NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15597807|ref|NP_251301|]
View 

siroheme synthase [Pseudomonas aeruginosa PAO1]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cysG super family cl32546
siroheme synthase CysG;
1-458 0e+00

siroheme synthase CysG;


The actual alignment was detected with superfamily member PRK10637:

Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 531.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807    1 MDFLPLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCALIIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   81 DDEPLNAEVSRAANARGIPVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLAGLASR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  161 FRHRVKELLPDLQQRRVFWENLF-QGEIAERVLAGRPAEAERLLEEHLAGGLAHiaTGEVYLVGAGPGDPDLLTFRALRL 239
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAVTETTEQLFSEPLDH--RGEVVLVGAGPGDAGLLTLKGLQQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  240 MQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELA 319
Cdd:PRK10637 239 IQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLC 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  320 AHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGtTDLPWQDLVAPGQTLVFYMGLVGLPVICEQLVAH 399
Cdd:PRK10637 319 NAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG-GELDWENLAAEKQTLVFYMGLNQAATIQQKLIEH 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597807  400 GRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAehEVHAPTLVIVGEVVQLRDKLAWF 458
Cdd:PRK10637 398 GMPADMPVALVENGTSVTQRVVSGTLTQLGELAQ--QVNSPSLIIVGRVVGLRDKLNWF 454
 
Name Accession Description Interval E-value
cysG PRK10637
siroheme synthase CysG;
1-458 0e+00

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 531.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807    1 MDFLPLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCALIIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   81 DDEPLNAEVSRAANARGIPVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLAGLASR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  161 FRHRVKELLPDLQQRRVFWENLF-QGEIAERVLAGRPAEAERLLEEHLAGGLAHiaTGEVYLVGAGPGDPDLLTFRALRL 239
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAVTETTEQLFSEPLDH--RGEVVLVGAGPGDAGLLTLKGLQQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  240 MQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELA 319
Cdd:PRK10637 239 IQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLC 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  320 AHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGtTDLPWQDLVAPGQTLVFYMGLVGLPVICEQLVAH 399
Cdd:PRK10637 319 NAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG-GELDWENLAAEKQTLVFYMGLNQAATIQQKLIEH 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597807  400 GRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAehEVHAPTLVIVGEVVQLRDKLAWF 458
Cdd:PRK10637 398 GMPADMPVALVENGTSVTQRVVSGTLTQLGELAQ--QVNSPSLIIVGRVVGLRDKLNWF 454
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 216-459 4.12e-154

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: 437.20  E-value: 4.12e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 216 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGK 295
Cdd:COG0007   1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 296 RVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTTDLPWQDLVA 375
Cdd:COG0007  81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 376 PGQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLRDKL 455
Cdd:COG0007 161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALREKL 240


                ....
gi 15597807 456 AWFE 459
Cdd:COG0007 241 SWFE 244
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 222-449 2.16e-131

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: 378.70  E-value: 2.16e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 222 VGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVLRLK 301
Cdd:cd11642   1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 302 GGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTTDLPWQDLVAPGQTLV 381
Cdd:cd11642  81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597807 382 FYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVV 449
Cdd:cd11642 161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 219-452 4.63e-118

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: 345.36  E-value: 4.63e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   219 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVL 298
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   299 RLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGT-TDLPWQDLVAPG 377
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKaLEVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597807   378 QTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLR 452
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 219-429 6.91e-54

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: 179.46  E-value: 6.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   219 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVL 298
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   299 RLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGhlKDGTTDLPWQDLVAPGQ 378
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPG--LARIELRLLEALLANGD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15597807   379 TLVFYMGLVGLPVICEQLVAHGRsAQTPAALIQQGTTAQQRVFTGTLENLP 429
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYP-DTTPVAVVERAGTPDEKVVRGTLGELA 209
 
Name Accession Description Interval E-value
cysG PRK10637
siroheme synthase CysG;
1-458 0e+00

siroheme synthase CysG;


Pssm-ID: 182606 [Multi-domain]  Cd Length: 457  Bit Score: 531.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807    1 MDFLPLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCALIIAAT 80
Cdd:PRK10637   1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   81 DDEPLNAEVSRAANARGIPVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLAGLASR 160
Cdd:PRK10637  81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  161 FRHRVKELLPDLQQRRVFWENLF-QGEIAERVLAGRPAEAERLLEEHLAGGLAHiaTGEVYLVGAGPGDPDLLTFRALRL 239
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAVTETTEQLFSEPLDH--RGEVVLVGAGPGDAGLLTLKGLQQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  240 MQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELA 319
Cdd:PRK10637 239 IQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLC 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  320 AHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGtTDLPWQDLVAPGQTLVFYMGLVGLPVICEQLVAH 399
Cdd:PRK10637 319 NAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG-GELDWENLAAEKQTLVFYMGLNQAATIQQKLIEH 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597807  400 GRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAehEVHAPTLVIVGEVVQLRDKLAWF 458
Cdd:PRK10637 398 GMPADMPVALVENGTSVTQRVVSGTLTQLGELAQ--QVNSPSLIIVGRVVGLRDKLNWF 454
CysG COG0007
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ...
 216-459 4.12e-154

