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Conserved domains on  [gi|489531269|ref|WP_003436001|]
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MULTISPECIES: siroheme synthase CysG [Pseudomonas]

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;
1-457 0e+00

siroheme synthase CysG;


The actual alignment was detected with superfamily member PRK10637:

Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 544.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269   1 MEFLPLFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGGEMILRGYSECDLDGCVLIIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  81 DDEPLNAQVSRDARLRCVPVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIPSSYGQLAGLAAR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 161 FRNQVKGLFPNVQQRRAFWEDVFQGAIADRQLAGQGAEAERMLIAKIAGEPPSETGEVYLVGAGPGDPDLLTFRALRLMQ 240
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 241 QADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAH 320
Cdd:PRK10637 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 321 GIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGtTDLPWSDLVAPAQTLVFYMGLIGLPVICEQLIRHGR 400
Cdd:PRK10637 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG-GELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGM 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489531269 401 SADTPAALVEQGTTVNQRVFTGTLANLPQLVAEhdVHAPTLVIIGEVVKLREKLAWF 457
Cdd:PRK10637 400 PADMPVALVENGTSVTQRVVSGTLTQLGELAQQ--VNSPSLIIVGRVVGLRDKLNWF 454
 
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: 544.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269   1 MEFLPLFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGGEMILRGYSECDLDGCVLIIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  81 DDEPLNAQVSRDARLRCVPVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIPSSYGQLAGLAAR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 161 FRNQVKGLFPNVQQRRAFWEDVFQGAIADRQLAGQGAEAERMLIAKIAGEPPSETGEVYLVGAGPGDPDLLTFRALRLMQ 240
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 241 QADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAH 320
Cdd:PRK10637 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 321 GIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGtTDLPWSDLVAPAQTLVFYMGLIGLPVICEQLIRHGR 400
Cdd:PRK10637 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG-GELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGM 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489531269 401 SADTPAALVEQGTTVNQRVFTGTLANLPQLVAEhdVHAPTLVIIGEVVKLREKLAWF 457
Cdd:PRK10637 400 PADMPVALVENGTSVTQRVVSGTLTQLGELAQQ--VNSPSLIIVGRVVGLRDKLNWF 454
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 215-458 1.51e-156

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: 443.36  E-value: 1.51e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGK 294
Cdd:COG0007    1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 295 RVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTTDLPWSDLVA 374
Cdd:COG0007   81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 375 PAQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVKLREKL 454
Cdd:COG0007  161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALREKL 240


                 ....
gi 489531269 455 AWFE 458
Cdd:COG0007  241 SWFE 244
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 221-448 8.94e-133

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: 382.17  E-value: 8.94e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 221 VGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVVRLK 300
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 301 GGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTTDLPWSDLVAPAQTLV 380
Cdd:cd11642   81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489531269 381 FYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVV 448
Cdd:cd11642  161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 218-451 5.01e-121

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: 352.68  E-value: 5.01e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  218 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVV 297
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  298 RLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGT-TDLPWSDLVAPA 376
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKaLEVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489531269  377 QTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVKLR 451
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 218-428 1.43e-56

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: 186.39  E-value: 1.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  218 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVV 297
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  298 RLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTTDlpWSDLVAPAQ 377
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRL--LEALLANGD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489531269  378 TLVFYMGLIGLPVICEQLIRHGRsADTPAALVEQGTTVNQRVFTGTLANLP 428
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYP-DTTPVAVVERAGTPDEKVVRGTLGELA 209
 
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: 544.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269   1 MEFLPLFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGGEMILRGYSECDLDGCVLIIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  81 DDEPLNAQVSRDARLRCVPVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIPSSYGQLAGLAAR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 161 FRNQVKGLFPNVQQRRAFWEDVFQGAIADRQLAGQGAEAERMLIAKIAGEPPSETGEVYLVGAGPGDPDLLTFRALRLMQ 240
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 241 QADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAH 320
Cdd:PRK10637 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 321 GIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGtTDLPWSDLVAPAQTLVFYMGLIGLPVICEQLIRHGR 400
Cdd:PRK10637 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG-GELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGM 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489531269 401 SADTPAALVEQGTTVNQRVFTGTLANLPQLVAEhdVHAPTLVIIGEVVKLREKLAWF 457
Cdd:PRK10637 400 PADMPVALVENGTSVTQRVVSGTLTQLGELAQQ--VNSPSLIIVGRVVGLRDKLNWF 454
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 215-458 1.51e-156

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: 443.36  E-value: 1.51e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGK 294
Cdd:COG0007    1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 295 RVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTTDLPWSDLVA 374
Cdd:COG0007   81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALAR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 375 PAQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVKLREKL 454
Cdd:COG0007  161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALREKL 240


