVYPVTTEATdhpggyagALE 83
Cdd:PRK05576    2 GKLYGIGLGPGDPELLTVKAARILEEADVVyAPASRKGGGSLALNIVRPYLKEETEIVELHFPMSKDEE--------EKE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  84 DFYAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTERFNAV-IVPGVTSVSAASAAIATPLVAGDEVLSVLPG 162
Cdd:PRK05576   74 AVWKENAEEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVeTVPGISSFTAIASRAGVPLAMGDESLAIIPA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184610966 163 TLPvAELTRRLADADAAVVLKLGRSYPAVREALSATGqlDDAFYVERASTSGQRILPAGEVDETGVPYFSLA 234
Cdd:PRK05576  154 TRE-ALIEQALTDFDSVVLMKVYKNFALIEELLEEGY--LDALYVRRAYMEGEQILRRLEEILDDLDYFSTI 222
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
249-491 3.24e-35

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 131.83  E-value: 3.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 249 AGTVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRVP-VREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSS 327
Cdd:PRK05765    1 MGKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISdLLDGKEVIGARMKEEIFRANTAIEKALEGNIVALVSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 328 GDPGVFAMATAVLE--EAKQWPgVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLA 405
Cdd:PRK05765   81 GDPQVYGMAGLVFEliSRRKLD-VDVEVIPGVTAALAAAARLGSPLSLDFVVISLSDLLIPREEILHRVTKAAEADFVIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 406 IYNPASKARTWQVgamRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADL--DPAEVDMRCLLIVGSSQTQWYsddfGD 483
Cdd:PRK05765  160 FYNPINENLLIEV---MDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWkeHMDEIGMTTTMIIGNSLTYSW----KN 232

                  ....*...
gi 1184610966 484 RVFTPRRY 491
Cdd:PRK05765  233 YMITPRGY 240
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
252-491 1.21e-34

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 130.00  E-value: 1.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 252 VAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRV-PVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGDP 330
Cdd:PRK15478    2 LSVIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVkAFTGDKQVIKTGMCKEIERCQAAIELAQAGHNVALISSGDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 331 GVFAMATAVLE-EAKQWPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVISARLAAAAAADLVLAIYNP 409
Cdd:PRK15478   82 GIYGMAGLVLElVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSDLLTPWPVIEKRIVAAGEADFVICFYNP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 410 ASKARTWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIVGSSQTqwYSDDfgDRVFTPR 489
Cdd:PRK15478  162 RSRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDFEPVDMTSLVIVGNKTT--YVQD--GLMITPR 237

                  ..
gi 1184610966 490 RY 491
Cdd:PRK15478  238 GY 239
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
6-220 2.10e-30

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 117.44  E-value: 2.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   6 TLWGVGLGPGDPELVTVKAARLIGEADVVAYhsarhGRSIARGIAEPYLRPGQIeehlvypvtteatDHPGGYAGALEDF 85
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLG-----DDSRALEILLDLLPEDLY-------------FPMTEDKEPLEEA 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  86 YAEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTER-FNAVIVPGVTSVSAASAAIATPLVAGDEVLSVL---- 160
Cdd:pfam00590  63 YEEIAEALAAALRAGKDVARLVSGDPLVYGTGSYLVEALRAAgIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLflpg 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184610966 161 PGTLPVAELTRRLADADAAVVLKLGRSYPAVREALSAT-GQLDDAFYVERASTSGQRILPA 220
Cdd:pfam00590 143 LARIELRLLEALLANGDTVVLLYGPRRLAELAELLLELyPDTTPVAVVERAGTPDEKVVRG 203
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
251-457 8.34e-22

Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.


Pssm-ID: 425769 [Multi-domain]  Cd Length: 209  Bit Score: 93.18  E-value: 8.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 251 TVAVVGLGPGHSDWMTPQSRRELAAATDLIGYRT-YLDRVPVREGQRRHPSDNTDEPARARL-------ACALAEEGCAV 322
Cdd:pfam00590   1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSrALEILLDLLPEDLYFPMTEDKEPLEEAyeeiaeaLAAALRAGKDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 323 AVVSSGDPGVFAMATAVLEEAKQwPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDrLKPWEVISARLAAAAAADL 402
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRA-AGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLF-LPGLARIELRLLEALLANG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184610966 403 VLAI--YNPaskartWQVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLD 457
Cdd:pfam00590 159 DTVVllYGP------RRLAELAELLLELYPDTTPVAVVERAGTPDEKVVRGTLGELA 209
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
255-470 9.56e-18

