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Conserved domains on  [gi|518284900|ref|WP_019455108|]
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MULTISPECIES: siroheme synthase CysG [Serratia]

Protein Classification

siroheme synthase( domain architecture ID 1001131)

siroheme synthase catalyzes all three steps of siroheme biosynthesis, including methylation, oxidation, and iron insertion into the tetrapyrrole uroporphyrinogen III (Uro-III)

Gene Ontology:  GO:0051266
PubMed:  14595395

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cysG super family cl32546
siroheme synthase CysG;
1-461 0e+00

siroheme synthase CysG;


The actual alignment was detected with superfamily member PRK10637:

Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 549.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900   1 MDYLPIFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEQQRQLGRVLWLGESFDPQQLDDVFLAIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  81 DDNALNAAVFAEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALLPASLGQMAQVAGR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 161 WRGQVKQRLASIGERRRFWEKTF-GGRFATLVANGQTAQAERQLEQDLHhfAAGDEgaQGEIALVGAGPGDVGLLTLRGL 239
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAVTETTEQLFS--EPLDH--RGEVVLVGAGPGDAGLLTLKGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 240 QVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLKGGDPFIFGRGGEELQV 319
Cdd:PRK10637 237 QQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELET 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 320 AAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDgLDWADLARARQTLAIYMGTMKAADISQRLI 399
Cdd:PRK10637 317 LCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGE-LDWENLAAEKQTLVFYMGLNQAATIQQKLI 395

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518284900 400 AHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPLPALLVIGEVVELHHQIAWFGHQ 461
Cdd:PRK10637 396 EHGMPADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH 457
 
Name Accession Description Interval E-value
cysG PRK10637
siroheme synthase CysG;
1-461 0e+00

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 549.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900   1 MDYLPIFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEQQRQLGRVLWLGESFDPQQLDDVFLAIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  81 DDNALNAAVFAEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALLPASLGQMAQVAGR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 161 WRGQVKQRLASIGERRRFWEKTF-GGRFATLVANGQTAQAERQLEQDLHhfAAGDEgaQGEIALVGAGPGDVGLLTLRGL 239
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAVTETTEQLFS--EPLDH--RGEVVLVGAGPGDAGLLTLKGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 240 QVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLKGGDPFIFGRGGEELQV 319
Cdd:PRK10637 237 QQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELET 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 320 AAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDgLDWADLARARQTLAIYMGTMKAADISQRLI 399
Cdd:PRK10637 317 LCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGE-LDWENLAAEKQTLVFYMGLNQAATIQQKLI 395

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518284900 400 AHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPLPALLVIGEVVELHHQIAWFGHQ 461
Cdd:PRK10637 396 EHGMPADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH 457
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 218-458 8.52e-133

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: 383.27  E-value: 8.52e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 218 QGEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGK 297
Cdd:COG0007    1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 298 RVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDGLDWADLAR 377
Cdd:COG0007   81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 378 ARQTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVELHHQI 455
Cdd:COG0007  161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLksPALIVVGEVVALREKL 240


                 ...
gi 518284900 456 AWF 458
Cdd:COG0007  241 SWF 243
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 224-449 7.74e-113

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: 332.09  E-value: 7.74e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLK 303
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 304 GGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDGLDWADLARARQTLA 383
Cdd:cd11642   81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518284900 384 IYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVV 449
Cdd:cd11642  161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIrsPALIVVGEVV 228
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 221-452 6.18e-106

uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273643  Cd Length: 236  Bit Score: 314.55  E-value: 6.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  221 IALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVV 300
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  301 RLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDG-LDWADLARAR 379
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALeVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518284900  380 QTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVELH 452
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLksPALIVIGEVVALR 236
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 221-431 1.31e-44

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: 155.19  E-value: 1.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  221 IALVGAGPGDVGLLTLRGLQVMQQADVVLYDH-LVSGEILDLVRRDAERIcVGKRAGAHSVIQEETNRLLVELAQQGKRV 299
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDsRALEILLDLLPEDLYFP-MTEDKEPLEEAYEEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  300 VRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDglDWADLARAR 379
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELR--LLEALLANG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 518284900  380 QTLAIYMGTMKAADISQRLIAHgRDAATPVAVISRGTRADQQVQIGTLDQLE 431
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLEL-YPDTTPVAVVERAGTPDEKVVRGTLGELA 209
 