                 ....
gi 489531269 455 AWFE 458
Cdd:COG0007  241 SWFE 244
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 221-448 8.94e-133

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: 382.17  E-value: 8.94e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 221 VGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVVRLK 300
Cdd:cd11642    1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 301 GGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTTDLPWSDLVAPAQTLV 380
Cdd:cd11642   81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489531269 381 FYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVV 448
Cdd:cd11642  161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
215-460 2.66e-127

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 369.16  E-value: 2.66e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGK 294
Cdd:PRK06136   2 MGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKGK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 295 RVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTT--DLPWSDL 372
Cdd:PRK06136  82 VVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLepEVNWSAL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 373 VAPAQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVKLRE 452
Cdd:PRK06136 162 ADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALRA 241


                 ....*...
gi 489531269 453 KLAWFEGA 460
Cdd:PRK06136 242 KLAWFEAQ 249
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 218-451 5.01e-121

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: 352.68  E-value: 5.01e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  218 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVV 297
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  298 RLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGT-TDLPWSDLVAPA 376
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKaLEVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489531269  377 QTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVKLR 451
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
 207-456 6.73e-114

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 335.83  E-value: 6.73e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 207 IAGEPPS--ETGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQ 284
Cdd:PLN02625   4 IASQLPEleGPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 285 QLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGT 364
Cdd:PLN02625  84 LLLSFAEAGKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 365 TD--LPWSDLVAPAQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLV 442
Cdd:PLN02625 164 TDplDVAEAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVI 243

                        250
                 ....*....|....
gi 489531269 443 IIGEVVKLREKLAW 456
Cdd:PLN02625 244 VVGEVVALSPLWPW 257
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 1-210 1.27e-91

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: 276.65  E-value: 1.27e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269   1 MEFLPLFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGGEMILRGYSECDLDGCVLIIAAT 80
Cdd:COG1648    1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  81 DDEPLNAQVSRDARLRCVPVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIPSSYGQLAGLAAR 160
Cdd:COG1648   81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489531269 161 FRNQVKGLFPNVQQRRAFWEDVFQGAIADRQLAGQGAEAERMLIAKIAGE 210
Cdd:COG1648  161 LRERVKARLPDGAERRRFWERLLDGPLAELLRAGDEEEAEALLEELLAEA 210
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
216-458 4.50e-87

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 274.18  E-value: 4.50e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 216 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKR 295
Cdd:PRK07168   3 GYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEGKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 296 VVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTTDLPWSDLVAP 375
Cdd:PRK07168  83 VVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAKGPLTDHGKYNSSHN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 376 AQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVKLREKLA 455
Cdd:PRK07168 163 SDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGDVVSLRNQIA 242


                 ...
gi 489531269 456 WFE 458
Cdd:PRK07168 243 WKE 245
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 4-208 8.03e-87

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: 264.27  E-value: 8.03e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269    4 LPLFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGGEMILRGYSECDLDGCVLIIAATDDE 83
Cdd:TIGR01470   1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269   84 PLNAQVSRDARLRCVPVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIPSSYGQLAGLAARFRN 163
Cdd:TIGR01470  81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 489531269  164 QVKGLFPNVQQRRAFWEDVFQGAIADRQLAGQGAEAERMLIAKIA 208
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFDGAFAERVLAGREEQAERVLATRLA 205
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 218-428 1.43e-56

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: 186.39  E-value: 1.43e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  218 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRRAEHAVPQEQINQQLVALAKQGKRVV 297
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  298 RLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNGTTDlpWSDLVAPAQ 377
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRL--LEALLANGD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489531269  378 TLVFYMGLIGLPVICEQLIRHGRsADTPAALVEQGTTVNQRVFTGTLANLP 428
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYP-DTTPVAVVERAGTPDEKVVRGTLGELA 209
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 221-449 2.31e-54

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: 181.05  E-value: 2.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 221 VGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPTILDLCRRDAERVyvgkrrAEHAVPQEQINQQLVALAKQGKRVVRL 299
Cdd:cd11641    1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV------DSAGMTLEEIIEVMREAAREGKDVVRL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 300 KGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVrFITGhlKNGTTDLP----WSDLVAP 375
Cdd:cd11641   75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTV-ILTR--LEGRTPVPegesLRELAKH 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489531269 376 AQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVK 449
Cdd:cd11641  152 GATLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
 214-448 3.04e-53