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: 437.20  E-value: 4.12e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 216 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGK 295
Cdd:COG0007   1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 296 RVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTTDLPWQDLVA 375
Cdd:COG0007  81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 376 PGQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLRDKL 455
Cdd:COG0007 161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALREKL 240


                ....
gi 15597807 456 AWFE 459
Cdd:COG0007 241 SWFE 244
SUMT cd11642
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ...
 222-449 2.16e-131

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: 378.70  E-value: 2.16e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 222 VGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVLRLK 301
Cdd:cd11642   1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 302 GGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTTDLPWQDLVAPGQTLV 381
Cdd:cd11642  81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597807 382 FYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVV 449
Cdd:cd11642 161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
PRK06136 PRK06136
uroporphyrinogen-III C-methyltransferase;
215-461 3.85e-124

uroporphyrinogen-III C-methyltransferase;


Pssm-ID: 235711  Cd Length: 249  Bit Score: 361.07  E-value: 3.85e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  215 ATGEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQG 294
Cdd:PRK06136   1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  295 KRVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTT--DLPWQD 372
Cdd:PRK06136  81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLepEVNWSA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  373 LVAPGQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLR 452
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALR 240


                 ....*....
gi 15597807  453 DKLAWFEGA 461
Cdd:PRK06136 241 AKLAWFEAQ 249
cobA_cysG_Cterm TIGR01469
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ...
 219-452 4.63e-118

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: 345.36  E-value: 4.63e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   219 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVL 298
Cdd:TIGR01469   2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   299 RLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGT-TDLPWQDLVAPG 377
Cdd:TIGR01469  82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKaLEVDWEALAKGA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597807   378 QTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLR 452
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
PLN02625 PLN02625
uroporphyrin-III C-methyltransferase
 217-457 4.39e-110

uroporphyrin-III C-methyltransferase


Pssm-ID: 178232 [Multi-domain]  Cd Length: 263  Bit Score: 325.82  E-value: 4.39e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  217 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKR 296
Cdd:PLN02625  15 GNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSFAEAGKT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  297 VLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTTD--LPWQDLV 374
Cdd:PLN02625  95 VVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTDplDVAEAAA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  375 APGQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLRDK 454
Cdd:PLN02625 175 DPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEVVALSPL 254


                 ...
gi 15597807  455 LAW 457
Cdd:PLN02625 255 WPW 257
cysG_Nterm TIGR01470
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ...
 4-208 1.59e-103

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: 307.02  E-value: 1.59e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807     4 LPLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCALIIAATDDE 83
Cdd:TIGR01470   1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807    84 PLNAEVSRAANARGIPVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLAGLASRFRH 163
Cdd:TIGR01470  81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15597807   164 RVKELLPDLQQRRVFWENLFQGEIAERVLAGRPAEAERLLEEHLA 208
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFDGAFAERVLAGREEQAERVLATRLA 205
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 1-211 1.65e-98

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: 294.37  E-value: 1.65e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   1 MDFLPLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCALIIAAT 80
Cdd:COG1648   1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  81 DDEPLNAEVSRAANARGIPVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLAGLASR 160
Cdd:COG1648  81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15597807 161 FRHRVKELLPDLQQRRVFWENLFQGEIAERVLAGRPAEAERLLEEHLAGGL 211
Cdd:COG1648 161 LRERVKARLPDGAERRRFWERLLDGPLAELLRAGDEEEAEALLEELLAEAA 211
PRK07168 PRK07168
uroporphyrin-III C-methyltransferase;
217-459 6.63e-84

uroporphyrin-III C-methyltransferase;


Pssm-ID: 180864 [Multi-domain]  Cd Length: 474  Bit Score: 266.09  E-value: 6.63e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  217 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKR 296
Cdd:PRK07168   3 GYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEGKI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  297 VLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDGTTDLPWQDLVAP 376
Cdd:PRK07168  83 VVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAKGPLTDHGKYNSSHN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  377 GQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVVQLRDKLA 456
Cdd:PRK07168 163 SDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGDVVSLRNQIA 242


                 ...
gi 15597807  457 WFE 459
Cdd:PRK07168 243 WKE 245
TP_methylase pfam00590
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ...
 219-429 6.91e-54

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: 179.46  E-value: 6.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   219 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRRAEHAVPQDRINRLLVELASQGKRVL 298
Cdd:pfam00590   2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDVA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   299 RLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGhlKDGTTDLPWQDLVAPGQ 378
Cdd:pfam00590  82 RLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPG--LARIELRLLEALLANGD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15597807   379 TLVFYMGLVGLPVICEQLVAHGRsAQTPAALIQQGTTAQQRVFTGTLENLP 429
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELYP-DTTPVAVVERAGTPDEKVVRGTLGELA 209
Precorrin-4_C11-MT cd11641
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ...
 222-449 2.91e-52