Name Accession Description Interval E-value
cysG PRK10637
siroheme synthase CysG;
1-461 0e+00

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 549.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900   1 MDYLPIFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEQQRQLGRVLWLGESFDPQQLDDVFLAIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  81 DDNALNAAVFAEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALLPASLGQMAQVAGR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 161 WRGQVKQRLASIGERRRFWEKTF-GGRFATLVANGQTAQAERQLEQDLHhfAAGDEgaQGEIALVGAGPGDVGLLTLRGL 239
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAVTETTEQLFS--EPLDH--RGEVVLVGAGPGDAGLLTLKGL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 240 QVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLKGGDPFIFGRGGEELQV 319
Cdd:PRK10637 237 QQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELET 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 320 AAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDgLDWADLARARQTLAIYMGTMKAADISQRLI 399
Cdd:PRK10637 317 LCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGE-LDWENLAAEKQTLVFYMGLNQAATIQQKLI 395

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518284900 400 AHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPLPALLVIGEVVELHHQIAWFGHQ 461
Cdd:PRK10637 396 EHGMPADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH 457
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 218-458 8.52e-133

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: 383.27  E-value: 8.52e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 218 QGEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGK 297
Cdd:COG0007    1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 298 RVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDGLDWADLAR 377
Cdd:COG0007   81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 378 ARQTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVELHHQI 455
Cdd:COG0007  161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLksPALIVVGEVVALREKL 240


                 ...
gi 518284900 456 AWF 458
Cdd:COG0007  241 SWF 243
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 224-449 7.74e-113

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: 332.09  E-value: 7.74e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLK 303
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 304 GGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDGLDWADLARARQTLA 383
Cdd:cd11642   81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518284900 384 IYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVV 449
Cdd:cd11642  161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIrsPALIVVGEVV 228
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
217-461 1.08e-111

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 329.87  E-value: 1.08e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 217 AQGEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQG 296
Cdd:PRK06136   1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 297 KRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGD--GLDWAD 374
Cdd:PRK06136  81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLepEVNWSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 375 LARARQTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVELH 452
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIqsPAIIVIGEVVALR 240


                 ....*....
gi 518284900 453 HQIAWFGHQ 461
Cdd:PRK06136 241 AKLAWFEAQ 249
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 221-452 6.18e-106

uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273643  Cd Length: 236  Bit Score: 314.55  E-value: 6.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  221 IALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVV 300
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  301 RLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDG-LDWADLARAR 379
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALeVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518284900  380 QTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVELH 452
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLksPALIVIGEVVALR 236
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 1-205 9.04e-96

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 287.82  E-value: 9.04e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900   1 MDYLPIFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEQQRQLGRVLWLGESFDPQQLDDVFLAIAAT 80
Cdd:COG1648    1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  81 DDNALNAAVFAEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALLPASLGQMAQVAGR 160
Cdd:COG1648   81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 518284900 161 WRGQVKQRLASIGERRRFWEKTFGGRFATLVANGQTAQAERQLEQ 205
Cdd:COG1648  161 LRERVKARLPDGAERRRFWERLLDGPLAELLRAGDEEEAEALLEE 205
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
 219-457 4.52e-86

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 264.96  E-value: 4.52e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 219 GEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKR 298
Cdd:PLN02625  15 GNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSFAEAGKT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 299 VVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDG-DGLD-WADLA 376
Cdd:PLN02625  95 VVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGtDPLDvAEAAA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 377 RARQTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVELHHQ 454
Cdd:PLN02625 175 DPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLvsPTVIVVGEVVALSPL 254


                 ...
gi 518284900 455 IAW 457
Cdd:PLN02625 255 WPW 257
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 4-207 4.56e-79

siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 130536 [Multi-domain]  Cd Length: 205  Bit Score: 244.62  E-value: 4.56e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900    4 LPIFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEQQRQLGRVLWLGESFDPQQLDDVFLAIAATDDN 83
Cdd:TIGR01470   1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900   84 ALNAAVFAEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALLPASLGQMAQVAGRWRG 163
Cdd:TIGR01470  81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 518284900  164 QVKQRLASIGERRRFWEKTFGGRFATLVANGQTAQAERQLEQDL 207
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFDGAFAERVLAGREEQAERVLATRL 204
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
219-457 1.72e-61

