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Conserved domains on  [gi|489958334|ref|WP_003861641|]
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MULTISPECIES: siroheme synthase CysG [Enterobacter]

Protein Classification

siroheme synthase( domain architecture ID 11484834)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cysG PRK10637
siroheme synthase CysG;
1-457 0e+00

siroheme synthase CysG;


:

Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 967.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334   1 MDHLPIFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVNALTFAPQFDVWAQEGMLTQVQGEFDESLLDTCWLTIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  81 DNDDVNQRVSDACEARRIFCNVVDAPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLPQHLGQIAQYAGQ 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 161 LRSRVKQTFATVGERRRFWEKFFVNDRLAQSLANQDAKAVEETTEQLLSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 241 QADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320
Cdd:PRK10637 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGSELDWHNLAAEKQTLVFYMGLNQAATIQAKLLEHGME 400
Cdd:PRK10637 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMP 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489958334 401 ADMPVALVENGTAITQHVVDGVLTQLGELAQQVQSPALIVVGRVVELREKLNWFSNH 457
Cdd:PRK10637 401 ADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH 457
 
Name Accession Description Interval E-value
cysG PRK10637
siroheme synthase CysG;
1-457 0e+00

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 967.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334   1 MDHLPIFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVNALTFAPQFDVWAQEGMLTQVQGEFDESLLDTCWLTIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  81 DNDDVNQRVSDACEARRIFCNVVDAPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLPQHLGQIAQYAGQ 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 161 LRSRVKQTFATVGERRRFWEKFFVNDRLAQSLANQDAKAVEETTEQLLSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 241 QADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320
Cdd:PRK10637 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGSELDWHNLAAEKQTLVFYMGLNQAATIQAKLLEHGME 400
Cdd:PRK10637 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMP 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489958334 401 ADMPVALVENGTAITQHVVDGVLTQLGELAQQVQSPALIVVGRVVELREKLNWFSNH 457
Cdd:PRK10637 401 ADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH 457
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 215-456 1.38e-141

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: 405.23  E-value: 1.38e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGK 294
Cdd:COG0007    1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 295 RVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGS-ELDWHNLAA 373
Cdd:COG0007   81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKlDLDWAALAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 374 EKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQ--QVQSPALIVVGRVVELREKL 451
Cdd:COG0007  161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAeaGLKSPALIVVGEVVALREKL 240


                 ....*
gi 489958334 452 NWFSN 456
Cdd:COG0007  241 SWFEA 245
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 221-445 1.10e-123

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: 359.06  E-value: 1.10e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 221 VGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLK 300
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 301 GGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGSELDW-HNLAAEKQTLV 379
Cdd:cd11642   81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDdAALARPGGTLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958334 380 FYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQQ--VQSPALIVVGRVV 445
Cdd:cd11642  161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEagIRSPALIVVGEVV 228
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 218-448 7.56e-112

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: 329.19  E-value: 7.56e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  218 VVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVV 297
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  298 RLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG--SELDWHNLAAEK 375
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDkaLEVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958334  376 QTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELA--QQVQSPALIVVGRVVELR 448
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAaeANLKSPALIVIGEVVALR 236
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 218-426 5.05e-49

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: 166.36  E-value: 5.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  218 VVLVGAGPGDAGLLTLKGLQQIQQADIVVYDR-LVSDDIMNLVRRDADRVFvGKRAGYHCVPQEEINQILLREAQKGKRV 296
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDsRALEILLDLLPEDLYFPM-TEDKEPLEEAYEEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  297 VRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVrLVTGHLKTGSELDWHNLAAEKQ 376
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSV-LFLPGLARIELRLLEALLANGD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489958334  377 TLVFYMGLNQAATIQAKLLEHGMEaDMPVALVENGTAITQHVVDGVLTQL 426
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYPD-TTPVAVVERAGTPDEKVVRGTLGEL 208
 
Name Accession Description Interval E-value
cysG PRK10637
siroheme synthase CysG;
1-457 0e+00