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381167 [Multi-domain]  Cd Length: 219  Bit Score: 82.06  E-value: 9.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 255 VGLGPGHSDWMTPQSRRELAAATDLIGYRTY------LDRVPVREGQR-RHPSDNTDEPARARLACALAEEGCAVAVVSS 327
Cdd:cd09815     1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDskllslVLRAILKDGKRiYDLHDPNVEEEMAELLLEEARQGKDVAFLSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 328 GDPGVFAMATAVLEEAKQwPGVRIRVVPAMTAAQAVASRVGAPLGHDYAVISLSDRLKPWEVIsaRLAAAAAADLVLAIY 407
Cdd:cd09815    81 GDPGVAGTGAELVERAER-EGVEVKVIPGVSAADAAAAALGIDLGESFLFVTASDLLENPRLL--VLKALAKERRHLVLF 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184610966 408 NPASKARTwqvgAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLD---PAEVDMRCLLIVG 470
Cdd:cd09815   158 LDGHRFLK----ALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRaerTERGKPLTTILVG 219
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
254-380 6.85e-17

Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441842 [Multi-domain]  Cd Length: 207  Bit Score: 79.03  E-value: 6.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 254 VVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRVPVREGQRRHPSDNTDEparARLACALAEEGCAVAVVSSGDPGVF 333
Cdd:COG2241     6 VVGIGPGGPDGLTPAAREAIAEADVVVGGKRHLELFPDLGAERIVWPSPLSE---LLEELLALLRGRRVVVLASGDPLFY 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1184610966 334 AMATAVLEEAkqwPGVRIRVVPAMTAAQAVASRVGAPLgHDYAVISL 380
Cdd:COG2241    83 GIGATLARHL---PAEEVRVIPGISSLQLAAARLGWPW-QDAAVVSL 125
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
255-469 1.13e-15

Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.


Pssm-ID: 381171 [Multi-domain]  Cd Length: 198  Bit Score: 75.61  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 255 VGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRVPVREGQRRH-PSDNTDEpararLACALAEEGCAVAVVSSGDPGVF 333
Cdd:cd11644     1 IGIGPGGPEYLTPEAREAIEEADVVIGAKRLLELFPDLGAEKIPlPSEDIAE-----LLEEIAEAGKRVVVLASGDPGFY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 334 AMATAVLEEakqWPGVRIRVVPAMTAAQAVASRVGAPLgHDYAVISLSDRlkPWEVIsarlaaAAAADLVLAIYNPASKA 413
Cdd:cd11644    76 GIGKTLLRR---LGGEEVEVIPGISSVQLAAARLGLPW-EDARLVSLHGR--DLENL------RRALRRGRKVFVLTDGK 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184610966 414 RTwqVGAMRDVLMAHREPGTPVVIGRDVSGPAEDVRVVRLADLDPAEVDMRCLLIV 469
Cdd:cd11644   144 NT--PAEIARLLLERGLGDSRVTVGENLGYPDERITEGTAEELAEEEFSDLNVVLI 197
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
10-135 1.95e-13

uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381178 [Multi-domain]  Cd Length: 243  Bit Score: 69.89  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAYHSarhgrSIARGIAEpYLRPGQIEE--HLVYPvTTEATDHPGGYAGALEDFY- 86
Cdd:cd11724     5 VGVGPGDPDLITLRALKAIKKADVVFAPP-----DLRKRFAE-YLAGKEVLDdpHGLFT-YYGKKCSPLEEAEKECEELe 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184610966  87 ---AEATRRIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTERfNAVIVPG 135
Cdd:cd11724    78 kqrAEIVQKIREALAQGKNVALLDSGDPTIYGPWIWYLEEFADL-NPEVIPG 128
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
254-383 1.45e-10

precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL.