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: 175.66  E-value: 2.91e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 222 VGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPSILELCRRDAERLyvgkrrAEHAVPQDRINRLLVELASQGKRVLRL 300
Cdd:cd11641   1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV------DSAGMTLEEIIEVMREAAREGKDVVRL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 301 KGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGhlkDGTTDLP----WQDLVAP 376
Cdd:cd11641  75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRL---EGRTPVPegesLRELAKH 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597807 377 GQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVV 449
Cdd:cd11641 152 GATLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPAL 224
CobM COG2875
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ...
 216-449 3.02e-51

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: 174.09  E-value: 3.02e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 216 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPSILELCRRDAERlyvgkrRAEHAVPQDRINRLLVELASQG 294
Cdd:COG2875   2 KGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEI------VDSASMTLEEIIALMKEAAAEG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 295 KRVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGhlkDGTTDLP----W 370
Cdd:COG2875  76 KDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRA---EGRTPMPegesL 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597807 371 QDLVAPGQTLVFYMGLVGLPVICEQLVAHgRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVV 449
Cdd:COG2875 153 ASLAAHGATLAIYLSAHRIDEVVEELLEG-YPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPAL 230
cobM_cbiF TIGR01465
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ...
 219-449 1.21e-46

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: 161.72  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   219 VYLVGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPSILELCRRDAERLYVGKRRAEHAVPqdrinrLLVELASQGKRV 297
Cdd:TIGR01465   1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAEVVNSAGMSLEEIVD------IMSDAHREGKDV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   298 LRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGhlkDGTTDLP----WQDL 373
Cdd:TIGR01465  75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRA---SGRTPMPegekLADL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597807   374 VAPGQTLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVGEVV 449
Cdd:TIGR01465 152 AKHGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPAL 227
cbiF PRK15473
cobalt-precorrin-4 methyltransferase;
218-446 9.69e-36

cobalt-precorrin-4 methyltransferase;


Pssm-ID: 185370  Cd Length: 257  Bit Score: 132.96  E-value: 9.69e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  218 EVYLVGAGPGDPDLLTFRALRLMQQADVVLY-DRLVAPSILELCRRDAERlyvgkrRAEHAVPQDRINRLLVELASQGKR 296
Cdd:PRK15473   9 CVWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAEC------HDSAELHLEQIIDLMEAGVKAGKT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  297 VLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVrFVTghLKDGTTDLPWQDLV-- 374
Cdd:PRK15473  83 VVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSL-IIT--RMEGRTPVPAREQLes 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597807  375 -APGQT-LVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEVHAPTLVIVG 446
Cdd:PRK15473 160 fASHQTsMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVG 233
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 6-115 1.48e-35

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


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 127.21  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807     6 LFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEqgggelLERDYQDGDQPGCALIIAATDDEPL 85
Cdd:pfam13241   1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEITPFLEGLLD------LIRREFEGDLDGADLVIAATDDPEL 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 15597807    86 NAEVSRAANARGIPVNVVDAPALCSVIFPA 115
Cdd:pfam13241  75 NERIAALARARGILVNVADDPELCDFYFPA 104
TP_methylase cd09815
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ...
 222-446 2.75e-33

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: 125.20  E-value: 2.75e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 222 VGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPsilELCRRDAERLYVGKR--RAEHAVPQDRINRLLVELASQGKRVLR 299
Cdd:cd09815   1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSK---LLSLVLRAILKDGKRiyDLHDPNVEEEMAELLLEEARQGKDVAF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 300 LKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLthrdhAQSVRFVTGH-LKDGTTDLPWQDLVAPGQ 378
Cdd:cd09815  78 LSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASdLLENPRLLVLKALAKERR 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597807 379 TLVFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQLVAEHEvHAPTLVIVG 446
Cdd:cd09815 153 HLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAERTERG-KPLTTILVG 219
TP_methylase cd11724
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ...
 219-446 4.24e-33

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: 125.36  E-value: 4.24e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 219 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDR---------------LVAPSIL--ELCRRDAERLYVGKRRAEHAVPQD 281
Cdd:cd11724   2 LYLVGVGPGDPDLITLRALKAIKKADVVFAPPdlrkrfaeylagkevLDDPHGLftYYGKKCSPLEEAEKECEELEKQRA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 282 RINRLLVELASQGKRVLRLKGGDPFIFGRGG---EEIDELAAhgipfQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVT 358
Cdd:cd11724  82 EIVQKIREALAQGKNVALLDSGDPTIYGPWIwylEEFADLNP-----EVIPGVSSFNAANAALKRSLTGGGDSRSVILTA 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 359 GHLKDGtTDLPWQDLVAPGQTLVFYMGLVGLPVICEQLvAHGRSAQTPAAL-IQQGTTAQQRVFTGTLENLPQLVAEHEV 437
Cdd:cd11724 157 PFALKE-NEDLLEDLAATGDTLVIFMMRLDLDELVEKL-KKHYPPDTPVAIvYHAGYSEKEKVIRGTLDDILEKLGGEKE 234


                ....*....
gi 15597807 438 HAPTLVIVG 446
Cdd:cd11724 235 PFLGLIYVG 243
PRK06718 PRK06718
NAD(P)-binding protein;
3-178 1.97e-28