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 967.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334   1 MDHLPIFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVNALTFAPQFDVWAQEGMLTQVQGEFDESLLDTCWLTIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  81 DNDDVNQRVSDACEARRIFCNVVDAPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLPQHLGQIAQYAGQ 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 161 LRSRVKQTFATVGERRRFWEKFFVNDRLAQSLANQDAKAVEETTEQLLSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 241 QADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320
Cdd:PRK10637 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGSELDWHNLAAEKQTLVFYMGLNQAATIQAKLLEHGME 400
Cdd:PRK10637 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMP 400

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489958334 401 ADMPVALVENGTAITQHVVDGVLTQLGELAQQVQSPALIVVGRVVELREKLNWFSNH 457
Cdd:PRK10637 401 ADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH 457
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 215-456 1.38e-141

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: 405.23  E-value: 1.38e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGK 294
Cdd:COG0007    1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 295 RVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGS-ELDWHNLAA 373
Cdd:COG0007   81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKlDLDWAALAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 374 EKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQ--QVQSPALIVVGRVVELREKL 451
Cdd:COG0007  161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAeaGLKSPALIVVGEVVALREKL 240


                 ....*
gi 489958334 452 NWFSN 456
Cdd:COG0007  241 SWFEA 245
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 221-445 1.10e-123

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: 359.06  E-value: 1.10e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 221 VGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLK 300
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 301 GGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGSELDW-HNLAAEKQTLV 379
Cdd:cd11642   81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDdAALARPGGTLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489958334 380 FYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQQ--VQSPALIVVGRVV 445
Cdd:cd11642  161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEagIRSPALIVVGEVV 228
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
216-454 1.71e-120

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 351.44  E-value: 1.71e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKR 295
Cdd:PRK06136   3 GKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKGKV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 296 VVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGS---ELDWHNLA 372
Cdd:PRK06136  83 VVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKlepEVNWSALA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 373 AEKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQQ--VQSPALIVVGRVVELREK 450
Cdd:PRK06136 163 DGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAedIQSPAIIVIGEVVALRAK 242


                 ....
gi 489958334 451 LNWF 454
Cdd:PRK06136 243 LAWF 246
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 218-448 7.56e-112

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: 329.19  E-value: 7.56e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  218 VVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVV 297
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  298 RLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG--SELDWHNLAAEK 375
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDkaLEVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958334  376 QTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELA--QQVQSPALIVVGRVVELR 448
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAaeANLKSPALIVIGEVVALR 236
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
 212-457 2.54e-97

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 293.08  E-value: 2.54e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 212 LDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQ 291
Cdd:PLN02625  11 LEGPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSFAE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 292 KGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGSE---LDW 368
Cdd:PLN02625  91 AGKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTdplDVA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 369 HNLAAEKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQQ--VQSPALIVVGRVVE 446
Cdd:PLN02625 171 EAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAagLVSPTVIVVGEVVA 250

                        250
                 ....*....|.
gi 489958334 447 LREKLNWFSNH 457
Cdd:PLN02625 251 LSPLWPWAAEE 261
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 1-212 8.48e-93

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: 279.34  E-value: 8.48e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334   1 MDHLPIFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVNALTFAPQFDVWAQEGMLTQVQGEFDESLLDTCWLTIAAT 80
Cdd:COG1648    1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  81 DNDDVNQRVSDACEARRIFCNVVDAPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLPQHLGQIAQYAGQ 160
Cdd:COG1648   81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489958334 161 LRSRVKQTFATVGERRRFWEKFFvNDRLAQSLANQDAKAVEETTEQLLSEPL 212
Cdd:COG1648  161 LRERVKARLPDGAERRRFWERLL-DGPLAELLRAGDEEEAEALLEELLAEAA 211
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
216-453 1.75e-71

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 233.73  E-value: 1.75e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKR 295
Cdd:PRK07168   3 GYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEGKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 296 VVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKtGSELDW--HNLAA 373
Cdd:PRK07168  83 VVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAK-GPLTDHgkYNSSH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 374 EKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELA--QQVQSPALIVVGRVVELREKL 451
Cdd:PRK07168 162 NSDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVknENISNPSMTIVGDVVSLRNQI 241


                 ..
gi 489958334 452 NW 453
Cdd:PRK07168 242 AW 243
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 4-208 6.62e-67