Pssm-ID: 274146 [Multi-domain]  Cd Length: 204  Bit Score: 60.79  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 254 VVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRVPVREGQRRHPSDNTDEPARARLACALAEEGCAVAVVSSGDPGVF 333
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIILTYKDLDELLEFIAATRKEKRVVVLASGDPLFY 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184610966 334 AMATAvleEAKQWPGVRIRVVPAMTAAQAVASRVGAPLgHDYAVISLSDR 383
Cdd:TIGR02467  81 GIGRT---LAERLGKERLEIIPGISSVQYAFARLGLPW-QDAVVISLHGR 126
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
7-135 3.14e-10

cobalt-precorrin-7 (C(5))-methyltransferase;


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 59.88  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   7 LWGVGLGPGDPELVTVKAARLIGEADVVaYHSARHgrsiargiaepylrpgqIEEhlvypvtteATDHPGGYAGALEDFY 86
Cdd:PRK05787    2 IYIVGIGPGDPEYLTLKALEAIRKADVV-VGSKRV-----------------LEL---------FPELIDGEAFVLTAGL 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1184610966  87 AEATRRIAAHlDAGRDVALLAEGDPLFYSsymhLHTRLTERFNAV----IVPG 135
Cdd:PRK05787   55 RDLLEWLELA-AKGKNVVVLSTGDPLFSG----LGKLLKVRRAVAedveVIPG 102
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
252-380 3.26e-10

cobalt-precorrin-7 (C(5))-methyltransferase;


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 59.88  E-value: 3.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 252 VAVVGLGPGHSDWMTPQSRRELAAATDLIGYRTYLDRVP-VREGQRRHPSDNTDEPARARLACALAEEgcaVAVVSSGDP 330
Cdd:PRK05787    2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPeLIDGEAFVLTAGLRDLLEWLELAAKGKN---VVVLSTGDP 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184610966 331 GVFAMATavLEEAKQWPGVRIRVVPAMTAAQAVASRVGAPLgHDYAVISL 380
Cdd:PRK05787   79 LFSGLGK--LLKVRRAVAEDVEVIPGISSVQYAAARLGIDM-NDVVFTTS 125
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
10-135 6.33e-09

S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.


Pssm-ID: 381167 [Multi-domain]  Cd Length: 219  Bit Score: 56.25  E-value: 6.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAYHSARHGRSIARGIAEpyLRPGQieeHLVYPvtteaTDHpggyagaleDFYAEA 89
Cdd:cd09815     1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLSLVLRAI--LKDGK---RIYDL-----HDP---------NVEEEM 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1184610966  90 TRRIAAHLDAGRDVALLAEGDPLFYSSYMHL-HTRLTERFNAVIVPG 135
Cdd:cd09815    62 AELLLEEARQGKDVAFLSPGDPGVAGTGAELvERAEREGVEVKVIPG 108
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
10-135 6.53e-09

Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.


Pssm-ID: 381171 [Multi-domain]  Cd Length: 198  Bit Score: 55.58  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAYhSARHGRSIARGIAE-PYLRPGQIEEHLvypvtteatdhpggyagaledfyae 88
Cdd:cd11644     1 IGIGPGGPEYLTPEAREAIEEADVVIG-AKRLLELFPDLGAEkIPLPSEDIAELL------------------------- 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184610966  89 atrriAAHLDAGRDVALLAEGDPLFYSsymhLHTRLTERFNA---VIVPG 135
Cdd:cd11644    55 -----EEIAEAGKRVVVLASGDPGFYG----IGKTLLRRLGGeevEVIPG 95
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
4-135 7.25e-09

Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 442122 [Multi-domain]  Cd Length: 256  Bit Score: 56.61  E-value: 7.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   4 RGTLWGVGLGPGDPELVTVKAARLIGEADVVAYhsarHGRSIARGIAEpYLRPG-QIeehlvypVTTEATDhpggyagaL 82
Cdd:COG2875     2 KGTVYFVGAGPGDPDLITVKGRRLLEEADVVLY----AGSLVPPELLA-YCKPGaEI-------VDSASMT--------L 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1184610966  83 EDFYAEatrrIAAHLDAGRDVALLAEGDPLFYSSYMHLHTRLTERFNAV-IVPG 135
Cdd:COG2875    62 EEIIAL----MKEAAAEGKDVVRLHSGDPSLYGAIAEQMRRLDALGIPYeVVPG 111
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
10-36 3.48e-08

Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.