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 207.92  E-value: 1.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 219 GEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKR 298
Cdd:PRK07168   3 GYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEGKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 299 VVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCR-PDGDGLDWADLAR 377
Cdd:PRK07168  83 VVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAKgPLTDHGKYNSSHN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 378 ArQTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVELHHQI 455
Cdd:PRK07168 163 S-DTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENIsnPSMTIVGDVVSLRNQI 241


                 ..
gi 518284900 456 AW 457
Cdd:PRK07168 242 AW 243
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 224-450 4.07e-46

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: 159.87  E-value: 4.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVLY-DHLVSGEILDLVRRDAERIcvgkraGAHSVIQEETNRLLVELAQQGKRVVRL 302
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV------DSAGMTLEEIIEVMREAAREGKDVVRL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 303 KGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCR---PDGDGLdwADLARAR 379
Cdd:cd11641   75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRtpvPEGESL--RELAKHG 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518284900 380 QTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVVE 450
Cdd:cd11641  153 ATLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGItrTALILVGPALG 225
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 221-431 1.31e-44

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: 155.19  E-value: 1.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  221 IALVGAGPGDVGLLTLRGLQVMQQADVVLYDH-LVSGEILDLVRRDAERIcVGKRAGAHSVIQEETNRLLVELAQQGKRV 299
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDsRALEILLDLLPEDLYFP-MTEDKEPLEEAYEEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  300 VRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCRPDGDglDWADLARAR 379
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELR--LLEALLANG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 518284900  380 QTLAIYMGTMKAADISQRLIAHgRDAATPVAVISRGTRADQQVQIGTLDQLE 431
Cdd:pfam00590 159 DTVVLLYGPRRLAELAELLLEL-YPDTTPVAVVERAGTPDEKVVRGTLGELA 209
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
 218-450 1.35e-41

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: 148.67  E-value: 1.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 218 QGEIALVGAGPGDVGLLTLRGLQVMQQADVVLY-DHLVSGEILDLVRRDAERIcvgkraGAHSVIQEETNRLLVELAQQG 296
Cdd:COG2875    2 KGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIV------DSASMTLEEIIALMKEAAAEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 297 KRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCR---PDGDGLdwA 373
Cdd:COG2875   76 KDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRtpmPEGESL--A 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518284900 374 DLARARQTLAIYMGTMKAADISQRLIAHgRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPLP--ALLVIGEVVE 450
Cdd:COG2875  154 SLAAHGATLAIYLSAHRIDEVVEELLEG-YPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITrtALILVGPALG 231
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
 224-449 2.05e-40

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: 145.55  E-value: 2.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  224 VGAGPGDVGLLTLRGLQVMQQADVVLY-DHLVSGEILDLVRRDAEricVGKRAGAHsviQEETNRLLVELAQQGKRVVRL 302
Cdd:TIGR01465   4 IGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAE---VVNSAGMS---LEEIVDIMSDAHREGKDVARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  303 KGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGHCR---PDGDGLdwADLARAR 379
Cdd:TIGR01465  78 HSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRtpmPEGEKL--ADLAKHG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518284900  380 QTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIGEVV 449
Cdd:TIGR01465 156 ATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIyrTTLILVGPAL 227
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 6-115 2.23e-33

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 121.81  E-value: 2.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900    6 IFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEqqrqlGRVLWLGESFdPQQLDDVFLAIAATDDNAL 85
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEITPFLE-----GLLDLIRREF-EGDLDGADLVIAATDDPEL 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 518284900   86 NAAVFAEADKRRVLANVVDDQPRCSFIFPS 115
Cdd:pfam13241  75 NERIAALARARGILVNVADDPELCDFYFPA 104
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 224-446 1.45e-31

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: 120.58  E-value: 1.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSgEILDLVRRDAERICVGKRAGAHSVIQEETNRLLVELAQQGKRVVRLK 303
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDS-KLLSLVLRAILKDGKRIYDLHDPNVEEEMAELLLEEARQGKDVAFLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 304 GGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLthrdhAQSVTFITGH-CRPDGDGLDWADLARARQTL 382
Cdd:cd09815   80 PGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASdLLENPRLLVLKALAKERRHL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518284900 383 AIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHL-AQRAPLPALLVIG 446
Cdd:cd09815  155 VLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAErTERGKPLTTILVG 219
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
224-446 4.77e-29