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: 213.03  E-value: 6.62e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334    4 LPIFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVNALTFAPQFDVWAQEGMLTQVQGEFDESLLDTCWLTIAATDND 83
Cdd:TIGR01470   1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334   84 DVNQRVSDACEARRIFCNVVDAPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLPQHLGQIAQYAGQLRS 163
Cdd:TIGR01470  81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 489958334  164 RVKQTFATVGERRRFWEKFFVNDRLAQSLANQDAKAVEETTEQLL 208
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFDGAFAERVLAGREEQAERVLATRLA 205
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 218-426 5.05e-49

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: 166.36  E-value: 5.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  218 VVLVGAGPGDAGLLTLKGLQQIQQADIVVYDR-LVSDDIMNLVRRDADRVFvGKRAGYHCVPQEEINQILLREAQKGKRV 296
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDsRALEILLDLLPEDLYFPM-TEDKEPLEEAYEEIAEALAAALRAGKDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  297 VRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVrLVTGHLKTGSELDWHNLAAEKQ 376
Cdd:pfam00590  81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSV-LFLPGLARIELRLLEALLANGD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489958334  377 TLVFYMGLNQAATIQAKLLEHGMEaDMPVALVENGTAITQHVVDGVLTQL 426
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYPD-TTPVAVVERAGTPDEKVVRGTLGEL 208
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 221-446 2.48e-47

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: 162.56  E-value: 2.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 221 VGAGPGDAGLLTLKGLQQIQQADIVVY-DRLVSDDIMNLVRRDADRVfvgKRAGyhcVPQEEINQILLREAQKGKRVVRL 299
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV---DSAG---MTLEEIIEVMREAAREGKDVVRL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 300 KGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG---SElDWHNLAAEKQ 376
Cdd:cd11641   75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPvpeGE-SLRELAKHGA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958334 377 TLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVvdgVLTQLGELAQQVQ-----SPALIVVGRVVE 446
Cdd:cd11641  154 TLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKI---IRGTLADLAEKVKeagitRTALILVGPALG 225
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
 218-445 2.55e-42

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: 150.17  E-value: 2.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  218 VVLVGAGPGDAGLLTLKGLQQIQQADIVVY-DRLVSDDIMNLVRRDADrvfVGKRAGYHCvpqEEINQILLREAQKGKRV 296
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAE---VVNSAGMSL---EEIVDIMSDAHREGKDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  297 VRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKT----GSELdwHNLA 372
Cdd:TIGR01465  75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTpmpeGEKL--ADLA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958334  373 AEKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGEL--AQQVQSPALIVVGRVV 445
Cdd:TIGR01465 153 KHGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLvrEEGIYRTTLILVGPAL 227
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
 215-446 3.61e-42

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: 149.82  E-value: 3.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVY-DRLVSDDIMNLVRRDADRVfvgKRAGYHcvpQEEINQILLREAQKG 293
Cdd:COG2875    2 KGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIV---DSASMT---LEEIIALMKEAAAEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 294 KRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKT---GSElDWHN 370
Cdd:COG2875   76 KDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTpmpEGE-SLAS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 371 LAAEKQTLVFYMGLNQAATIQAKLLEHgMEADMPVALVENGTAITQHVVDGvltQLGELAQQVQ-----SPALIVVGRVV 445
Cdd:COG2875  155 LAAHGATLAIYLSAHRIDEVVEELLEG-YPPDTPVAVVYRASWPDEKIVRG---TLADIAEKVKeagitRTALILVGPAL 230


                 .
gi 489958334 446 E 446
Cdd:COG2875  231 G 231
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 221-442 1.68e-35

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: 130.98  E-value: 1.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 221 VGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSddimnlvRRDADRVFVGKRAGYHCVP------QEEINQILLREAQKGK 294
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDS-------KLLSLVLRAILKDGKRIYDlhdpnvEEEMAELLLEEARQGK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 295 RVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLthrdyAQSVRLVTGHLKTGSE--LDWHNLA 372
Cdd:cd09815   74 DVAFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASDLLENPrlLVLKALA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958334 373 AEKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTaITQHVVD-GVLTQLGEL-AQQVQSPALIVVG 442
Cdd:cd09815  149 KERRHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAG-SEGEVIRtGTVKELRAErTERGKPLTTILVG 219
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 6-115 5.00e-34