Pssm-ID: 381168 [Multi-domain]  Cd Length: 225  Bit Score: 53.94  E-value: 3.48e-08
                          10        20
                  ....*....|....*....|....*..
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAY 36
Cdd:cd11641     1 VGAGPGDPELITVKGARLLEEADVVIY 27
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
3-36 6.62e-08

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 53.68  E-value: 6.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1184610966   3 ARGTLWGVGLGPGDPELVTVKAARLIGEADVVAY 36
Cdd:PRK06136    1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLY 34
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
4-36 1.16e-07

Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439778 [Multi-domain]  Cd Length: 245  Bit Score: 52.77  E-value: 1.16e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1184610966   4 RGTLWGVGLGPGDPELVTVKAARLIGEADVVAY 36
Cdd:COG0007     1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLY 33
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
7-135 1.26e-07

precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 200107  Cd Length: 247  Bit Score: 52.71  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966   7 LWGVGLGPGDPELVTVKAARLIGEADVVAYhsarHGRSIARGIAePYLRPGqieehlvypvtTEATDHPGGYAGALEDFY 86
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILY----AGSLVPPELL-AHCRPG-----------AEVVNSAGMSLEEIVDIM 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184610966  87 AEATRRiaahldaGRDVALLAEGDPLFYSSyMHLHTRLTERFNA--VIVPG 135
Cdd:TIGR01465  65 SDAHRE-------GKDVARLHSGDPSIYGA-IAEQMRLLEALGIpyEVVPG 107
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
10-36 6.57e-07

Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.


Pssm-ID: 381169  Cd Length: 228  Bit Score: 50.13  E-value: 6.57e-07
                          10        20
                  ....*....|....*....|....*..
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAY 36
Cdd:cd11642     1 VGAGPGDPDLLTLKALRALQQADVVLY 27
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
10-135 2.00e-06

precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL.


Pssm-ID: 274146 [Multi-domain]  Cd Length: 204  Bit Score: 48.47  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVAyHSARHGRSIARGIAEPYlrpgqieehlvypvttEATDHPGGYAGALEdfyaea 89
Cdd:TIGR02467   2 VGIGPGGPELLTPAAIEAIRKADLVV-GGERHLELLAELIGEKR----------------EIILTYKDLDELLE------ 58
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1184610966  90 trRIAAhLDAGRDVALLAEGDPLFYSsymhLHTRLTERF---NAVIVPG 135
Cdd:TIGR02467  59 --FIAA-TRKEKRVVVLASGDPLFYG----IGRTLAERLgkeRLEIIPG 100
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
255-372 2.36e-06

Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.


Pssm-ID: 381172 [Multi-domain]  Cd Length: 223  Bit Score: 48.66  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 255 VGLGPGHSDWMT---------------PQSRRELAAATDLIGYRTYLDRVPV----------REGQRRHPSDNTDEpara 309
Cdd:cd11645     1 VGVGPGDPELLTlkavrilkeadvifvPVSKGGEGSAALIIAAALLIPDKEIiplefpmtkdREELEEAWDEAAEE---- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184610966 310 rlACALAEEGCAVAVVSSGDPGVFAMATAVLEEAKQwPGVRIRVVPAMTAAQAVASRVGAPLG 372
Cdd:cd11645    77 --IAEELKEGKDVAFLTLGDPSLYSTFSYLLERLRA-PGVEVEIIPGITSFSAAAARLGIPLA 136
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
10-135 3.19e-06

Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441842 [Multi-domain]  Cd Length: 207  Bit Score: 47.83  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVaYHSARHGRSIARGIAEpylrpgQIEEhlvypvtteatdhPGGYAGALEdfyaea 89
Cdd:COG2241     7 VGIGPGGPDGLTPAAREAIAEADVV-VGGKRHLELFPDLGAE------RIVW-------------PSPLSELLE------ 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1184610966  90 trRIAAHLdAGRDVALLAEGDPLFYSsymhLHTRLTERFNA---VIVPG 135
Cdd:COG2241    61 --ELLALL-RGRRVVVLASGDPLFYG----IGATLARHLPAeevRVIPG 102
Precorrin-6A-synthase cd11643
Precorrin-6A synthase (also named CobF); Precorrin-6A synthase participates in the pathway ...
10-134 6.33e-06

Precorrin-6A synthase (also named CobF); Precorrin-6A synthase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model represents CobF, the precorrin-6A synthase, an enzyme specific to the aerobic pathway. After precorrin-4 is methylated at C-11 by CobM to produce precorrin-5, CobF catalyzes the removal of the extruded acyl group in the subsequent step, and the addition of a methyl group at C-1. The product of this reaction is precorrin-6A, which gets reduced by an NADH-dependent reductase to yield precorrin-6B. This family includes enzymes in GC-rich Gram-positive bacteria, alpha proteobacteria and Pseudomonas-related species.