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 114.85  E-value: 4.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVLY-DHLVSGEILDLVRRDAERicvGKRAGAHsviQEETNRLLVELAQQGKRVVRL 302
Cdd:PRK15473  13 VGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAEC---HDSAELH---LEQIIDLMEAGVKAGKTVVRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 303 KGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDHAQSV--TFITGHC-RPDGDGLDwaDLARAR 379
Cdd:PRK15473  87 QTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLiiTRMEGRTpVPAREQLE--SFASHQ 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518284900 380 QTLAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHLAQRAPL--PALLVIG 446
Cdd:PRK15473 165 TSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIrkTALILVG 233
PRK06718 PRK06718
NAD(P)-binding protein;
5-153 7.02e-25

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 101.65  E-value: 7.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900   5 PIFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEQQRQLGRVLWLGESFDPQQLDDVFLAIAATDDNA 84
Cdd:PRK06718   3 PLMIDLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVISPELTENLVKLVEEGKIRWKQKEFEPSDIVDAFLVIAATNDPR 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518284900  85 LNAAVfAEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALLPASLGQ 153
Cdd:PRK06718  83 VNEQV-KEDLPENALFNVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYES 150
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
 223-446 1.41e-24

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: 101.86  E-value: 1.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 223 LVGAGPGDVGLLTLRGLQVMQQADVVL--------YDHLVSG-EILD--------LVRRDAERICVGKRAGAHSVIQEET 285
Cdd:cd11724    4 LVGVGPGDPDLITLRALKAIKKADVVFappdlrkrFAEYLAGkEVLDdphglftyYGKKCSPLEEAEKECEELEKQRAEI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 286 NRLLVELAQQGKRVVRLKGGDPFIFGRGG---EELQVAAAagipfQVVPGVTAAAGATAYAGIPLTHRDHAQSVTFITGH 362
Cdd:cd11724   84 VQKIREALAQGKNVALLDSGDPTIYGPWIwylEEFADLNP-----EVIPGVSSFNAANAALKRSLTGGGDSRSVILTAPF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 363 CRPDGDGLdWADLARARQTLAIYMGTMKAADISQRLiAHGRDAATPVAVISR-GTRADQQVQIGTLDQLEHLAQRAPLPA 441
Cdd:cd11724  159 ALKENEDL-LEDLAATGDTLVIFMMRLDLDELVEKL-KKHYPPDTPVAIVYHaGYSEKEKVIRGTLDDILEKLGGEKEPF 236


                 ....*..
gi 518284900 442 --LLVIG 446
Cdd:cd11724  237 lgLIYVG 243
PRK06719 PRK06719
precorrin-2 dehydrogenase; Validated
 5-156 5.28e-20

precorrin-2 dehydrogenase; Validated


Pssm-ID: 180668 [Multi-domain]  Cd Length: 157  Bit Score: 86.56  E-value: 5.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900   5 PIFADLKQRPVLVVGGGDVAARKVDLLQRAGAEIRIVaqslSPEL-EQQRQLGRVLWLGESFDPQQLDDVFLAIAATDDN 83
Cdd:PRK06719   6 PLMFNLHNKVVVIIGGGKIAYRKASGLKDTGAFVTVV----SPEIcKEMKELPYITWKQKTFSNDDIKDAHLIYAATNQH 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518284900  84 ALNAAVfAEADKRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALLPASLGQMAQ 156
Cdd:PRK06719  82 AVNMMV-KQAAHDFQWVNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQELTSILPKLIKKISR 153
CysG_dimerizer pfam10414
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the ...
 152-207 1.42e-16

Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the iron-containing porphinoid sirohaem. CysG, S-adenosyl-L-methionine (SAM)-dependent bis-methyltransferase, dehydrogenase and ferrochelatase, synthesizes sirohaem from uroporphyrinogen III via reactions which encompass two branchpoint intermediates in tetrapyrrole biosynthesis, diverting flux first from protoporphyrin IX biosynthesis and then from cobalamin (vitamin B12) biosynthesis. CysG is a dimer of two structurally similar protomers held together asymmetrically through a number of salt-bridges across complementary residues in the CysG_dimerizer region to produce a series of active sites, accounting for CysG's multifunctionality, catalysing four diverse reactions: two SAM-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation. The CysG_dimerizer region holding the two protomers together is of 74 residues.