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


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 122.97  E-value: 5.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334    6 IFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVnaltFAPQFDvWAQEGMLTQVQGEFDESLLDTcWLTIAATDNDDV 85
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTV----VSPEIT-PFLEGLLDLIRREFEGDLDGA-DLVIAATDDPEL 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 489958334   86 NQRVSDACEARRIFCNVVDAPKEASFIMPS 115
Cdd:pfam13241  75 NERIAALARARGILVNVADDPELCDFYFPA 104
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
208-443 1.46e-29

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 116.01  E-value: 1.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 208 LSEPLDHRgEVVLVGAGPGDAGLLTLKGLQQIQQADIVVY-DRLVSDDIMNLVRRDADRvfvGKRAGYHCvpqEEINQIL 286
Cdd:PRK15473   1 MSETFDPR-CVWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAEC---HDSAELHL---EQIIDLM 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 287 LREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRL--VTGHLKTGS 364
Cdd:PRK15473  74 EAGVKAGKTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIItrMEGRTPVPA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 365 ELDWHNLAAEKQTLVFYMGLNQAATIQAKLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQQ--VQSPALIVVG 442
Cdd:PRK15473 154 REQLESFASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDagIRKTALILVG 233


                 .
gi 489958334 443 R 443
Cdd:PRK15473 234 N 234
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
 220-442 6.37e-27

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: 108.41  E-value: 6.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 220 LVGAGPGDAGLLTLKGLQQIQQADIVVY-------------DRLVSDD----IMNLVRRDADRVFVGKRAGYHCVPQEEI 282
Cdd:cd11724    4 LVGVGPGDPDLITLRALKAIKKADVVFAppdlrkrfaeylaGKEVLDDphglFTYYGKKCSPLEEAEKECEELEKQRAEI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 283 NQIlLREA-QKGKRVVRLKGGDPFIFGRGGEELETLcnAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLK 361
Cdd:cd11724   84 VQK-IREAlAQGKNVALLDSGDPTIYGPWIWYLEEF--ADLNPEVIPGVSSFNAANAALKRSLTGGGDSRSVILTAPFAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 362 TGSELDWHNLAAEKQTLVFYMGLNQAATIQAKLLEHgMEADMPVALVEN-GTAITQHVVDGVLTQLGELAQQVQSPA--L 438
Cdd:cd11724  161 KENEDLLEDLAATGDTLVIFMMRLDLDELVEKLKKH-YPPDTPVAIVYHaGYSEKEKVIRGTLDDILEKLGGEKEPFlgL 239


                 ....
gi 489958334 439 IVVG 442
Cdd:cd11724  240 IYVG 243
PRK06718 PRK06718
NAD(P)-binding protein;
5-181 6.01e-21

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 90.47  E-value: 6.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334   5 PIFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVnaltFAPQFDV----WAQEGMLTQVQGEFDESLLDTCWLTIAAT 80
Cdd:PRK06718   3 PLMIDLSNKRVVIVGGGKVAGRRAITLLKYGAHIVV----ISPELTEnlvkLVEEGKIRWKQKEFEPSDIVDAFLVIAAT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  81 DNDDVNQRVSDACEARRIFcNVVDAPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLPQHLGQIAQYAGQ 160
Cdd:PRK06718  79 NDPRVNEQVKEDLPENALF-NVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYE 157

                        170       180
                 ....*....|....*....|.
gi 489958334 161 LRSRVKQTFATVGERRRFWEK 181
Cdd:PRK06718 158 CRQKIKELQIEKREKQILLQE 178
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 216-422 4.78e-18

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: 82.84  E-value: 4.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADIVVY---------------DRLVSD-DIMNL---VRRDADRvfvgKRAGYHc 276
Cdd:COG2243    3 GKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslareivAPYLPPaRIVELvfpMTTDYEA----LVAAWD- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 277 vpqEEINQILlREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDyaQSVRLV 356
Cdd:COG2243   78 ---EAAARIA-EELEAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLAEGD--EPLTVL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958334 357 TGhlkTGSELDWHNLAAEKQTLVFyMGLNQA-ATIQAKLLEHGMEADmpVALVENGTAITQHVVDGV 422
Cdd:COG2243  152 PG---TLLEEELERALDDFDTVVI-MKVGRNfPKVREALEEAGLLDR--AWYVERAGMPDERIVPGL 212
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
 215-350 1.09e-17