Pssm-ID: 381170  Cd Length: 244  Bit Score: 47.49  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVV-AYHSARHGRSIA---RGIAEPYLRPGQIEeHLVYPVTTEATDhPGGYAGALEDF 85
Cdd:cd11643     2 IGIGPGDPDHLTLQAIEALNRVDVFfVLDKGEEKSDLAalrREICERHLGDRPYR-VVEFPDPERDRS-PADYRAAVADW 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1184610966  86 YAEATRR----IAAHLDAGRDVALLAEGDPLFYSSYMhlhtRLTERFNAVIVP 134
Cdd:cd11643    80 HDARAALwedaIAEELPEGGTGAFLVWGDPSLYDSTL----RILDRLRAGRVA 128
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
250-372 6.45e-06

precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273642 [Multi-domain]  Cd Length: 230  Bit Score: 47.30  E-value: 6.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAATDL-----------IGYRT---YLDRVPVREgQRRHPSDNTDEP-------AR 308
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIavpaskkgresLARKIvedYLKPNDTRI-LELVFPMTKDRDelekawdEA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184610966 309 ARLACALAEEGCAVAVVSSGDPGVFAMATAVLEeAKQWPGVRIRVVPAMTAAQAVASRVGAPLG 372
Cdd:TIGR01467  80 AEAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQ-RLQGMGIEVEVVPGITSFAACASAAGLPLV 142
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
1-36 1.11e-05

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 46.93  E-value: 1.11e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1184610966   1 MSARGTLWGVGLGPGDPELVTVKAARLIGEADVVAY 36
Cdd:PLN02625   11 LEGPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLY 46
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
7-36 9.10e-05

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 43.98  E-value: 9.10e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1184610966   7 LWGVGLGPGDPELVTVKAARLIGEADVVAY 36
Cdd:PRK15473   10 VWFVGAGPGDKELITLKGYRLLQQAQVVIY 39
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
327-470 2.16e-04

Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 439778 [Multi-domain]  Cd Length: 245  Bit Score: 42.75  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 327 SGDPGVFAMAT---AVLEEAkqwpGVRIRVVPAMTAAQAVASRVGAPLGH-DYA----VISLSDR----LKPWEVISarl 394
Cdd:COG0007    87 GGDPFVFGRGGeeaEALAAA----GIPFEVVPGITAAIAAPAYAGIPLTHrGVAssvtFVTGHEKdgklDLDWAALA--- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 395 aaaaAADLVLAIYNPASKArtwqvGAMRDVLMAH-REPGTPVVIGRDVSGPAEDVRVVRLADL----DPAEVDMRCLLIV 469
Cdd:COG0007   160 ----RPGGTLVIYMGVKNL-----PEIAAALIAAgRSPDTPVAVIENGTTPDQRVVTGTLATLaelaAEAGLKSPALIVV 230

                  .
gi 1184610966 470 G 470
Cdd:COG0007   231 G 231
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
10-114 2.48e-04

precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273641 [Multi-domain]  Cd Length: 239  Bit Score: 42.67  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADV-VAYhsarhgrsiargiaEPYLRpgqieehLVYPVTTEATDHPGGYAGALEdfyaE 88
Cdd:TIGR01466   4 VGIGPGAEELMTPEAKEALAEADViVGY--------------KTYLD-------LIEDLIPGKEVVTSGMREEIA----R 58
                          90       100
                  ....*....|....*....|....*.
gi 1184610966  89 ATRRIAAHLdAGRDVALLAEGDPLFY 114
Cdd:TIGR01466  59 AELAIELAA-EGRTVALVSSGDPGIY 83
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
250-371 2.03e-03

Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441844 [Multi-domain]  Cd Length: 229  Bit Score: 39.70  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAAtDLIgyrTYLDRVPVREGQRR-----HPSDN---------TDEPARARLA--- 312
Cdd:COG2243     3 GKLYGVGVGPGDPELLTLKAVRALREA-DVI---AYPAKGAGKASLAReivapYLPPArivelvfpmTTDYEALVAAwde 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184610966 313 -----CALAEEGCAVAVVSSGDPGVFAMATAVLEEAKQWpGVRIRVVPAMTAAQAVASRVGAPL 371
Cdd:COG2243    79 aaariAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRER-GFEVEVIPGITSFSAAAAALGIPL 141
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
255-470 2.52e-03

Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.