NAD(P)-binding protein;


Pssm-ID: 180667 [Multi-domain]  Cd Length: 202  Bit Score: 111.28  E-value: 1.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807    3 FLPLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCALIIAATDD 82
Cdd:PRK06718   1 NMPLMIDLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVISPELTENLVKLVEEGKIRWKQKEFEPSDIVDAFLVIAATND 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   83 EPLNAEVSRAAnARGIPVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLAGLASRFR 162
Cdd:PRK06718  81 PRVNEQVKEDL-PENALFNVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYECR 159

                        170
                 ....*....|....*.
gi 15597807  163 HRVKELLPDLQQRRVF 178
Cdd:PRK06718 160 QKIKELQIEKREKQIL 175
CobJ COG1010
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ...
 215-446 7.21e-27

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: 108.23  E-value: 7.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 215 ATGEVYLVGAGPGDPDLLTFRALRLMQQADVV----LYDRLVAPsilelCRRDAERLYVGKR----RAEHAVpqdrinrl 286
Cdd:COG1010   2 MRGKLYVVGLGPGSAELMTPRARAALAEADVVvgygTYLDLIPP-----LLPGKEVHASGMReeveRAREAL-------- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 287 lvELASQGKRVLRLKGGDPFIFGRGG---EEIDEL-AAHGIPFQVVPGITAASGCAAYAGIPLTHrDhaqsvrFVTGHLK 362
Cdd:COG1010  69 --ELAAEGKTVAVVSSGDPGVYGMAGlvlEVLEEGgAWRDVEVEVVPGITAAQAAAARLGAPLGH-D------FCVISLS 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 363 DGTTdlPWQ------DLVAPGqtlvfymGLV-------------GLPVICEQLVAHgRSAQTPAALIQQGTTAQQRVFTG 423
Cdd:COG1010 140 DLLT--PWEviekrlRAAAEA-------DFVialynprsrkrpwQLERALEILLEH-RPPDTPVGIVRNAGRPDESVTVT 209

                       250       260
                ....*....|....*....|...
gi 15597807 424 TLENLPqlvaEHEVHAPTLVIVG 446
Cdd:COG1010 210 TLGELD----PEEVDMLTTVIIG 228
Precorrin_3B_C17_MT cd11646
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ...
 219-446 3.29e-26

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: 106.35  E-value: 3.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 219 VYLVGAGPGDPDLLTFRALRLMQQADVV----LYDRLVAPSIlelcrRDAERLYVGKR----RAEHAVpqdrinrllvEL 290
Cdd:cd11646   1 LYVVGIGPGSADLMTPRAREALEEADVIvgykTYLDLIEDLL-----PGKEVISSGMGeeveRAREAL----------EL 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 291 ASQGKRVLRLKGGDPFIFGRGG---EEIDElAAHGIPFQVVPGITAASGCAAYAGIPLTHrDhaqsvrFVTGHLKDGTTd 367
Cdd:cd11646  66 ALEGKRVALVSSGDPGIYGMAGlvlELLDE-RWDDIEVEVVPGITAALAAAALLGAPLGH-D------FAVISLSDLLT- 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 368 lPWQ------------DLVapgqtLVFY----MGLVG-LPVICEQLVAHgRSAQTPAALIQQGTTAQQRVFTGTLENLPq 430
Cdd:cd11646 137 -PWEviekrlraaaeaDFV-----IALYnprsKKRPWqLEKALEILLEH-RPPDTPVGIVRNAGREGEEVTITTLGELD- 208

                       250
                ....*....|....*.
gi 15597807 431 lvaEHEVHAPTLVIVG 446
Cdd:cd11646 209 ---PEDVDMFTTVIIG 221
CobF COG2243
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ...
 216-434 4.50e-25

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: 102.87  E-value: 4.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 216 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVLY------DRLVAPSILELCRRDAERLYVG---KRRAEHAVP--QDRIN 284
Cdd:COG2243   2 MGKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagKASLAREIVAPYLPPARIVELVfpmTTDYEALVAawDEAAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 285 RLLVELAsQGKRVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDhaQSVRFVTGHLKDG 364
Cdd:COG2243  82 RIAEELE-AGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLAEGD--EPLTVLPGTLLEE 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 365 TtdlpWQDLVAPGQTLVFYMGLVGLPVICEQLVAHGRSAQtpAALIQQGTTAQQRVFTGtLENLPQLVAE 434
Cdd:COG2243 159 E----LERALDDFDTVVIMKVGRNFPKVREALEEAGLLDR--AWYVERAGMPDERIVPG-LAEVDIEEAP 221
Precorrin_2_C20_MT cd11645
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ...
 222-430 1.01e-21