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: 179.10  E-value: 3.04e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 214 ETGEVYLVGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPTILDLCRRDAERVyvgkrrAEHAVPQEQINQQLVALAKQ 292
Cdd:COG2875    1 MKGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIV------DSASMTLEEIIALMKEAAAE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 293 GKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHlknGTTDLP---- 368
Cdd:COG2875   75 GKDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAE---GRTPMPeges 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 369 WSDLVAPAQTLVFYMGLIGLPVICEQLIRHgRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVV 448
Cdd:COG2875  152 LASLAAHGATLAIYLSAHRIDEVVEELLEG-YPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPAL 230
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
 218-452 5.95e-48

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: 165.19  E-value: 5.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  218 VYLVGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPTILDLCRRDAERVyvgkrrAEHAVPQEQINQQLVALAKQGKRV 296
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAEVV------NSAGMSLEEIVDIMSDAHREGKDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  297 VRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGhlkNGTTDLP----WSDL 372
Cdd:TIGR01465  75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRA---SGRTPMPegekLADL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  373 VAPAQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIGEVVKLRE 452
Cdd:TIGR01465 152 AKHGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRI 231
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
214-445 8.76e-38

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 138.35  E-value: 8.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 214 ETGEVYLVGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPTILDLCRRDAERvyvgkrRAEHAVPQEQINQQLVALAKQ 292
Cdd:PRK15473   6 DPRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAEC------HDSAELHLEQIIDLMEAGVKA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 293 GKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVrfITGHLKNGTTDLPWSDL 372
Cdd:PRK15473  80 GKTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSL--IITRMEGRTPVPAREQL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489531269 373 VAPAQ---TLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHDVHAPTLVIIG 445
Cdd:PRK15473 158 ESFAShqtSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVG 233
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
 218-445 4.78e-35

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: 130.75  E-value: 4.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 218 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDR---------------LVAPTIL--DLCRRDAERVYVGKRRAEHAVPQE 280
Cdd:cd11724    2 LYLVGVGPGDPDLITLRALKAIKKADVVFAPPdlrkrfaeylagkevLDDPHGLftYYGKKCSPLEEAEKECEELEKQRA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 281 QINQQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAahGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVrFITGHL 360
Cdd:cd11724   82 EIVQKIREALAQGKNVALLDSGDPTIYGPWIWYLEEFA--DLNPEVIPGVSSFNAANAALKRSLTGGGDSRSV-ILTAPF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 361 KNGTTDLPWSDLVAPAQTLVFYMGLIGLPVICEQLIRHgRSADTPAALVEQ-GTTVNQRVFTGTLANLPQLVAEHDVHAP 439
Cdd:cd11724  159 ALKENEDLLEDLAATGDTLVIFMMRLDLDELVEKLKKH-YPPDTPVAIVYHaGYSEKEKVIRGTLDDILEKLGGEKEPFL 237


                 ....*.
gi 489531269 440 TLVIIG 445
Cdd:cd11724  238 GLIYVG 243
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 221-445 1.55e-34

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: 128.66  E-value: 1.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 221 VGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPT----ILDLCRRDAERVYVGKRRaehavPQEQINQQLVALAKQGKRV 296
Cdd:cd09815    1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLlslvLRAILKDGKRIYDLHDPN-----VEEEMAELLLEEARQGKDV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 297 VRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLthrdhAQSVRFITGH-LKNGTTDLPWSDLVAP 375
Cdd:cd09815   76 AFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASdLLENPRLLVLKALAKE 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 376 AQTLVFYMGLIGLPVICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHdVHAPTLVIIG 445
Cdd:cd09815  151 RRHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAERTER-GKPLTTILVG 219
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 6-115 3.48e-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: 121.04  E-value: 3.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269    6 LFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGgemilRGYSEcDLDGCVLIIAATDDEPL 85
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEITPFLEGLLDLIR-----REFEG-DLDGADLVIAATDDPEL 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 489531269   86 NAQVSRDARLRCVPVNVVDAPALCTVIFPA 115
Cdd:pfam13241  75 NERIAALARARGILVNVADDPELCDFYFPA 104
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
 215-445 1.45e-30

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: 118.63  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVV----LYDRLVAPtildlCRRDAERVYVGKR----RAEHAVpqeqinqql 286
Cdd:COG1010    3 RGKLYVVGLGPGSAELMTPRARAALAEADVVvgygTYLDLIPP-----LLPGKEVHASGMReeveRAREAL--------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 287 vALAKQGKRVVRLKGGDPFIFGRGG---EEIEEL-AAHGIPFQVVPGITAASGCAAYAGIPLTHrDHAQ---Svrfitgh 359
Cdd:COG1010   69 -ELAAEGKTVAVVSSGDPGVYGMAGlvlEVLEEGgAWRDVEVEVVPGITAAQAAAARLGAPLGH-DFCVislS------- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 360 lkngttDL--PWSD----LVAPAQ---TLVFY----MGLI-GLPVICEQLIRHgRSADTPAALVEQGTTVNQRVFTGTLA 425
Cdd:COG1010  140 ------DLltPWEViekrLRAAAEadfVIALYnprsRKRPwQLERALEILLEH-RPPDTPVGIVRNAGRPDESVTVTTLG 212