Pssm-ID: 431269 [Multi-domain]  Cd Length: 56  Bit Score: 73.74  E-value: 1.42e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 518284900  152 GQMAQVAGRWRGQVKQRLASIGERRRFWEKTFGGRFATLVANGQTAQAERQLEQDL 207
Cdd:pfam10414   1 GRLAALAGRFRDRVKARLPDVAARRRFWERVFDGPVAELVLAGDEDEAEALLEQAL 56
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
 216-431 1.42e-13

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: 70.48  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 216 GAQGEIALVGAGPGDVGLLTLRGLQVMQQADVV----LYdhlvsgeiLDLV---RRDAERICVGKRagahsviqEETNR- 287
Cdd:COG1010    1 PMRGKLYVVGLGPGSAELMTPRARAALAEADVVvgygTY--------LDLIpplLPGKEVHASGMR--------EEVERa 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 288 -LLVELAQQGKRVVRLKGGDPFIFGRGGEELQVA----AAAGIPFQVVPGVTAAAGATAYAGIPLTHrDHAQ---Svtfi 359
Cdd:COG1010   65 rEALELAAEGKTVAVVSSGDPGVYGMAGLVLEVLeeggAWRDVEVEVVPGITAAQAAAARLGAPLGH-DFCVislS---- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 360 tghcrpdgDGL-DW------------ADLA--------RARQT-LAiymgtmKAADIsqrLIAHgRDAATPVAVISRGTR 417
Cdd:COG1010  140 --------DLLtPWeviekrlraaaeADFVialynprsRKRPWqLE------RALEI---LLEH-RPPDTPVGIVRNAGR 201

                        250
                 ....*....|....
gi 518284900 418 ADQQVQIGTLDQLE 431
Cdd:COG1010  202 PDESVTVTTLGELD 215
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 221-430 4.83e-13

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: 68.60  E-value: 4.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 221 IALVGAGPGDVGLLTLRGLQVMQQADVV----LYdhlvsgeiLDLVR---RDAERICVGKRagahsviqEETNR--LLVE 291
Cdd:cd11646    1 LYVVGIGPGSADLMTPRAREALEEADVIvgykTY--------LDLIEdllPGKEVISSGMG--------EEVERarEALE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 292 LAQQGKRVVRLKGGDPFIFGRGGEELQVAAAAG--IPFQVVPGVTAAAGATAYAGIPLTHrDHAQ---Svtfitghcrpd 366
Cdd:cd11646   65 LALEGKRVALVSSGDPGIYGMAGLVLELLDERWddIEVEVVPGITAALAAAALLGAPLGH-DFAVislS----------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 367 gDGL-DW------------ADLArarqtLAIY-------MGTMKAAdisQRLIAHGRDAATPVAVISRGTRADQQVQIGT 426
Cdd:cd11646  133 -DLLtPWeviekrlraaaeADFV-----IALYnprskkrPWQLEKA---LEILLEHRPPDTPVGIVRNAGREGEEVTITT 203


                 ....
gi 518284900 427 LDQL 430
Cdd:cd11646  204 LGEL 207
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 219-422 9.24e-12

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: 64.73  E-value: 9.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 219 GEIALVGAGPGDVGLLTLRGLQVMQQADVVLY----------------DHLVSGEILDL---VRRDAERicvgkRAGAHs 279
Cdd:COG2243    3 GKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslareivaPYLPPARIVELvfpMTTDYEA-----LVAAW- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 280 viqEETNRLLVELAQQGKRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDhaQSVTFI 359
Cdd:COG2243   77 ---DEAAARIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLAEGD--EPLTVL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518284900 360 TGHCRPDG--DGLDWADlararqTLAIymgtMKA----ADISQRLIAHGRDAAtpVAVISRGTRADQQV 422
Cdd:COG2243  152 PGTLLEEEleRALDDFD------TVVI----MKVgrnfPKVREALEEAGLLDR--AWYVERAGMPDERI 208
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 221-446 5.98e-11