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: 93.34  E-value: 1.01e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 222 VGAGPGDPDLLTFRALRLMQQADVVLY------DRLVAPSI---LELCRRDAERLYV--GKRRAEHAVPQDRINRLLVEL 290
Cdd:cd11645   1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggEGSAALIIaaaLLIPDKEIIPLEFpmTKDREELEEAWDEAAEEIAEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 291 ASQGKRV--LRLkgGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDhaQSVRFVTGHLKDGTtdl 368
Cdd:cd11645  81 LKEGKDVafLTL--GDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLAILPATYDEEE--- 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597807 369 pWQDLVAPGQTLVFYMGLVGLPVICEQLVAHGRSAQtpAALIQQGTTAQQRVFTGTLENLPQ 430
Cdd:cd11645 154 -LEKALENFDTVVLMKVGRNLEEIKELLEELGLLDK--AVYVERCGMEGERIYTDLEELKEE 212
cobJ_cbiH TIGR01466
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ...
 219-446 1.16e-20

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: 90.82  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   219 VYLVGAGPGDPDLLTFRALRLMQQADVV----LYDRLVAPsilelCRRDAERLYVGKR----RAEHAVpqdrinrllvEL 290
Cdd:TIGR01466   1 LYVVGIGPGAEELMTPEAKEALAEADVIvgykTYLDLIED-----LIPGKEVVTSGMReeiaRAELAI----------EL 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   291 ASQGKRVLRLKGGDPFIFGRGGEEIDELAAHG--IPFQVVPGITAASGCAAYAGIPLTHrdhaqsvRFVTGHLKDGTTDL 368
Cdd:TIGR01466  66 AAEGRTVALVSSGDPGIYGMAALVFEALEKKGaeVDIEVIPGITAASAAASLLGAPLGH-------DFCVISLSDLLTPW 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   369 PW--QDLVAPGQ---TLVFYMGLV-----GLPVICEQLVAHgRSAQTPAALIQQGTTAQQRVFTGTLENLpqlvAEHEVH 438
Cdd:TIGR01466 139 PEieKRLRAAAEadfVIAIYNPRSkrrpeQFRRAMEILLEH-RKPDTPVGIVRNAGREGEEVEITTLAEL----DEELID 213


                  ....*...
gi 15597807   439 APTLVIVG 446
Cdd:TIGR01466 214 MLTTVIIG 221
cobI_cbiL TIGR01467
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ...
 217-420 2.74e-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: 83.51  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   217 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLY------DRLVAPSILE-LCRRDAERLY-----VGKRRAEHAVPQDRIN 284
Cdd:TIGR01467   1 GKLYGVGVGPGDPELITVKALEALRSADVIAVpaskkgRESLARKIVEdYLKPNDTRILelvfpMTKDRDELEKAWDEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   285 RLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTGHLKDG 364
Cdd:TIGR01467  81 EAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEGDESLAILPATAGEAEL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597807   365 TTDLPWQDlvapgqTLVFYMGLVGLPVICEQLVAHGRSAQtpAALIQQGTTAQQRV 420
Cdd:TIGR01467 161 EKALAEFD------TVVLMKVGRNLPQIKEALAKLGRLDA--AVVVERATMPDEKI 208
CysG_dimerizer pfam10414
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the ...
 152-207 8.92e-18

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: 76.82  E-value: 8.92e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597807   152 GQLAGLASRFRHRVKELLPDLQQRRVFWENLFQGEIAERVLAGRPAEAERLLEEHL 207
Cdd:pfam10414   1 GRLAALAGRFRDRVKARLPDVAARRRFWERVFDGPVAELVLAGDEDEAEALLEQAL 56
Precorrin-6Y-MT cd11644
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ...
 222-445 5.49e-17

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: 79.08  E-value: 5.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 222 VGAGPGDPDLLTFRALRLMQQADVVlydrLVAPSILELCRRDAERLYVgkrraehaVPQDRINRLLVELASQGKRVLRLK 301
Cdd:cd11644   1 IGIGPGGPEYLTPEAREAIEEADVV----IGAKRLLELFPDLGAEKIP--------LPSEDIAELLEEIAEAGKRVVVLA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 302 GGDPFIFGRGGEEIDELAAHgiPFQVVPGITAASGCAAYAGIPLthrdhaQSVRFVTGHlkdGTTDLPWQDLVAPGQTLV 381
Cdd:cd11644  69 SGDPGFYGIGKTLLRRLGGE--EVEVIPGISSVQLAAARLGLPW------EDARLVSLH---GRDLENLRRALRRGRKVF 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597807 382 FYMGLVGLP-VICEQLVAHGRsAQTPAALIQQGTTAQQRVFTGTLENLpqlvAEHEVHAPTLVIV 445
Cdd:cd11644 138 VLTDGKNTPaEIARLLLERGL-GDSRVTVGENLGYPDERITEGTAEEL----AEEEFSDLNVVLI 197
PRK05765 PRK05765
precorrin-3B C17-methyltransferase; Provisional
 217-446 6.07e-17