                        250       260
                 ....*....|....*....|
gi 489531269 426 NLPqlvaEHDVHAPTLVIIG 445
Cdd:COG1010  213 ELD----PEEVDMLTTVIIG 228
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 218-445 5.79e-29

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: 113.66  E-value: 5.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 218 VYLVGAGPGDPDLLTFRALRLMQQADVV----LYDRLVAPTIldlcrRDAERVYVGKR----RAEHAVpqeqinqqlvAL 289
Cdd:cd11646    1 LYVVGIGPGSADLMTPRAREALEEADVIvgykTYLDLIEDLL-----PGKEVISSGMGeeveRAREAL----------EL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 290 AKQGKRVVRLKGGDPFIFGRGG---EEIEElAAHGIPFQVVPGITAASGCAAYAGIPLTHrDHAQ---Svrfitghlkng 363
Cdd:cd11646   66 ALEGKRVALVSSGDPGIYGMAGlvlELLDE-RWDDIEVEVVPGITAALAAAALLGAPLGH-DFAVislS----------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 364 ttDL--PWSD----LVAPAQT---LVFY----MGLIG-LPVICEQLIRHgRSADTPAALVEQGTTVNQRVFTGTLANLPq 429
Cdd:cd11646  133 --DLltPWEViekrLRAAAEAdfvIALYnprsKKRPWqLEKALEILLEH-RPPDTPVGIVRNAGREGEEVTITTLGELD- 208

                        250
                 ....*....|....*.
gi 489531269 430 lvaEHDVHAPTLVIIG 445
Cdd:cd11646  209 ---PEDVDMFTTVIIG 221
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 215-433 1.12e-27

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: 110.19  E-value: 1.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLY------DRLVAPTILDLCRRDAERVYVG---KRRAEHAVPQ-EQINQ 284
Cdd:COG2243    2 MGKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagKASLAREIVAPYLPPARIVELVfpmTTDYEALVAAwDEAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 285 QLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDhaQSVRFITGhlkngt 364
Cdd:COG2243   82 RIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLAEGD--EPLTVLPG------ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489531269 365 TDLP--WSDLVAPAQTLVFYMGLIGLPVICEQLIRHGRSADtpAALVEQGTTVNQRVFTGtLANLPQLVAE 433
Cdd:COG2243  154 TLLEeeLERALDDFDTVVIMKVGRNFPKVREALEEAGLLDR--AWYVERAGMPDERIVPG-LAEVDIEEAP 221
PRK06718 PRK06718
NAD(P)-binding protein;
3-182 7.77e-25

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 101.26  E-value: 7.77e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269   3 FLPLFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQsgGEMIL--RGYSECDLDGCVLIIAAT 80
Cdd:PRK06718   1 NMPLMIDLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVISPELTENLVKLVEE--GKIRWkqKEFEPSDIVDAFLVIAAT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  81 DDEPLNAQVSRDARLRCVpVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIPSSYGQLAGLAAR 160
Cdd:PRK06718  79 NDPRVNEQVKEDLPENAL-FNVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYE 157

                        170       180
                 ....*....|....*....|..
gi 489531269 161 FRNQVKGLFPNVQQRRAFWEDV 182
Cdd:PRK06718 158 CRQKIKELQIEKREKQILLQEV 179
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 218-445 6.51e-23

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: 96.99  E-value: 6.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  218 VYLVGAGPGDPDLLTFRALRLMQQADVV----LYDRLVAPTildlcRRDAERVYVGKR----RAEHAVpqeqinqqlvAL 289
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIvgykTYLDLIEDL-----IPGKEVVTSGMReeiaRAELAI----------EL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  290 AKQGKRVVRLKGGDPFIFGRGGEEIEELAAHG--IPFQVVPGITAASGCAAYAGIPLTHrdhaqsvRFITGHLKNGTTDL 367
Cdd:TIGR01466  66 AAEGRTVALVSSGDPGIYGMAALVFEALEKKGaeVDIEVIPGITAASAAASLLGAPLGH-------DFCVISLSDLLTPW 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  368 PW--SDLVAPAQ---TLVFYMGLI-----GLPVICEQLIRHgRSADTPAALVEQGTTVNQRVFTGTLANLpqlvAEHDVH 437
Cdd:TIGR01466 139 PEieKRLRAAAEadfVIAIYNPRSkrrpeQFRRAMEILLEH-RKPDTPVGIVRNAGREGEEVEITTLAEL----DEELID 213