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: 62.32  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  221 IALVGAGPGDVGLLTLRGLQVMQQADVV----LYDHLVSgeilDLvRRDAERICVGKRagahsviqEETNR--LLVELAQ 294
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIvgykTYLDLIE----DL-IPGKEVVTSGMR--------EEIARaeLAIELAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  295 QGKRVVRLKGGDPFIFGRGGEELQVAAAAG--IPFQVVPGVTAAAGATAYAGIPLTHrDHAqsVTFITGHCRPdgdgldW 372
Cdd:TIGR01466  68 EGRTVALVSSGDPGIYGMAALVFEALEKKGaeVDIEVIPGITAASAAASLLGAPLGH-DFC--VISLSDLLTP------W 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  373 ADL-------ARARQTLAIY--------MGTMKAADIsqrlIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEhlAQRA 437
Cdd:TIGR01466 139 PEIekrlraaAEADFVIAIYnprskrrpEQFRRAMEI----LLEHRKPDTPVGIVRNAGREGEEVEITTLAELD--EELI 212


                  ....*....
gi 518284900  438 PLPALLVIG 446
Cdd:TIGR01466 213 DMLTTVIIG 221
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
 224-422 6.00e-11

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: 62.33  E-value: 6.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  224 VGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGE-------ILDLVRRDAERIC-----VGKRAGAHSVIQEETNRLLVE 291
Cdd:TIGR01467   6 VGVGPGDPELITVKALEALRSADVIAVPASKKGReslarkiVEDYLKPNDTRILelvfpMTKDRDELEKAWDEAAEAVAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  292 LAQQGKRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDhaQSVTFITGHCRPD--GDG 369
Cdd:TIGR01467  86 ELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEGD--ESLAILPATAGEAelEKA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 518284900  370 LDWADlararqTLAIYMGTMKAADISQRLIAHGR-DAAtpvAVISRGTRADQQV 422
Cdd:TIGR01467 164 LAEFD------TVVLMKVGRNLPQIKEALAKLGRlDAA---VVVERATMPDEKI 208
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 223-444 4.80e-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: 59.25  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  223 LVGAGPGDVGLLTLRGLQVMQQADVVlydhlVSGE-ILDLVRrdaERICVGKRAGAHSVIQEETNRLLVELAQQgKRVVR 301
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLV-----VGGErHLELLA---ELIGEKREIILTYKDLDELLEFIAATRKE-KRVVV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  302 LKGGDPFIFGRGGEELQVAAAAGIpfQVVPGVTAAAGATAYAGIPLthrdhaQSVTFITGHCRPDgDGLDWADLARARQT 381
Cdd:TIGR02467  72 LASGDPLFYGIGRTLAERLGKERL--EIIPGISSVQYAFARLGLPW------QDAVVISLHGREL-DELLLALLRGHRKV 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518284900  382 LAIYMGTMKAADISQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQLEHlAQRAPLPALLV 444
Cdd:TIGR02467 143 AVLTDPRNGPAEIARELIELGIGGSYELTVGENLGYEDERITEGTLEEIAA-AQFDFSPLLVV 204
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 224-422 7.52e-10

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: 59.06  E-value: 7.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVLY-------DHLVSGEILDLVRRDAERICV----GKRAGAHSVIQEETNRLLVEL 292
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggeGSAALIIAAALLIPDKEIIPLefpmTKDREELEEAWDEAAEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 293 AQQGKRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDhaQSVTFITGHCRPDgdglDW 372
Cdd:cd11645   81 LKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLAILPATYDEE----EL 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 518284900 373 ADLARARQTLAIYMGTMKAADISQRLIAHGRDAatPVAVISRGTRADQQV 422
Cdd:cd11645  155 EKALENFDTVVLMKVGRNLEEIKELLEELGLLD--KAVYVERCGMEGERI 202
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 224-445 1.23e-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: 57.89  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVlydhlVSGE-ILDLVRR-DAERICVGKragahsviqEETNRLLVELAQQGKRVVR 301
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVV-----IGAKrLLELFPDlGAEKIPLPS---------EDIAELLEEIAEAGKRVVV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 302 LKGGDPFIFG--------RGGEELQV----------AAAAGIPFqvvpgvtaaagatayagiplthrdhaQSVTFITGHC 363
Cdd:cd11644   67 LASGDPGFYGigktllrrLGGEEVEVipgissvqlaAARLGLPW--------------------------EDARLVSLHG 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 364 RPDGdglDWADLARARQTLAIYM-GTMKAADISQRLIAHGRDAATpVAVISRGTRADQQVQIGTLDQLEHlaQRAPLPAL 442
Cdd:cd11644  121 RDLE---NLRRALRRGRKVFVLTdGKNTPAEIARLLLERGLGDSR-VTVGENLGYPDERITEGTAEELAE--EEFSDLNV 194