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 235597  Cd Length: 246  Bit Score: 80.21  E-value: 6.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  217 GEVYLVGAGPGDPDLLTFRALRLMQQADVVL----YDRLVApSILE----LCRRDAERLYvgkrRAEHAvpqdrinrllV 288
Cdd:PRK05765   2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgyntYLRLIS-DLLDgkevIGARMKEEIF----RANTA----------I 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  289 ELASQGKRVLRLKGGDPFIFGRGGEEIDELAAHGIP--FQVVPGITAASGCAAYAGIPLthrdhaqSVRFVTGHLKDGTT 366
Cdd:PRK05765  67 EKALEGNIVALVSSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGSPL-------SLDFVVISLSDLLI 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  367 dlPWQDLV------APGQTLVFYMGLVGLPVICEQL--VAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPqlVAEHEVH 438
Cdd:PRK05765 140 --PREEILhrvtkaAEADFVIVFYNPINENLLIEVMdiVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWK--EHMDEIG 215


                 ....*...
gi 15597807  439 APTLVIVG 446
Cdd:PRK05765 216 MTTTMIIG 223
PRK06719 PRK06719
precorrin-2 dehydrogenase; Validated
 5-155 2.37e-16

precorrin-2 dehydrogenase; Validated


Pssm-ID: 180668 [Multi-domain]  Cd Length: 157  Bit Score: 76.16  E-value: 2.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807    5 PLFHSLQGRLALVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHL--VEQGGGELLERDYQDGDqpgcaLIIAATDD 82
Cdd:PRK06719   6 PLMFNLHNKVVVIIGGGKIAYRKASGLKDTGAFVTVVSPEICKEMKELpyITWKQKTFSNDDIKDAH-----LIYAATNQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597807   83 EPLNAEVSRAANARGIpVNVVDAPALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWIPSTYGQLA 155
Cdd:PRK06719  81 HAVNMMVKQAAHDFQW-VNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQELTSILPKLIKKIS 152
PRK05576 PRK05576
cobalt-factor II C(20)-methyltransferase;
217-359 2.75e-16

cobalt-factor II C(20)-methyltransferase;


Pssm-ID: 235512 [Multi-domain]  Cd Length: 229  Bit Score: 77.65  E-value: 2.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  217 GEVYLVGAGPGDPDLLTFRALRLMQQADVVlydrlVAPSILELCRRDAERL---YV-------------GKRRAEHAVPQ 280
Cdd:PRK05576   2 GKLYGIGLGPGDPELLTVKAARILEEADVV-----YAPASRKGGGSLALNIvrpYLkeeteivelhfpmSKDEEEKEAVW 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597807  281 DRINRLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRFVTG 359
Cdd:PRK05576  77 KENAEEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGDESLAIIPATR 155
PRK05990 PRK05990
precorrin-2 C(20)-methyltransferase; Reviewed
 215-354 3.93e-15

precorrin-2 C(20)-methyltransferase; Reviewed


Pssm-ID: 180341  Cd Length: 241  Bit Score: 74.64  E-value: 3.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  215 ATGEVYLVGAGPGDPDLLTFRALRLMQQADVVLY-----DRLVAPSILE-LCRRDAERL---Y---VGKRRAEHAVPQ-- 280
Cdd:PRK05990   1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYfvakgKKGNAFGIVEaHLSPGQTLLplvYpvtTEILPPPLCYETvi 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597807  281 ----DRINRLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELAAHgIPFQVVPGITAASGCAAYAGIPLTHRDHAQSV 354
Cdd:PRK05990  81 adfyDTSAEAVAAHLDAGRDVAVICEGDPFFYGSYMYLHDRLAPR-YETEVIPGVCSMLGCWSVLGAPLVYRNQSLSV 157
PRK05787 PRK05787
cobalt-precorrin-7 (C(5))-methyltransferase;
219-363 3.83e-13

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


Pssm-ID: 235609 [Multi-domain]  Cd Length: 210  Bit Score: 68.36  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  219 VYLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKRraehavpqDRINRLlvELASQGKRVL 298
Cdd:PRK05787   2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGLR--------DLLEWL--ELAAKGKNVV 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597807  299 RLKGGDPFIFGRGGEEIdELAAHGIPFQVVPGITAASGCAAYAGIPLTHrdhaqsVRFVTGHLKD 363
Cdd:PRK05787  72 VLSTGDPLFSGLGKLLK-VRRAVAEDVEVIPGISSVQYAAARLGIDMND------VVFTTSHGRG 129
CobL COG2241
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ...
 219-445 1.64e-11

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: 63.24  E-value: 1.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 219 VYLVGAGPGDPDLLTFRALRLMQQADVVL-YDRLvapsiLELCR-RDAERLYVGkrraehaVPQDRINRLLVELAsQGKR 296
Cdd:COG2241   4 LTVVGIGPGGPDGLTPAAREAIAEADVVVgGKRH-----LELFPdLGAERIVWP-------SPLSELLEELLALL-RGRR 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 297 VLRLKGGDPFIFGRGGEEIDELAAHgiPFQVVPGITAASGCAAYAGIPLthrdhaQSVRFVTGHlkdGTTDLPWQDLVAP 376
Cdd:COG2241  71 VVVLASGDPLFYGIGATLARHLPAE--EVRVIPGISSLQLAAARLGWPW------QDAAVVSLH---GRPLERLLPALAP 139