                  ....*...
gi 489531269  438 APTLVIIG 445
Cdd:TIGR01466 214 MLTTVIIG 221
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 221-429 8.27e-23

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: 96.42  E-value: 8.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 221 VGAGPGDPDLLTFRALRLMQQADVVLY------DRLVAPTILDLCRRDAERVY-----VGKRRAEHAVPQEQINQQLVAL 289
Cdd:cd11645    1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggEGSAALIIAAALLIPDKEIIplefpMTKDREELEEAWDEAAEEIAEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 290 AKQGKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDhaQSVRFITGHLKNGTtdlpW 369
Cdd:cd11645   81 LKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLAILPATYDEEE----L 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 370 SDLVAPAQTLVFYMGLIGLPVICEQLIRHGRSADtpAALVEQGTTVNQRVFTGTLANLPQ 429
Cdd:cd11645  155 EKALENFDTVVLMKVGRNLEEIKELLEELGLLDK--AVYVERCGMEGERIYTDLEELKEE 212
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
 216-445 5.81e-19

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 85.99  E-value: 5.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 216 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCrrDAERVYVGKRRaehavpqEQINQQLVALAK--QG 293
Cdd:PRK05765   2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISDLL--DGKEVIGARMK-------EEIFRANTAIEKalEG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 294 KRVVRLKGGDPFIFGRGGEEIEELAAHGIP--FQVVPGITAASGCAAYAGIPLthrdhaqSVRFITGHLkngttdlpwSD 371
Cdd:PRK05765  73 NIVALVSSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGSPL-------SLDFVVISL---------SD 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 372 LVAPAQ--------------TLVFYmGLIGLPVICEQL--IRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQLVAEHD 435
Cdd:PRK05765 137 LLIPREeilhrvtkaaeadfVIVFY-NPINENLLIEVMdiVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWKEHMDEIG 215

                        250
                 ....*....|
gi 489531269 436 VHapTLVIIG 445
Cdd:PRK05765 216 MT--TTMIIG 223
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 221-444 1.69e-18

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: 83.31  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 221 VGAGPGDPDLLTFRALRLMQQADVVlydrLVAPTILDLCRRDAERVYVgkrraehaVPQEQINQQLVALAKQGKRVVRLK 300
Cdd:cd11644    1 IGIGPGGPEYLTPEAREAIEEADVV----IGAKRLLELFPDLGAEKIP--------LPSEDIAELLEEIAEAGKRVVVLA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 301 GGDPFIFGRGGEEIEELAAHgiPFQVVPGITAASGCAAYAGIPLthrdhaQSVRFITGHlknGTTDLPWSDLVAPAQTLV 380
Cdd:cd11644   69 SGDPGFYGIGKTLLRRLGGE--EVEVIPGISSVQLAAARLGLPW------EDARLVSLH---GRDLENLRRALRRGRKVF 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489531269 381 FYM-GLIGLPVICEQLIRHGRsADTPAALVEQGTTVNQRVFTGTLANLpqlvAEHDVHAPTLVII 444
Cdd:cd11644  138 VLTdGKNTPAEIARLLLERGL-GDSRVTVGENLGYPDERITEGTAEEL----AEEEFSDLNVVLI 197
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
 216-419 4.59e-18

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: 83.13  E-value: 4.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  216 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLY------DRLVAPTIL-DLCRRDAERVY-----VGKRRAEHAVPQEQIN 283
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIAVpaskkgRESLARKIVeDYLKPNDTRILelvfpMTKDRDELEKAWDEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  284 QQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFITGHLKNG 363
Cdd:TIGR01467  81 EAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEGDESLAILPATAGEAEL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 489531269  364 TTDLPWSDlvapaqTLVFYMGLIGLPVICEQLIRHGRSADtpAALVEQGTTVNQRV 419
Cdd:TIGR01467 161 EKALAEFD------TVVLMKVGRNLPQIKEALAKLGRLDA--AVVVERATMPDEKI 208
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
216-353 2.18e-17