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: 82.43  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADIVV----YDRLVSDDIMNLVRRD------ADRVfvgKRAgyhcvpqeeinq 284
Cdd:COG1010    3 RGKLYVVGLGPGSAELMTPRARAALAEADVVVgygtYLDLIPPLLPGKEVHAsgmreeVERA---REA------------ 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 285 ilLREAQKGKRVVRLKGGDPFIFGRGG---EELETLCNA-GIPFSVVPGITAASGCSAYSGIPLTHrDYA 350
Cdd:COG1010   68 --LELAAEGKTVAVVSSGDPGVYGMAGlvlEVLEEGGAWrDVEVEVVPGITAAQAAAARLGAPLGH-DFC 134
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 221-428 2.34e-17

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: 80.63  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 221 VGAGPGDAGLLTLKGLQQIQQADIVVY-------DRLVSDDIMNLVRRDADRVFV--------GKRAGYHcvpqEEINQI 285
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggeGSAALIIAAALLIPDKEIIPLefpmtkdrEELEEAW----DEAAEE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 286 LLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDyaQSVRLVTGhLKTGSE 365
Cdd:cd11645   77 IAEELKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLAILPA-TYDEEE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958334 366 LDwhNLAAEKQTLVFYMGLNQAATIQAKLLEHGMEADmpVALVENGTAITQHVVDGVLTQLGE 428
Cdd:cd11645  154 LE--KALENFDTVVLMKVGRNLEEIKELLEELGLLDK--AVYVERCGMEGERIYTDLEELKEE 212
PRK06719 PRK06719
precorrin-2 dehydrogenase; Validated
 5-156 2.45e-17

precorrin-2 dehydrogenase; Validated


Pssm-ID: 180668 [Multi-domain]  Cd Length: 157  Bit Score: 78.85  E-value: 2.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334   5 PIFCQLRNRDCLLVGGGDVAERKARLLLEAGARLTVnaltFAPQFDVWAQE-GMLTQVQGEFDESLLDTCWLTIAATDND 83
Cdd:PRK06719   6 PLMFNLHNKVVVIIGGGKIAYRKASGLKDTGAFVTV----VSPEICKEMKElPYITWKQKTFSNDDIKDAHLIYAATNQH 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489958334  84 DVNQRVSDACEARRiFCNVVDAPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLPQHLGQIAQ 156
Cdd:PRK06719  82 AVNMMVKQAAHDFQ-WVNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQELTSILPKLIKKISR 153
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 220-350 4.74e-17

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: 80.15  E-value: 4.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 220 LVGAGPGDAGLLTLKGLQQIQQADIVV----YDRLVSDDI---------MnlvRRDADRVfvgKRAgyhcvpqeeinqil 286
Cdd:cd11646    3 VVGIGPGSADLMTPRAREALEEADVIVgyktYLDLIEDLLpgkevissgM---GEEVERA---REA-------------- 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489958334 287 LREAQKGKRVVRLKGGDPFIFGRGGEELETLC--NAGIPFSVVPGITAASGCSAYSGIPLTHrDYA 350
Cdd:cd11646   63 LELALEGKRVALVSSGDPGIYGMAGLVLELLDerWDDIEVEVVPGITAALAAAALLGAPLGH-DFA 127
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 218-441 7.12e-15