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 377 GQTLVFYMGLV-GLPVICEQLVAHGRSAqTPAALIQQGTTAQQRVFTGTLENLpqlvAEHEVHAPTLVIV 445
Cdd:COG2241 140 GRRVLVLTDDGnTPAAIARLLLERGFGD-SRLTVLENLGGPDERITRGTAEEL----ADADFSDLNVVAI 204
cbiH PRK15478
precorrin-3B C(17)-methyltransferase;
219-446 5.35e-09

precorrin-3B C(17)-methyltransferase;


Pssm-ID: 185375 [Multi-domain]  Cd Length: 241  Bit Score: 56.81  E-value: 5.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  219 VYLVGAGPGDPDLLTFRALRLMQQADVVL----YDRLVAPSILelcrrDAERLYVGKRRaehavpqdRINRLL--VELAS 292
Cdd:PRK15478   2 LSVIGIGPGSQAMMTMEAIEALQAAEIVVgyktYTHLVKAFTG-----DKQVIKTGMCK--------EIERCQaaIELAQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  293 QGKRVLRLKGGDPFIFGRGGEEIDELAAHGIPFQV--VPGITAASGCAAYAGIPLTHrdhaqsvRFVTGHLKDGTTdlPW 370
Cdd:PRK15478  69 AGHNVALISSGDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLGAPLMH-------DFCHISLSDLLT--PW 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  371 ----QDLVAPGQ---TLVFY----MGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQlvaeHEVHA 439
Cdd:PRK15478 140 pvieKRIVAAGEadfVICFYnprsRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTLGDMDF----EPVDM 215


                 ....*..
gi 15597807  440 PTLVIVG 446
Cdd:PRK15478 216 TSLVIVG 222
PRK05948 PRK05948
precorrin-2 C(20)-methyltransferase;
216-431 1.79e-08

precorrin-2 C(20)-methyltransferase;


Pssm-ID: 180320  Cd Length: 238  Bit Score: 55.03  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  216 TGEVYLVGAGPGDPDLLTFRALRLMQQADVV-----------LYDRLVAPSIlelcRRDAERL-----YVGKRRAEHAVP 279
Cdd:PRK05948   3 LGTLYGISVGPGDPELITLKGLRLLQSAPVVafpaglagqpgLAEQIIAPWL----SPQQIKLplyfpYVQDEEQLEQAW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  280 QDRINRLLVELAsQGKRVLRLKGGDPFI---FGRGGEEIDELAAHgIPFQVVPGITAASGCAAYAGIPLTHRDHAQSVRF 356
Cdd:PRK05948  79 QAAADQVWHYLE-QGEDVAFACEGDVSFystFTYLAQTLQELYPQ-VAIQTIPGVCSPLAAAAALGIPLTLGSQRLAILP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597807  357 VTGHLKDGTTDLPWQDLVAPGQTLVFYmglvglPVICEQLVAHGRSAQtpAALIQQGTTAQQRVFTgTLENLPQL 431
Cdd:PRK05948 157 ALYHLEELEQALTWADVVVLMKVSSVY------PQVWQWLKARNLLEQ--ASLVERATTPEQVIYR-NLEDYPDL 222
CbiE TIGR02467
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ...
 221-430 4.57e-08

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: 53.09  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   221 LVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPSILELCRRDAERLYVGKrraehavPQDRINRLLVElASQGKRVLRL 300
Cdd:TIGR02467   1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIILTYK-------DLDELLEFIAA-TRKEKRVVVL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   301 KGGDPFIFGRGGEEIDELAAHGIpfQVVPGITAASGCAAYAGIPLthrdhaQSVRFVTGHLKDGTTDLPwQDLVAPGQTL 380
Cdd:TIGR02467  73 ASGDPLFYGIGRTLAERLGKERL--EIIPGISSVQYAFARLGLPW------QDAVVISLHGRELDELLL-ALLRGHRKVA 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597807   381 VFYMGLVGLPVICEQLVAHGRSAQTPAALIQQGTTAQQRVFTGTLENLPQ 430
Cdd:TIGR02467 144 VLTDPRNGPAEIARELIELGIGGSYELTVGENLGYEDERITEGTLEEIAA 193
PRK05991 PRK05991
precorrin-3B C17-methyltransferase; Provisional
 216-347 1.79e-07

precorrin-3B C17-methyltransferase; Provisional


Pssm-ID: 180342 [Multi-domain]  Cd Length: 250  Bit Score: 52.06  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807  216 TGEVYLVGAGPGDPDLLTFRALRLMQQADVVL-YdrlvAPSILELCRRDAERLYVGKRRAEhavpQDRINRLLvELASQG 294
Cdd:PRK05991   2 SGRLFVIGTGPGNPEQMTPEALAAVEAATDFFgY----GPYLDRLPLRADQLRHASDNREE----LDRAGAAL-AMAAAG 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597807  295 KRVLRLKGGDPFIFGRGG---EEIDE--LAAHGIPFQVVPGITAASGCAAYAGIPLTH 347
Cdd:PRK05991  73 ANVCVVSGGDPGVFAMAAavcEAIENgpAAWRAVDLTIVPGVTAMLAVAARIGAPLGH 130
Precorrin-6A-synthase cd11643
Precorrin-6A synthase (also named CobF); Precorrin-6A synthase participates in the pathway ...
 221-346 6.39e-06