                 ...
gi 518284900 443 LVI 445
Cdd:cd11644  195 VLI 197
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
221-435 3.77e-09

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 56.42  E-value: 3.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 221 IALVGAGPGDVGLLTLRGLQVMQQADVVLYdhlvSGEILDLVR--RDAERICVGKragahsVIQEETNRLlvELAQQGKR 298
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVVG----SKRVLELFPelIDGEAFVLTA------GLRDLLEWL--ELAAKGKN 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 299 VVRLKGGDPFIFGRGGEELqVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHrdhaqsVTFITGHCR-PDGDGLDWAdLAR 377
Cdd:PRK05787  70 VVVLSTGDPLFSGLGKLLK-VRRAVAEDVEVIPGISSVQYAAARLGIDMND------VVFTTSHGRgPNFEELEDL-LKN 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 518284900 378 ARQTLAIYMGTMKAADISQRLIAHGrDAATPVAVISRGTRADQQVQIGTLDQLEHLAQ 435
Cdd:PRK05787 142 GRKVIMLPDPRFGPKEIAAELLERG-KLERRIVVGENLSYPDERIHKLTLSEIEPLEF 198
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
 219-429 1.94e-08

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 55.17  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 219 GEIALVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSGEILDLVrrDAERICVGKragahsvIQEETNR--LLVELAQQG 296
Cdd:PRK05765   2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISDLL--DGKEVIGAR-------MKEEIFRanTAIEKALEG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 297 KRVVRLKGGDPFIFGRGGEELQVAAAAGIP--FQVVPGVTAAAGATAYAGIPLThRDHAqsVTFITGHCRPDGDGLDWAD 374
Cdd:PRK05765  73 NIVALVSSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGSPLS-LDFV--VISLSDLLIPREEILHRVT 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 375 -LARARQTLAIY----MGTMKAAdisQRLIAHGRDAATPVAVISRGTRADQQVQIGTLDQ 429
Cdd:PRK05765 150 kAAEADFVIVFYnpinENLLIEV---MDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSS 206
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
224-333 1.42e-07

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 52.23  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 224 VGAGPGDVGLLTLRGLQVMQQADVVL--YDHLVSGEI-LDLVRR---DAERICV-----GKRAGAHSVIQEETNRLLVEL 292
Cdd:PRK05576   7 IGLGPGDPELLTVKAARILEEADVVYapASRKGGGSLaLNIVRPylkEETEIVElhfpmSKDEEEKEAVWKENAEEIAAE 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 518284900 293 AQQGKRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQVVPGV 333
Cdd:PRK05576  87 AEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGI 127
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 223-333 4.14e-07

diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells.


Pssm-ID: 381174  Cd Length: 241  Bit Score: 50.88  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 223 LVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSgEILDLVRRDAERIcVGKRagahsVIQ------EETNRLLVELAQQg 296
Cdd:cd11647    4 LIGLGLGDEKDITLEGLEALKKADKVYLEAYTS-ILPGSKLEELEKL-IGKK-----IILldredlEEESEEILEEAKK- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 518284900 297 KRVVRLKGGDPFI----FgrggeELQV-AAAAGIPFQVVPGV 333
Cdd:cd11647   76 KDVALLVPGDPLIatthI-----DLRLeAKKRGIKVKVIHNA 112
PRK05562 PRK05562
NAD(P)-dependent oxidoreductase;
15-147 1.31e-05

NAD(P)-dependent oxidoreductase;


Pssm-ID: 235504  Cd Length: 223  Bit Score: 46.18  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900  15 VLVVGGGDVAARKVDLLQRAGAEIRIVAQSLSPELEQQRQLGRVLWLGESFDPQQLDDVFLAIAATDDNALNAAVFAEAD 94
Cdd:PRK05562  28 VLIIGGGKAAFIKGKTFLKKGCYVYILSKKFSKEFLDLKKYGNLKLIKGNYDKEFIKDKHLIVIATDDEKLNNKIRKHCD 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518284900  95 KRRVLANVVDDQPRCSFIFPSIIDRSPLVVAVSSSGQAPVLARLLREKLEALL 147
Cdd:PRK05562 108 RLYKLYIDCSDYKKGLCIIPYQRSTKNFVFALNTKGGSPKTSVFIGEKVKNFL 160
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 221-432 1.70e-05

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: 45.52  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 221 IALVGAGPGDVGLLTLRGLQVMQQADVVlydhlVSGE-ILDLVR-RDAERIcvgkragahsVIQEETNRLLVELAQ--QG 296
Cdd:COG2241    4 LTVVGIGPGGPDGLTPAAREAIAEADVV-----VGGKrHLELFPdLGAERI----------VWPSPLSELLEELLAllRG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 297 KRVVRLKGGDPFIFGRGG--------EELQV----------AAAAGIPFqvvpgvtaaagatayagiplthrdhaQSVTF 358
Cdd:COG2241   69 RRVVVLASGDPLFYGIGAtlarhlpaEEVRVipgisslqlaAARLGWPW--------------------------QDAAV 122

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518284900 359 ITGHCRPDGDGLDWadLARARQTLAIYMGTMKAADISQRLIAHGRDAATpVAVISRGTRADQQVQIGTLDQLEH 432
Cdd:COG2241  123 VSLHGRPLERLLPA--LAPGRRVLVLTDDGNTPAAIARLLLERGFGDSR-LTVLENLGGPDERITRGTAEELAD 193
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
221-349 2.38e-05

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 45.64  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 221 IALVGAGPGDVGLLTLRGLQVMQQADVVL----YDHLVSGeildlVRRDAERICVGkragahsvIQEETNRLL--VELAQ 294
Cdd:PRK15478   2 LSVIGIGPGSQAMMTMEAIEALQAAEIVVgyktYTHLVKA-----FTGDKQVIKTG--------MCKEIERCQaaIELAQ 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518284900 295 QGKRVVRLKGGDPFIFGRGGEELQVAAAAGIPFQV--VPGVTAAAGATAYAGIPLTH 349
Cdd:PRK15478  69 AGHNVALISSGDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLGAPLMH 125
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
 217-412 3.17e-05

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 45.36  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 217 AQGEIALVGAGPGDVGLLTLRGLQVMQQADVVLY---------------DHLVSGEI-LDLV-----RRDAERICVgkra 275
Cdd:PRK05990   1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYfvakgkkgnafgiveAHLSPGQTlLPLVypvttEILPPPLCY---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 276 gaHSVIQ---EETNRLLVELAQQGKRVVRLKGGDPFIFGrGGEELQVAAAAGIPFQVVPGVTAAAGATAYAGIPLTHRDh 352
Cdd:PRK05990  77 --ETVIAdfyDTSAEAVAAHLDAGRDVAVICEGDPFFYG-SYMYLHDRLAPRYETEVIPGVCSMLGCWSVLGAPLVYRN- 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 353 aqsvtfitghcrpdgdgldwadlararQTLAIYMGTMKAADISQRLiahgrdAATPVAVI 412
Cdd:PRK05990 153 ---------------------------QSLSVLSGVLPEEELRRRL------ADADAAVI 179
Sirohm_synth_M pfam14824
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme ...
 122-146 5.86e-04

Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme which catalyzes the biosynthesis of sirohaem. Both of the catalytic activities of this enzyme (precorrin-2 dehydrogenase EC:1.3.1.76) and sirohydrochlorin ferrochelatase (EC:4.99.1.4) are located in the N-terminal domain of this enzyme, pfam13241.


Pssm-ID: 464336 [Multi-domain]  Cd Length: 25  Bit Score: 36.98  E-value: 5.86e-04
                          10        20
                  ....*....|....*....|....*
gi 518284900  122 LVVAVSSSGQAPVLARLLREKLEAL 146
Cdd:pfam14824   1 LQIAISTNGKSPRLAALIRREIERS 25
PTZ00175 PTZ00175
diphthine synthase; Provisional
 223-330 1.31e-03

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 40.71  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518284900 223 LVGAGPGDVGLLTLRGLQVMQQADVVLYDHLVSgeILDLVRRDAERICVGKRagahsVIQ------EETNRLLVELAQQg 296
Cdd:PTZ00175   5 IIGLGLGDEKDITVKGLEAVKSADVVYLESYTS--ILINSNKEKLEEFYGKP-----VIEadremvEEGCDEILEEAKE- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 518284900 297 KRVVRLKGGDPF-------IFGRggeelqvAAAAGIPFQVV 330
Cdd:PTZ00175  77 KNVAFLVVGDPFcatthtdLYLR-------AKKKGIEVEVI 110
 
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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