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: 73.87  E-value: 7.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  218 VVLVGAGPGDAGLLTLKGLQQIQQADIVV----YDRLVSDdimnlVRRDADRVFVGKRagyhcvpqEEIN--QILLREAQ 291
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIVgyktYLDLIED-----LIPGKEVVTSGMR--------EEIAraELAIELAA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  292 KGKRVVRLKGGDPFIFGRGGEELETL--CNAGIPFSVVPGITAASGCSAYSGIPLTHrDYAqSVRLvTGHLKTGSELDWH 369
Cdd:TIGR01466  68 EGRTVALVSSGDPGIYGMAALVFEALekKGAEVDIEVIPGITAASAAASLLGAPLGH-DFC-VISL-SDLLTPWPEIEKR 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489958334  370 NLAAEKQTLV--FYMGLNQAATIQAK-----LLEHgMEADMPVALVENGTAITQHVvdgVLTQLGELAQQVQSPALIVV 441
Cdd:TIGR01466 145 LRAAAEADFViaIYNPRSKRRPEQFRrameiLLEH-RKPDTPVGIVRNAGREGEEV---EITTLAELDEELIDMLTTVI 219
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 221-410 1.51e-14

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: 72.14  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 221 VGAGPGDAGLLTLKGLQQIQQADIVV-YDRLVsddimNLVRRDADRVFVgkragyhcVPQEEINQILLREAQKGKRVVRL 299
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVVIgAKRLL-----ELFPDLGAEKIP--------LPSEDIAELLEEIAEAGKRVVVL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 300 KGGDPFIFGRGGEELETLcnAGIPFSVVPGITAASGCSAYSGIPLthrdyaQSVRLVTGHLKTGSELDWHnLAAEKQTLV 379
Cdd:cd11644   68 ASGDPGFYGIGKTLLRRL--GGEEVEVIPGISSVQLAAARLGLPW------EDARLVSLHGRDLENLRRA-LRRGRKVFV 138

                        170       180       190
                 ....*....|....*....|....*....|.
gi 489958334 380 FYMGLNQAATIQAKLLEHGMEaDMPVALVEN 410
Cdd:cd11644  139 LTDGKNTPAEIARLLLERGLG-DSRVTVGEN 168
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
 215-442 1.62e-14

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 72.89  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADIVV----YDRLVSDDImnlvrrDADRVFVGKRagyhcvpQEEI--NQILLR 288
Cdd:PRK05765   1 MGKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgyntYLRLISDLL------DGKEVIGARM-------KEEIfrANTAIE 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 289 EAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIP--FSVVPGITAASGCSAYSGIPLThRDYAqSVRLvtGHLKTGSEL 366
Cdd:PRK05765  68 KALEGNIVALVSSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGSPLS-LDFV-VISL--SDLLIPREE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 367 DWHNL--AAEKQ-TLVFYMGLNQAATIQA-KLLEHGMEADMPVALVENGTAITQHVVDGVLTQLGELAQQVQSPALIVVG 442
Cdd:PRK05765 144 ILHRVtkAAEADfVIVFYNPINENLLIEVmDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWKEHMDEIGMTTTMIIG 223
CysG_dimerizer pfam10414
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the ...
 152-208 3.24e-14

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: 66.81  E-value: 3.24e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489958334  152 GQIAQYAGQLRSRVKQTFATVGERRRFWEKFFvNDRLAQSLANQDAKAVEETTEQLL 208
Cdd:pfam10414   1 GRLAALAGRFRDRVKARLPDVAARRRFWERVF-DGPVAELVLAGDEDEAEALLEQAL 56
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 220-410 3.56e-14

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: 71.19  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  220 LVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKragyhcvPQEEINQiLLREAQKGKRVVRL 299
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIILTYK-------DLDELLE-FIAATRKEKRVVVL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  300 KGGDPFIFGRGGEELETLCNAGIpfSVVPGITAASGCSAYSGIPLthrdyaQSVRLVTGHLKTGSELDWHNLAAEKQTLV 379
Cdd:TIGR02467  73 ASGDPLFYGIGRTLAERLGKERL--EIIPGISSVQYAFARLGLPW------QDAVVISLHGRELDELLLALLRGHRKVAV 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 489958334  380 FYMGLNQAATIQAKLLEHGMEADMPVALVEN 410
Cdd:TIGR02467 145 LTDPRNGPAEIARELIELGIGGSYELTVGEN 175
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
 221-422 3.96e-14