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 81.12  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 216 GEVYLVGAGPGDPDLLTFRALRLMQQADVVlydrlVAPTILDLCRRDAERV---YV-------------GKRRAEHAVPQ 279
Cdd:PRK05576   2 GKLYGIGLGPGDPELLTVKAARILEEADVV-----YAPASRKGGGSLALNIvrpYLkeeteivelhfpmSKDEEEKEAVW 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489531269 280 EQINQQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSV 353
Cdd:PRK05576  77 KENAEEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGDESLAI 150
CysG_dimerizer pfam10414
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the ...
 152-203 1.46e-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: 73.36  E-value: 1.46e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489531269  152 GQLAGLAARFRNQVKGLFPNVQQRRAFWEDVFQGAIADRQLAGQGAEAERML 203
Cdd:pfam10414   1 GRLAALAGRFRDRVKARLPDVAARRRFWERVFDGPVAELVLAGDEDEAEALL 52
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
 215-419 3.27e-15

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 75.02  E-value: 3.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYdrLVAP--------TILDLCRRDAER---VY-VGKRRAEHAVPQEQI 282
Cdd:PRK05990   2 KGRLIGLGVGPGDPELLTLKALRLLQAAPVVAY--FVAKgkkgnafgIVEAHLSPGQTLlplVYpVTTEILPPPLCYETV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 283 --------NQQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAHgIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVR 354
Cdd:PRK05990  80 iadfydtsAEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPR-YETEVIPGVCSMLGCWSVLGAPLVYRNQSLSVL 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489531269 355 fitghlkNGTtdLPWSDL---VAPAQTLVFyMGL-IGLPVICEQLIRHGRSADtpAALVEQGTTVNQRV 419
Cdd:PRK05990 159 -------SGV--LPEEELrrrLADADAAVI-MKLgRNLDKVRRVLAALGLLDR--ALYVERATMANQRI 215
PRK06719 PRK06719
precorrin-2 dehydrogenase; Validated
 5-155 3.59e-15

precorrin-2 dehydrogenase; Validated


Pssm-ID: 180668 [Multi-domain]  Cd Length: 157  Bit Score: 72.69  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269   5 PLFHNLRGSRVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGGEmilRGYSECDLDGCVLIIAATDDEP 84
Cdd:PRK06719   6 PLMFNLHNKVVVIIGGGKIAYRKASGLKDTGAFVTVVSPEICKEMKELPYITWKQ---KTFSNDDIKDAHLIYAATNQHA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489531269  85 LNAQVSRDARlRCVPVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIPSSYGQLA 155
Cdd:PRK06719  83 VNMMVKQAAH-DFQWVNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQELTSILPKLIKKIS 152
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 218-444 3.78e-15

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: 74.03  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 218 VYLVGAGPGDPDLLTFRALRLMQQADVVL-YDRLvaptiLDLCR-RDAERVYVGkrraehaVPQEQINQQLVALAKqGKR 295
Cdd:COG2241    4 LTVVGIGPGGPDGLTPAAREAIAEADVVVgGKRH-----LELFPdLGAERIVWP-------SPLSELLEELLALLR-GRR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 296 VVRLKGGDPFIFGRGGEEIEELAAHgiPFQVVPGITAASGCAAYAGIPLthrdhaQSVRFITGHlknGTtdlPWSDL--- 372
Cdd:COG2241   71 VVVLASGDPLFYGIGATLARHLPAE--EVRVIPGISSLQLAAARLGWPW------QDAAVVSLH---GR---PLERLlpa 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489531269 373 VAPAQTLVFYM-GLIGLPVICEQLIRHGRSaDTPAALVEQGTTVNQRVFTGTLANLpqlvAEHDVHAPTLVII 444
Cdd:COG2241  137 LAPGRRVLVLTdDGNTPAAIARLLLERGFG-DSRLTVLENLGGPDERITRGTAEEL----ADADFSDLNVVAI 204
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
218-359 6.08e-14

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 70.67  E-value: 6.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 218 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPTILDLCRRDAERVYVGKRraehavpqEQINQqlVALAKQGKRVV 297
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGLR--------DLLEW--LELAAKGKNVV 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489531269 298 RLKGGDPFIFGRGGEEIEElAAHGIPFQVVPGITAASGCAAYAGIPLTHrdhaqsVRFITGH 359
Cdd:PRK05787  72 VLSTGDPLFSGLGKLLKVR-RAVAEDVEVIPGISSVQYAAARLGIDMND------VVFTTSH 126
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 220-442 2.02e-11