Pssm-ID: 381169  Cd Length: 228  Bit Score: 39.34  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 255 VGLGPGHSDWMTPQSRRELAAAtDLIGY------------RTYLDRVPV--REGQRRHPSDNTDEpararLACALAEEGC 320
Cdd:cd11642     1 VGAGPGDPDLLTLKALRALQQA-DVVLYdrlvspeilalaPPGAELIYVgkRPGRHSVPQEEINE-----LLVELAREGK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 321 AVAVVSSGDPGVFAMAT---AVLEEAkqwpGVRIRVVPAMTAAQAVASRVGAPLGH-DYA--VISLSDRLKPwEVISARL 394
Cdd:cd11642    75 RVVRLKGGDPFVFGRGGeeiEALREA----GIPFEVVPGITSAIAAAAYAGIPLTHrGVAssVTFVTGHEAD-GKLPDDD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 395 AAAAAADLVLAIYNPASKARTWQvgamrDVLMAH-REPGTPVVIGRDVSGPAEDVRVVRLADL----DPAEVDMRCLLIV 469
Cdd:cd11642   150 AALARPGGTLVIYMGVSNLEEIA-----ERLIAAgLPPDTPVAIVENATTPDQRVVVGTLAELaekaAEAGIRSPALIVV 224

                  .
gi 1184610966 470 G 470
Cdd:cd11642   225 G 225
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
249-373 4.18e-03

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 38.84  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 249 AGTVAVVGLGPGHSDWMTPQSRRELAAAtDLIGY-----RTYLDRVP---VREGQRRHPSDNT-DEPARARLACALAEEG 319
Cdd:PLN02625   14 PGNVFLVGTGPGDPDLLTLKALRLLQTA-DVVLYdrlvsPDILDLVPpgaELLYVGKRGGYHSrTQEEIHELLLSFAEAG 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184610966 320 CAVAVVSSGDPGVFAMA-TAVLEEAKQwpGVRIRVVPAMTAAQAVASRVGAPLGH 373
Cdd:PLN02625   93 KTVVRLKGGDPLVFGRGgEEMDALRKN--GIPVTVVPGITAAIGAPAELGIPLTH 145
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
250-376 4.59e-03

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 38.66  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966 250 GTVAVVGLGPGHSDWMTPQSRRELAAAT-----DLIG------YRTYLDRVPV--REGQRRHPSDNTDEpararLACALA 316
Cdd:PRK06136    3 GKVYLVGAGPGDPDLITLKGVRLLEQADvvlydDLVSpeilayAKPDAELIYVgkRAGRHSTKQEEINR-----LLVDYA 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184610966 317 EEGCAVAVVSSGDPGVFAMA---TAVLEEAkqwpGVRIRVVPAMTAAQAVASRVGAPLGH-DYA 376
Cdd:PRK06136   78 RKGKVVVRLKGGDPFVFGRGgeeLEALEAA----GIPYEVVPGITAAIAAAAYAGIPLTHrGVA 137
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
10-135 5.12e-03

N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known.


Pssm-ID: 381177  Cd Length: 218  Bit Score: 38.24  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVayhsarhgrsiargiaepYLRpgqIEEHlvyPVTTEATDHPGGYaGALEDFYAEA 89
Cdd:cd11723     4 VGLGPGDPDLLTLGALEALKSADKV------------------YLR---TARH---PVVEELKEEGIEF-ESFDDLYEEA 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184610966  90 T------RRIAAHLDA---GRDVALLAEGDPLFY-SSYMHLHTRLTERFNAVIVPG 135
Cdd:cd11723    59 EdfeevyEAIAERLLEaaeHGDVVYAVPGHPLVAeRTVQLLLERAEEGIEVEIIPG 114
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
10-35 7.40e-03

Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone.


Pssm-ID: 381173 [Multi-domain]  Cd Length: 238  Bit Score: 38.16  E-value: 7.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 1184610966  10 VGLGPGDPELVTVKAARLIGEADVVA 35
Cdd:cd11646     4 VGIGPGSADLMTPRAREALEEADVIV 29
 
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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