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: 71.57  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  221 VGAGPGDAGLLTLKGLQQIQQADIVVYDR-----------LVSDDIMNLVRRDADRVF-VGKRAGYHCVPQEEINQILLR 288
Cdd:TIGR01467   6 VGVGPGDPELITVKALEALRSADVIAVPAskkgreslarkIVEDYLKPNDTRILELVFpMTKDRDELEKAWDEAAEAVAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  289 EAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDyaQSVRLVTGhlkTGSELDW 368
Cdd:TIGR01467  86 ELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEGD--ESLAILPA---TAGEAEL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489958334  369 HNLAAEKQTLVFYMGLNQAATIQAKLLEHGMEADmpVALVENGTAITQHVVDGV 422
Cdd:TIGR01467 161 EKALAEFDTVVLMKVGRNLPQIKEALAKLGRLDA--AVVVERATMPDEKIVDLV 212
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
216-401 1.40e-12

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 66.86  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADIVV--YDRLVSDDI-MNLVRRDAD---RVFV-----GKRAGYHCVPQEEINQ 284
Cdd:PRK05576   2 GKLYGIGLGPGDPELLTVKAARILEEADVVYapASRKGGGSLaLNIVRPYLKeetEIVElhfpmSKDEEEKEAVWKENAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 285 ILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGS 364
Cdd:PRK05576  82 EIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGDESLAIIPATREALIEQ 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489958334 365 ELDWHNlaaekqTLVFYMGLNQAATIQAKLLEHGMEA 401
Cdd:PRK05576 162 ALTDFD------SVVLMKVYKNFALIEELLEEGYLDA 192
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
218-399 1.61e-11

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 63.35  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 218 VVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRagyhcvpqEEINQilLREAQKGKRVV 297
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGLR--------DLLEW--LELAAKGKNVV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 298 RLKGGDPFIFGRGGEELEtLCNAGIPFSVVPGITAASGCSAYSGIPLTHrdyaqsVRLVTGHLKTGSELDWHNLAAEKQT 377
Cdd:PRK05787  72 VLSTGDPLFSGLGKLLKV-RRAVAEDVEVIPGISSVQYAAARLGIDMND------VVFTTSHGRGPNFEELEDLLKNGRK 144

                        170       180
                 ....*....|....*....|....*.
gi 489958334 378 LVF----YMGLNQAAtiqAKLLEHGM 399
Cdd:PRK05787 145 VIMlpdpRFGPKEIA---AELLERGK 167
PRK05562 PRK05562
NAD(P)-dependent oxidoreductase;
16-166 7.86e-10

NAD(P)-dependent oxidoreductase;


Pssm-ID: 235504  Cd Length: 223  Bit Score: 58.89  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334  16 LLVGGGDVAERKARLLLEAGARLTVNALTFAPQFDVWAQEGMLTQVQGEFDESLLDTCWLTIAATDNDDVNQRVSDACEA 95
Cdd:PRK05562  29 LIIGGGKAAFIKGKTFLKKGCYVYILSKKFSKEFLDLKKYGNLKLIKGNYDKEFIKDKHLIVIATDDEKLNNKIRKHCDR 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958334  96 R-RIFCNVVDaPKEASFIMPSIIDRSPLMIAVSSGGRSPVLARLLREKLEAVLpQHLGQIAQYAGQLRSRVK 166
Cdd:PRK05562 109 LyKLYIDCSD-YKKGLCIIPYQRSTKNFVFALNTKGGSPKTSVFIGEKVKNFL-KKYDDFIEYVTKIRNKAK 178
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
 215-353 4.06e-09

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 56.92  E-value: 4.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVY--------------DRLVSDDIMNL-----VRRDADRvfvgKRAGYH 275
Cdd:PRK05990   2 KGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYfvakgkkgnafgivEAHLSPGQTLLplvypVTTEILP----PPLCYE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 276 CVPQ---EEINQILLREAQKGKRVVRLKGGDPFIFG-------RGGEELETlcnagipfSVVPGITAASGCSAYSGIPLT 345
Cdd:PRK05990  78 TVIAdfyDTSAEAVAAHLDAGRDVAVICEGDPFFYGsymylhdRLAPRYET--------EVIPGVCSMLGCWSVLGAPLV 149


                 ....*...
gi 489958334 346 HRDYAQSV 353
Cdd:PRK05990 150 YRNQSLSV 157
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
220-346 7.63e-09

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 56.04  E-value: 7.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 220 LVGAGPGDAGLLTLKGLQQIQQADIVV----YDRLVsddimnlvrrdadRVFVGKRAGYHCVPQEEIN--QILLREAQKG 293
Cdd:PRK15478   4 VIGIGPGSQAMMTMEAIEALQAAEIVVgyktYTHLV-------------KAFTGDKQVIKTGMCKEIErcQAAIELAQAG 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489958334 294 KRVVRLKGGDPFIFGRGGEELETLCNAGIPFSV--VPGITAASGCSAYSGIPLTH 346
Cdd:PRK15478  71 HNVALISSGDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLGAPLMH 125
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 218-426 8.41e-08

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: 52.46  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 218 VVLVGAGPGDAGLLTLKGLQQIQQADIVV-YDRLVSddimnLVR-RDADRVFVGkragyhcVPQEE-INQILlrEAQKGK 294
Cdd:COG2241    4 LTVVGIGPGGPDGLTPAAREAIAEADVVVgGKRHLE-----LFPdLGAERIVWP-------SPLSElLEELL--ALLRGR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 295 RVVRLKGGDPFIFGRGGEELETLCNAgiPFSVVPGITAASGCSAYSGIPLthrdyaQSVRLVTGHLKTGSELDwHNLAAE 374
Cdd:COG2241   70 RVVVLASGDPLFYGIGATLARHLPAE--EVRVIPGISSLQLAAARLGWPW------QDAAVVSLHGRPLERLL-PALAPG 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489958334 375 KQTLVFYMGLNQAATIQAKLLEHGMEaDMPVALVENGTAITQHVVDGVLTQL 426
Cdd:COG2241  141 RRVLVLTDDGNTPAAIARLLLERGFG-DSRLTVLENLGGPDERITRGTAEEL 191
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 219-337 4.02e-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: 4.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 219 VLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVS-------DDIMNLVRRD---ADRVFVgkragyhcvpqEEINQILLR 288
Cdd:cd11647    3 YLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSilpgsklEELEKLIGKKiilLDREDL-----------EEESEEILE 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958334 289 EAQKgKRVVRLKGGDPFIfgrggeeletlcnA-------------GIPFSVVPG---ITAASGCS 337
Cdd:cd11647   72 EAKK-KDVALLVPGDPLI-------------AtthidlrleakkrGIKVKVIHNasiLSAAGSTS 122
PRK05991 PRK05991
precorrin-3B C17-methyltransferase; Provisional
 215-346 3.54e-06

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 180342 [Multi-domain]  Cd Length: 250  Bit Score: 48.20  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADIVV-----YDRLvsDDIMNLVRRDADRvfvgkragyhcvpQEEIN--QILL 287
Cdd:PRK05991   2 SGRLFVIGTGPGNPEQMTPEALAAVEAATDFFgygpyLDRL--PLRADQLRHASDN-------------REELDraGAAL 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489958334 288 REAQKGKRVVRLKGGDPFIFGRGGEELETLCNA-----GIPFSVVPGITAASGCSAYSGIPLTH 346
Cdd:PRK05991  67 AMAAAGANVCVVSGGDPGVFAMAAAVCEAIENGpaawrAVDLTIVPGVTAMLAVAARIGAPLGH 130
Sirohm_synth_M pfam14824
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme ...
 122-145 2.24e-05

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: 40.84  E-value: 2.24e-05
                          10        20
                  ....*....|....*....|....
gi 489958334  122 LMIAVSSGGRSPVLARLLREKLEA 145
Cdd:pfam14824   1 LQIAISTNGKSPRLAALIRREIER 24
PTZ00175 PTZ00175
diphthine synthase; Provisional
 220-305 7.19e-05

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 44.18  E-value: 7.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958334 220 LVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSddIMNLVRRDADRVFVGKR---AGYHCVpqEEINQILLREAqKGKRV 296
Cdd:PTZ00175   5 IIGLGLGDEKDITVKGLEAVKSADVVYLESYTS--ILINSNKEKLEEFYGKPvieADREMV--EEGCDEILEEA-KEKNV 79


                 ....*....
gi 489958334 297 VRLKGGDPF 305
Cdd:PTZ00175  80 AFLVVGDPF 88
 
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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