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: 63.10  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  220 LVGAGPGDPDLLTFRALRLMQQADVVL-YDRLV--APTILDLCRRdaervyVGKrraeHAVPQEQINQQLVALAKQgKRV 296
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVgGERHLelLAELIGEKRE------IIL----TYKDLDELLEFIAATRKE-KRV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  297 VRLKGGDPFIFGRGGEEIEELAAHGIpfQVVPGITAASGCAAYAGIPLthrdhaQSVRFITGHlknGTTDLPWS-DLVAP 375
Cdd:TIGR02467  70 VVLASGDPLFYGIGRTLAERLGKERL--EIIPGISSVQYAFARLGLPW------QDAVVISLH---GRELDELLlALLRG 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489531269  376 AQTLVFYMGLIGLP-VICEQLIRHGRSADTPAALVEQGTTVNQRVFTGTLANLPQlvAEHDVHAPTLV 442
Cdd:TIGR02467 139 HRKVAVLTDPRNGPaEIARELIELGIGGSYELTVGENLGYEDERITEGTLEEIAA--AQFDFSPLLVV 204
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
218-346 4.86e-09

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 56.81  E-value: 4.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 218 VYLVGAGPGDPDLLTFRALRLMQQADVVL----YDRLVAPTILD-------LCRrDAERVyvgkrraehavpqeqinQQL 286
Cdd:PRK15478   2 LSVIGIGPGSQAMMTMEAIEALQAAEIVVgyktYTHLVKAFTGDkqviktgMCK-EIERC-----------------QAA 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489531269 287 VALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAHGIPFQV--VPGITAASGCAAYAGIPLTH 346
Cdd:PRK15478  64 IELAQAGHNVALISSGDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLGAPLMH 125
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
215-430 8.83e-09

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 55.81  E-value: 8.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYdrlvaPTILDLCRRDAER-VYVGKRRAEHAVP--------QEQINQ- 284
Cdd:PRK05948   3 LGTLYGISVGPGDPELITLKGLRLLQSAPVVAF-----PAGLAGQPGLAEQiIAPWLSPQQIKLPlyfpyvqdEEQLEQa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 285 ------QLVALAKQGKRVVRLKGGDPFI---FGRGGEEIEELAAHgIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRF 355
Cdd:PRK05948  78 wqaaadQVWHYLEQGEDVAFACEGDVSFystFTYLAQTLQELYPQ-VAIQTIPGVCSPLAAAAALGIPLTLGSQRLAILP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489531269 356 ITGHLKNGTTDLPWSDLVAPAQTLVFYmgliglPVICEQLIRHGRSADtpAALVEQGTTVNQRVFTgTLANLPQL 430
Cdd:PRK05948 157 ALYHLEELEQALTWADVVVLMKVSSVY------PQVWQWLKARNLLEQ--ASLVERATTPEQVIYR-NLEDYPDL 222
PRK05991 PRK05991
precorrin-3B C17-methyltransferase; Provisional
 215-346 4.65e-08

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 180342 [Multi-domain]  Cd Length: 250  Bit Score: 53.98  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 215 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVL-----YDRLVAptildlcRRDAERVYVGKR----RAEHAVpqeqinqq 285
Cdd:PRK05991   2 SGRLFVIGTGPGNPEQMTPEALAAVEAATDFFgygpyLDRLPL-------RADQLRHASDNReeldRAGAAL-------- 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489531269 286 lvALAKQGKRVVRLKGGDPFIFGRGG---EEIEE--LAAHGIPFQVVPGITAASGCAAYAGIPLTH 346
Cdd:PRK05991  67 --AMAAAGANVCVVSGGDPGVFAMAAavcEAIENgpAAWRAVDLTIVPGVTAMLAVAARIGAPLGH 130
PRK05562 PRK05562
NAD(P)-dependent oxidoreductase;
14-167 4.12e-07

NAD(P)-dependent oxidoreductase;


Pssm-ID: 235504  Cd Length: 223  Bit Score: 50.80  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269  14 RVLVVGGGEIALRKSRLIADAGAVLRVVAPEVEAQLSELVVQSGGEMILRGYSECDLDGCVLIIAATDDEPLNAQVSRDA 93
Cdd:PRK05562  27 KVLIIGGGKAAFIKGKTFLKKGCYVYILSKKFSKEFLDLKKYGNLKLIKGNYDKEFIKDKHLIVIATDDEKLNNKIRKHC 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489531269  94 RLRCVPVNVVDAPALCTVIFPAIVDRSPLVIAVSSGGDAPVLARLIRAKLETWIpSSYGQLAGLAARFRNQVKG 167
Cdd:PRK05562 107 DRLYKLYIDCSDYKKGLCIIPYQRSTKNFVFALNTKGGSPKTSVFIGEKVKNFL-KKYDDFIEYVTKIRNKAKK 179
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 219-337 3.63e-06

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: 48.18  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 219 YLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPtILDLCRRDAERVYvGKR-----RAEHavpqEQINQQLVALAKQg 293
Cdd:cd11647    3 YLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSI-LPGSKLEELEKLI-GKKiilldREDL----EEESEEILEEAKK- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489531269 294 KRVVRLKGGDPFI------FgrggeeIEELAAHGIPFQVVPG---ITAASGCA 337
Cdd:cd11647   76 KDVALLVPGDPLIatthidL------RLEAKKRGIKVKVIHNasiLSAAGSTS 122
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
 218-342 5.74e-06

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


Pssm-ID: 381177  Cd Length: 218  Bit Score: 47.10  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 218 VYLVGAGPGDPDLLTFRALRLMQQADVVlYDR-LVAPTILDLCRRDA---------------ERVYvgkrraehavpqEQ 281
Cdd:cd11723    1 ITIVGLGPGDPDLLTLGALEALKSADKV-YLRtARHPVVEELKEEGIefesfddlyeeaedfEEVY------------EA 67

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489531269 282 INQQLVALAKQGKrVVRLKGGDPFIFGRGGEEIEELAAHGIPFQVVPGITAASGCAAYAGI 342
Cdd:cd11723   68 IAERLLEAAEHGD-VVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSFLDAALAALGI 127
Precorrin-6A-synthase cd11643
Precorrin-6A synthase (also named CobF); Precorrin-6A synthase participates in the pathway ...
 220-345 1.27e-04

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


Pssm-ID: 381170  Cd Length: 244  Bit Score: 43.25  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 220 LVGAGPGDPDLLTFRALRLMQQADVVLY-------DRLVAPtILDLCRR-------------DAER-----VYVGKRRAE 274
Cdd:cd11643    1 LIGIGPGDPDHLTLQAIEALNRVDVFFVldkgeekSDLAAL-RREICERhlgdrpyrvvefpDPERdrspaDYRAAVADW 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489531269 275 HAVPQEQINQQLVALAKQGKRVVRLKGGDPFIFGRGGEEIEELAAHGIPF--QVVPGITAASGCAAYAGIPLT 345
Cdd:cd11643   80 HDARAALWEDAIAEELPEGGTGAFLVWGDPSLYDSTLRILDRLRAGRVALevEVIPGISSVQALAARHRIPLN 152
OphMA_like cd19916
tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin ...
 216-332 1.29e-04

tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin methyltransferase (OphMA) and Dendrothele bispora dbOphMA; OphMA, is the precursor protein of the fungal cyclic peptide Omphalotin A. Omphalotin A is a potent nematicide, having 9 out of 12 of its residues methylated at the backbone amide. Omphalotin A derives from the C-terminus of OphMA (also known as OphA). OphMA catalyzes the automethylation of its own C-terminus using S-adenosyl methionine (SAM); this C terminus is subsequently released and macrocyclized by the protease OphP to give Omphalotin A.


Pssm-ID: 381179  Cd Length: 237  Bit Score: 43.24  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 216 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLY---DRLVAPTILDLCrRDAERVYV----GKRRAEhavPQEQINQQLVA 288
Cdd:cd19916    1 GSLVVVGTGIKGIGHLTLEAESAIEQADKVFYlvaDPLTEEWLRELN-PNAEDLYDlygeGKPRLD---TYREMAERILE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489531269 289 LAKQGKRVVRLKGGDPFIFGRGGEE-IEELAAHGIPFQVVPGITA 332
Cdd:cd19916   77 AVRAGKPVCAAFYGHPGVFVSPSHLaIRIARREGYRARMLPGISA 121
PTZ00175 PTZ00175
diphthine synthase; Provisional
 219-305 1.61e-04

diphthine synthase; Provisional


Pssm-ID: 185500  Cd Length: 270  Bit Score: 43.41  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489531269 219 YLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAptILDLCRRDAERVYVGKRRAE---HAVpqEQINQQLVALAKQgKR 295
Cdd:PTZ00175   4 YIIGLGLGDEKDITVKGLEAVKSADVVYLESYTS--ILINSNKEKLEEFYGKPVIEadrEMV--EEGCDEILEEAKE-KN 78

                         90
                 ....*....|
gi 489531269 296 VVRLKGGDPF 305
Cdd:PTZ00175  79 VAFLVVGDPF 88
Sirohm_synth_M pfam14824
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme ...
 122-144 3.40e-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: 37.75  E-value: 3.40e-04
                          10        20
                  ....*....|....*....|...
gi 489531269  122 LVIAVSSGGDAPVLARLIRAKLE 144
Cdd:pfam14824   1 LQIAISTNGKSPRLAALIRREIE 23
 
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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