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


Pssm-ID: 381170  Cd Length: 244  Bit Score: 47.49  E-value: 6.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 221 LVGAGPGDPDLLTFRALRLMQQADVVLY-------DRLVAPsILELCRR-------------DAERL-----YVGKRRAE 275
Cdd:cd11643   1 LIGIGPGDPDHLTLQAIEALNRVDVFFVldkgeekSDLAAL-RREICERhlgdrpyrvvefpDPERDrspadYRAAVADW 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597807 276 HAVPQDRINRLLVELASQGKRVLRLKGGDPFIFGRGGEEIDELAAHGIPF--QVVPGITAASGCAAYAGIPLT 346
Cdd:cd11643  80 HDARAALWEDAIAEELPEGGTGAFLVWGDPSLYDSTLRILDRLRAGRVALevEVIPGISSVQALAARHRIPLN 152
DHP5_DphB cd11647
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ...
 220-338 8.85e-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: 47.03  E-value: 8.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 220 YLVGAGPGDPDLLTFRALRLMQQADVVLYDRLVAPsILELCRRDAERLYvGKR-----RAEHAVPQDRInrllVELASQG 294
Cdd:cd11647   3 YLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSI-LPGSKLEELEKLI-GKKiilldREDLEEESEEI----LEEAKKK 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597807 295 KRVLrLKGGDPFIfgrggeeidelaA--H----------GIPFQVVPG---ITAASGCA 338
Cdd:cd11647  77 DVAL-LVPGDPLI------------AttHidlrleakkrGIKVKVIHNasiLSAAGSTS 122
PRK05562 PRK05562
NAD(P)-dependent oxidoreductase;
16-147 3.75e-05

NAD(P)-dependent oxidoreductase;


Pssm-ID: 235504  Cd Length: 223  Bit Score: 45.02  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807   16 LVVGGGEVALRKARLLADAGARLRVVAPQIHIELRHLVEQGGGELLERDYQDGDQPGCALIIAATDDEPLNAEVSRaaNA 95
Cdd:PRK05562  29 LIIGGGKAAFIKGKTFLKKGCYVYILSKKFSKEFLDLKKYGNLKLIKGNYDKEFIKDKHLIVIATDDEKLNNKIRK--HC 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597807   96 RGIPVNVVDA--PALCSVIFPAIVDRSPLVVAVSSGGDAPVLARLIRAKLETWI 147
Cdd:PRK05562 107 DRLYKLYIDCsdYKKGLCIIPYQRSTKNFVFALNTKGGSPKTSVFIGEKVKNFL 160
YabN_N_like cd11723
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ...
 219-374 6.25e-04

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: 40.93  E-value: 6.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 219 VYLVGAGPGDPDLLTFRALRLMQQADVVlYDR-LVAPSILELCRRDAE-----RLYvgkRRAEH--AVPQdRINRLLVEL 290
Cdd:cd11723   1 ITIVGLGPGDPDLLTLGALEALKSADKV-YLRtARHPVVEELKEEGIEfesfdDLY---EEAEDfeEVYE-AIAERLLEA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 291 ASQGKrVLRLKGGDPFIFGRGGEEIDELAAHGIPFQVVPGITAASGCAAYAGIplthrDHAQSVRFVTGHLKDGTTDLPW 370
Cdd:cd11723  76 AEHGD-VVYAVPGHPLVAERTVQLLLERAEEGIEVEIIPGVSFLDAALAALGI-----DPIEGLQILDALDLDAEDLDPR 149


                ....
gi 15597807 371 QDLV 374
Cdd:cd11723 150 LPLL 153
Sirohm_synth_M pfam14824
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme ...
 122-144 8.23e-04

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


Pssm-ID: 464336 [Multi-domain]  Cd Length: 25  Bit Score: 36.60  E-value: 8.23e-04
                          10        20
                  ....*....|....*....|...
gi 15597807   122 LVVAVSSGGDAPVLARLIRAKLE 144
Cdd:pfam14824   1 LQIAISTNGKSPRLAALIRREIE 23
OphMA_like cd19916
tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin ...
 217-333 4.31e-03

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: 38.61  E-value: 4.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597807 217 GEVYLVGAGPGDPDLLTFRALRLMQQADVVLY---DRLVAPSILELCrRDAERLYV----GKRRAEhaVPQDRINRLLVE 289
Cdd:cd19916   1 GSLVVVGTGIKGIGHLTLEAESAIEQADKVFYlvaDPLTEEWLRELN-PNAEDLYDlygeGKPRLD--TYREMAERILEA 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15597807 290 lASQGKRVLRLKGGDPFIFGRGGEE-IDELAAHGIPFQVVPGITA 333
Cdd:cd19916  78 -VRAGKPVCAAFYGHPGVFVSPSHLaIRIARREGYRARMLPGISA 121
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH