|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
3-245 |
2.20e-119 |
|
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: 349.76 E-value: 2.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVT 82
Cdd:COG0007 3 KVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGKRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLaDLNFAELAKT 162
Cdd:COG0007 83 VRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKL-DLDWAALARP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQK-DIDTLSSPAIIVIGEVVKLREKLC 241
Cdd:COG0007 162 GGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELaAEAGLKSPALIVVGEVVALREKLS 241
|
....
gi 1589195127 242 FYEQ 245
Cdd:COG0007 242 WFEA 245
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
7-234 |
7.10e-108 |
|
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: 319.77 E-value: 7.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 7 VGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVTVRLK 86
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 87 GGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLADLnFAELAKTKDTL 166
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDD-DAALARPGGTL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589195127 167 IFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQK-DIDTLSSPAIIVIGEVV 234
Cdd:cd11642 160 VIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKaAEAGIRSPALIVVGEVV 228
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
3-237 |
7.79e-103 |
|
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: 307.23 E-value: 7.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVT 82
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLADLNFAELAKT 162
Cdd:TIGR01469 81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALEVDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDID-TLSSPAIIVIGEVVKLR 237
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEaNLKSPALIVIGEVVALR 236
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
1-240 |
3.85e-101 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 303.29 E-value: 3.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 1 MNKVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYP 80
Cdd:PRK06136 2 MGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 81 VTVRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVL-ADLNFAEL 159
Cdd:PRK06136 82 VVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLePEVNWSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 160 AKTKDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDIDT-LSSPAIIVIGEVVKLRE 238
Cdd:PRK06136 162 ADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEdIQSPAIIVIGEVVALRA 241
|
..
gi 1589195127 239 KL 240
Cdd:PRK06136 242 KL 243
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
3-214 |
5.94e-43 |
|
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: 150.96 E-value: 5.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVT 82
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTngfRVYTAHSQKDVLADLNFAELAKT 162
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEV---LSVLFLPGLARIELRLLEALLAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEkATPMAICSHVSMPSQKVLTTTLAEL 214
Cdd:pfam00590 158 GDTVVLLYGPRRLAELAELLLELYPD-TTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
260-477 |
9.23e-34 |
|
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole (linear) to uroporphyrinogen-III, the fourth step in the biosynthesis of heme. This ubiquitous enzyme is present in eukaryotes, bacteria and archaea. Mutations in the human uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria, a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 119440 [Multi-domain] Cd Length: 239 Bit Score: 127.42 E-value: 9.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 260 KEEHQA---AKLLREQGAWCEEV---QCGYCKAIAHTWTKEAFQSFTHVVFTSAQVVHILMKQLQEAGfdSRILYQCKLC 333
Cdd:cd06578 5 RPRPQAdelAALLEALGAEVLELpliEIEPLDDAELDAALADLDEYDWLIFTSPNAVEAFFEALEELG--LRALAGLKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 334 VMGKGTKKALAQYGLCADLMPNIHDSKHMAELLTASVQKQDHILLPKAVNGNTYLQKTLETQ-CKVSYVPLYT------I 406
Cdd:cd06578 83 AVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQDGKGKRILRPRGGRAREDLAEALRERgAEVDEVEVYRtvppdlD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589195127 407 EELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQRKQM------VYAMGERTKQALIKEGFTSITTLKHAEMEEFVKAI 477
Cdd:cd06578 163 AELLELLEEGAIDAVLFTSPSTVRNLLELLGKEGRAllknvkIAAIGPRTAEALRELGLKVVIVAESPTLEALLEAL 239
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
294-462 |
8.57e-27 |
|
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III synthase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 441195 Cd Length: 229 Bit Score: 107.68 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 294 EAFQSFTHVVFTSAQVVHILMKQLQEAGFDsriLYQCKLCVMGKGTKKALAQYGLCADLMPNIHDSKHMAELLTAsvQKQ 373
Cdd:COG1587 51 ERLGDYDWVIFTSANAVRAFFEALEELGLR---LAGLKIAAVGPKTAAALRAAGLKVDLVPEGFTSEGLLELLQA--LAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 374 DHILLPKAVNGNTYLQKTLETQ-CKVSYVPLY-------TIEELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQRKQ---- 441
Cdd:COG1587 126 KRVLIPRGDGGREDLAETLRAAgAEVDEVEVYrtvppddLPEELLEALAAGEIDAVLFTSPSTVRNLLELAPDAGLaala 205
|
170 180
....*....|....*....|...
gi 1589195127 442 --MVYAMGERTKQALIKEGFTSI 462
Cdd:COG1587 206 rvRIAAIGPRTAEAARELGLKVV 228
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
294-471 |
1.34e-25 |
|
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyzes the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as Swiss:Q59294 with pfam00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 426866 [Multi-domain] Cd Length: 230 Bit Score: 104.71 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 294 EAFQSFTHVVFTSAQVVHILMKQLQEAGFDSRILYQCKLCVMGKGTKKALAQYGLCADLMP-NIHDSKHMAELLTASVQK 372
Cdd:pfam02602 35 KDLGEYDWLIFTSANAVRAFFEALKLEGEDLRALANIKIAAVGPKTARALREAGLTPDFVPsEEGTAEGLAEELAELLAG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 373 QdHILLPKAVNGNTYLQKTLETQ-CKVSYVPLYT-------IEELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQRKQM-- 442
Cdd:pfam02602 115 K-RVLLLRGNIGRDDLAEALRERgAEVTEVVVYRtvppeelPEELREALKDGEIDAVTFTSPSTVRNLLELLKDEGLDwl 193
|
170 180 190
....*....|....*....|....*....|...
gi 1589195127 443 ----VYAMGERTKQALIKEGFTSITTLKHAEME 471
Cdd:pfam02602 194 ksvkAAAIGPTTAEALKELGLKVDVVAERPTME 226
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
297-482 |
1.67e-21 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 93.49 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 297 QSFTHVVFTSAQVVHILMKQLQEAGFDSRILYqcKLCVMGKGTKKALAQYGLCADLMPNIHDSKHMAELLTASVQKQDHI 376
Cdd:PRK05928 51 LGADWVIFTSKNAVEFLLSALKKKKLKWPKNK--KYAAIGEKTALALKKLGGKVVFVPEDGESSELLLELPELLLKGKRV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 377 LLPKAVNGNTYLQKTLETQ-CKVSYVPLYTI-------EELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQR-------KQ 441
Cdd:PRK05928 129 LYLRGNGGREVLGDTLEERgAEVDECEVYERvppkldgAELLARLQSGEVDAVIFTSPSTVRAFFSLAPELgrrewllSC 208
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1589195127 442 MVYAMGERTKQALIKEGFTSITTLKHAEMEEFVKAILHHEK 482
Cdd:PRK05928 209 KAVVIGERTAEALRELGIKVIIVPDSADNEALLRALKELLK 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
3-245 |
2.20e-119 |
|
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: 349.76 E-value: 2.20e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVT 82
Cdd:COG0007 3 KVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGKRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLaDLNFAELAKT 162
Cdd:COG0007 83 VRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKL-DLDWAALARP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQK-DIDTLSSPAIIVIGEVVKLREKLC 241
Cdd:COG0007 162 GGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELaAEAGLKSPALIVVGEVVALREKLS 241
|
....
gi 1589195127 242 FYEQ 245
Cdd:COG0007 242 WFEA 245
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
7-234 |
7.10e-108 |
|
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: 319.77 E-value: 7.10e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 7 VGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVTVRLK 86
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 87 GGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLADLnFAELAKTKDTL 166
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDD-DAALARPGGTL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589195127 167 IFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQK-DIDTLSSPAIIVIGEVV 234
Cdd:cd11642 160 VIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKaAEAGIRSPALIVVGEVV 228
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
3-237 |
7.79e-103 |
|
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: 307.23 E-value: 7.79e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVT 82
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLADLNFAELAKT 162
Cdd:TIGR01469 81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALEVDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDID-TLSSPAIIVIGEVVKLR 237
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEaNLKSPALIVIGEVVALR 236
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
1-240 |
3.85e-101 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 303.29 E-value: 3.85e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 1 MNKVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYP 80
Cdd:PRK06136 2 MGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 81 VTVRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVL-ADLNFAEL 159
Cdd:PRK06136 82 VVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLePEVNWSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 160 AKTKDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDIDT-LSSPAIIVIGEVVKLRE 238
Cdd:PRK06136 162 ADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEdIQSPAIIVIGEVVALRA 241
|
..
gi 1589195127 239 KL 240
Cdd:PRK06136 242 KL 243
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
1-237 |
3.16e-79 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 247.62 E-value: 3.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 1 MNKVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVD---AGR 77
Cdd:PLN02625 14 PGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSfaeAGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 78 TypvTVRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLADLNFA 157
Cdd:PLN02625 94 T---VVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTDPLDVA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 158 ELAKTKD-TLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDIDT-LSSPAIIVIGEVVK 235
Cdd:PLN02625 171 EAAADPDtTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAgLVSPTVIVVGEVVA 250
|
..
gi 1589195127 236 LR 237
Cdd:PLN02625 251 LS 252
|
|
| PRK07168 |
PRK07168 |
uroporphyrin-III C-methyltransferase; |
1-348 |
6.22e-79 |
|
uroporphyrin-III C-methyltransferase;
Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 254.15 E-value: 6.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 1 MNK-VYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTY 79
Cdd:PRK07168 1 MNGyVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 80 PVTVRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSqKDVLADLNFAEL 159
Cdd:PRK07168 81 KIVVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHA-KGPLTDHGKYNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 160 AKTKDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQ--KDiDTLSSPAIIVIGEVVKLR 237
Cdd:PRK07168 160 SHNSDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSivKN-ENISNPSMTIVGDVVSLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 238 EKLCFYEQKPLFQKRYLLVKVQKEEHQAAKLLREQGAwcEEVQCGYCKAIAHTWTKEAFQSFTHV---VFTSAQVVHILM 314
Cdd:PRK07168 239 NQIAWKERKPLHGKKVLFTSATNKTSVMKQKLQEAGA--EIYQIPTFKKEEYTLTLEQINEIFNVnrlVFCSAESVEILM 316
|
330 340 350
....*....|....*....|....*....|....
gi 1589195127 315 KQLQEAGFDSRILyQCKLCVMGKGTKKALAQYGL 348
Cdd:PRK07168 317 QSCSKYKKDIRSL-QAELQHMNVATQEKLMQYGL 349
|
|
| cysG |
PRK10637 |
siroheme synthase CysG; |
3-240 |
1.99e-68 |
|
siroheme synthase CysG;
Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 225.79 E-value: 1.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVT 82
Cdd:PRK10637 217 EVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDvlADLNFAELAKT 162
Cdd:PRK10637 297 VRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTG--GELDWENLAAE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLT---TTLAELHQKdidtLSSPAIIVIGEVVKLREK 239
Cdd:PRK10637 375 KQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVSgtlTQLGELAQQ----VNSPSLIIVGRVVGLRDK 450
|
.
gi 1589195127 240 L 240
Cdd:PRK10637 451 L 451
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
3-214 |
5.94e-43 |
|
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: 150.96 E-value: 5.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSLLSYAKADCKLIYVGKENHKHTMPQAMIQKLLVDAGRTYPVT 82
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTngfRVYTAHSQKDVLADLNFAELAKT 162
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEV---LSVLFLPGLARIELRLLEALLAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEkATPMAICSHVSMPSQKVLTTTLAEL 214
Cdd:pfam00590 158 GDTVVLLYGPRRLAELAELLLELYPD-TTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
7-235 |
1.12e-38 |
|
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: 140.22 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 7 VGAGCGDPALLSLKGKACIEEADCILY-DRLIDPSLLSYAKADCKLIyvgkenHKHTMPQAMIQKLLVDAGRTYPVTVRL 85
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV------DSAGMTLEEIIEVMREAAREGKDVVRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 86 KGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFrVYT-AHSQKDVLADLNFAELAKTKD 164
Cdd:cd11641 75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTV-ILTrLEGRTPVPEGESLRELAKHGA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195127 165 TL-IFLmglrSAM---QLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDIDT-LSSPAIIVIGEVVK 235
Cdd:cd11641 154 TLaIFL----SAAlieEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAgITRTALILVGPALG 225
|
|
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
1-234 |
2.96e-34 |
|
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: 129.02 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 1 MNKVYLVGAGCGDPALLSLKGKACIEEADCILY-DRLIDPSLLSYAKADCKLIyvgkeNHKHtMPQAMIQKLLVDAGRTY 79
Cdd:COG2875 2 KGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIV-----DSAS-MTLEEIIALMKEAAAEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 80 PVTVRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTN-------GFRvyTAHSQKDVLa 152
Cdd:COG2875 76 KDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQtviltraEGR--TPMPEGESL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 153 dlnfAELAKTKDTLIFLMGLRSAMQLVEKLLAcGMEKATPMAICSHVSMPSQKVLTTTLAELHQK----DIdtlSSPAII 228
Cdd:COG2875 153 ----ASLAAHGATLAIYLSAHRIDEVVEELLE-GYPPDTPVAVVYRASWPDEKIVRGTLADIAEKvkeaGI---TRTALI 224
|
....*.
gi 1589195127 229 VIGEVV 234
Cdd:COG2875 225 LVGPAL 230
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
260-477 |
9.23e-34 |
|
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole (linear) to uroporphyrinogen-III, the fourth step in the biosynthesis of heme. This ubiquitous enzyme is present in eukaryotes, bacteria and archaea. Mutations in the human uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria, a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 119440 [Multi-domain] Cd Length: 239 Bit Score: 127.42 E-value: 9.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 260 KEEHQA---AKLLREQGAWCEEV---QCGYCKAIAHTWTKEAFQSFTHVVFTSAQVVHILMKQLQEAGfdSRILYQCKLC 333
Cdd:cd06578 5 RPRPQAdelAALLEALGAEVLELpliEIEPLDDAELDAALADLDEYDWLIFTSPNAVEAFFEALEELG--LRALAGLKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 334 VMGKGTKKALAQYGLCADLMPNIHDSKHMAELLTASVQKQDHILLPKAVNGNTYLQKTLETQ-CKVSYVPLYT------I 406
Cdd:cd06578 83 AVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQDGKGKRILRPRGGRAREDLAEALRERgAEVDEVEVYRtvppdlD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589195127 407 EELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQRKQM------VYAMGERTKQALIKEGFTSITTLKHAEMEEFVKAI 477
Cdd:cd06578 163 AELLELLEEGAIDAVLFTSPSTVRNLLELLGKEGRAllknvkIAAIGPRTAEALRELGLKVVIVAESPTLEALLEAL 239
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
4-238 |
1.22e-32 |
|
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: 124.36 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 4 VYLVGAGCGDPALLSLKGKACIEEADCILY-DRLIDPSLLSYAKADCKLIYVGkenhkhTMPQAMIQKLLVDAGRTYPVT 82
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAEVVNSA------GMSLEEIVDIMSDAHREGKDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 83 VRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLADLNFAELAKT 162
Cdd:TIGR01465 75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTPMPEGEKLADLAKH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 163 KDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAEL----HQKDIdtlSSPAIIVIGEVVKLRE 238
Cdd:TIGR01465 155 GATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLadlvREEGI---YRTTLILVGPALDPRI 231
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
7-231 |
7.68e-28 |
|
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: 110.56 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 7 VGAGCGDPALLSLKGKACIEEADCILYDRlIDPSLLSYA-----KADCKLIYVGKENHKHTMPQAMIQKLlvDAGRTypv 81
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAED-KDSKLLSLVlrailKDGKRIYDLHDPNVEEEMAELLLEEA--RQGKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 82 TVRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHrgytnGFRVYTAHSQKDVLADLNFAELAK 161
Cdd:cd09815 75 VAFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGE-----SFLFVTASDLLENPRLLVLKALAK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 162 TKDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDIDTLSSPAIIVIG 231
Cdd:cd09815 150 ERRHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAERTERGKPLTTILVG 219
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
294-462 |
8.57e-27 |
|
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III synthase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 441195 Cd Length: 229 Bit Score: 107.68 E-value: 8.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 294 EAFQSFTHVVFTSAQVVHILMKQLQEAGFDsriLYQCKLCVMGKGTKKALAQYGLCADLMPNIHDSKHMAELLTAsvQKQ 373
Cdd:COG1587 51 ERLGDYDWVIFTSANAVRAFFEALEELGLR---LAGLKIAAVGPKTAAALRAAGLKVDLVPEGFTSEGLLELLQA--LAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 374 DHILLPKAVNGNTYLQKTLETQ-CKVSYVPLY-------TIEELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQRKQ---- 441
Cdd:COG1587 126 KRVLIPRGDGGREDLAETLRAAgAEVDEVEVYrtvppddLPEELLEALAAGEIDAVLFTSPSTVRNLLELAPDAGLaala 205
|
170 180
....*....|....*....|...
gi 1589195127 442 --MVYAMGERTKQALIKEGFTSI 462
Cdd:COG1587 206 rvRIAAIGPRTAEAARELGLKVV 228
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
294-471 |
1.34e-25 |
|
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyzes the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as Swiss:Q59294 with pfam00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 426866 [Multi-domain] Cd Length: 230 Bit Score: 104.71 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 294 EAFQSFTHVVFTSAQVVHILMKQLQEAGFDSRILYQCKLCVMGKGTKKALAQYGLCADLMP-NIHDSKHMAELLTASVQK 372
Cdd:pfam02602 35 KDLGEYDWLIFTSANAVRAFFEALKLEGEDLRALANIKIAAVGPKTARALREAGLTPDFVPsEEGTAEGLAEELAELLAG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 373 QdHILLPKAVNGNTYLQKTLETQ-CKVSYVPLYT-------IEELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQRKQM-- 442
Cdd:pfam02602 115 K-RVLLLRGNIGRDDLAEALRERgAEVTEVVVYRtvppeelPEELREALKDGEIDAVTFTSPSTVRNLLELLKDEGLDwl 193
|
170 180 190
....*....|....*....|....*....|...
gi 1589195127 443 ----VYAMGERTKQALIKEGFTSITTLKHAEME 471
Cdd:pfam02602 194 ksvkAAAIGPTTAEALKELGLKVDVVAERPTME 226
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
297-482 |
1.67e-21 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 93.49 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 297 QSFTHVVFTSAQVVHILMKQLQEAGFDSRILYqcKLCVMGKGTKKALAQYGLCADLMPNIHDSKHMAELLTASVQKQDHI 376
Cdd:PRK05928 51 LGADWVIFTSKNAVEFLLSALKKKKLKWPKNK--KYAAIGEKTALALKKLGGKVVFVPEDGESSELLLELPELLLKGKRV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 377 LLPKAVNGNTYLQKTLETQ-CKVSYVPLYTI-------EELPHSIQDEDYDGVLMTCPFSVQQYAKQTKQR-------KQ 441
Cdd:PRK05928 129 LYLRGNGGREVLGDTLEERgAEVDECEVYERvppkldgAELLARLQSGEVDAVIFTSPSTVRAFFSLAPELgrrewllSC 208
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1589195127 442 MVYAMGERTKQALIKEGFTSITTLKHAEMEEFVKAILHHEK 482
Cdd:PRK05928 209 KAVVIGERTAEALRELGIKVIIVPDSADNEALLRALKELLK 249
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
1-231 |
3.54e-20 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 89.81 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 1 MNKVYLVGAGCGDPALLSLKGKACIEEADCILY-DRLIDPSLLSYAKADCkliyvgkENHKHT-MPQAMIQKLLVDAGRT 78
Cdd:PRK15473 7 PRCVWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQA-------ECHDSAeLHLEQIIDLMEAGVKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 79 YPVTVRLKGGDPYVFGRGAEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGYTNGFRVYTAHSQKDVLADLNFAE 158
Cdd:PRK15473 80 GKTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRTPVPAREQLES 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1589195127 159 LAKTKDTLIFLMGLRSAMQLVEKLLACGMEKATPMAICSHVSMPSQKVLTTTLAELHQKDIDT-LSSPAIIVIG 231
Cdd:PRK15473 160 FASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAgIRKTALILVG 233
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
3-231 |
1.52e-18 |
|
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: 84.91 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCIL--------YDRLI-------DPSLL--SYAKADCKLIYVGKENHKHTMPQ 65
Cdd:cd11724 1 KLYLVGVGPGDPDLITLRALKAIKKADVVFappdlrkrFAEYLagkevldDPHGLftYYGKKCSPLEEAEKECEELEKQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 66 AMIQKL---LVDAGRTypVTVrLKGGDPYVFGRGAeeGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHrGYTNGFRVY 142
Cdd:cd11724 81 AEIVQKireALAQGKN--VAL-LDSGDPTIYGPWI--WYLEEFADLNPEVIPGVSSFNAANAALKRSLTG-GGDSRSVIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 143 TA-HSQKDvlADLNFAELAKTKDTLIFLMGLRSAMQLVEKLLAcGMEKATPMAICSHV-SMPSQKVLTTTLAELHQK-DI 219
Cdd:cd11724 155 TApFALKE--NEDLLEDLAATGDTLVIFMMRLDLDELVEKLKK-HYPPDTPVAIVYHAgYSEKEKVIRGTLDDILEKlGG 231
|
250
....*....|..
gi 1589195127 220 DTLSSPAIIVIG 231
Cdd:cd11724 232 EKEPFLGLIYVG 243
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
7-230 |
1.75e-14 |
|
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.
Pssm-ID: 381171 [Multi-domain] Cd Length: 198 Bit Score: 71.76 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 7 VGAGCGDPALLSLKGKACIEEADCIL-YDRLIDpsllSYAKADCKLIYVGKENhkhtmpqamIQKLLVDAGRTY-PVTVr 84
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVIgAKRLLE----LFPDLGAEKIPLPSED---------IAELLEEIAEAGkRVVV- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 85 LKGGDPYVFGRGAeeGLALAQAGIAFEVVCGISSAIGGLAYAGIPVthrgytNGFRVYTAHSQKdvlaDLNFAELAKTKD 164
Cdd:cd11644 67 LASGDPGFYGIGK--TLLRRLGGEEVEVIPGISSVQLAAARLGLPW------EDARLVSLHGRD----LENLRRALRRGR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589195127 165 TLIFLMGLR-SAMQLVEKLLACGMEKATpMAICSHVSMPSQKVLTTTLAELHQKDIDTLSspaIIVI 230
Cdd:cd11644 135 KVFVLTDGKnTPAEIARLLLERGLGDSR-VTVGENLGYPDERITEGTAEELAEEEFSDLN---VVLI 197
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
3-213 |
7.62e-10 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 58.73 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCIL-YDRLIDpSLLSYAKADCKLIYVGKENHKhtmpqamIQKLLVDAGRTypV 81
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVVgSKRVLE-LFPELIDGEAFVLTAGLRDLL-------EWLELAAKGKN--V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 82 TVrLKGGDPYVFGRGaEEGLALAQAGIAFEVVCGISSAIGGLAYAGIPVthrgytNGFRVYTAHSQKDVLADLnfAELAK 161
Cdd:PRK05787 71 VV-LSTGDPLFSGLG-KLLKVRRAVAEDVEVIPGISSVQYAAARLGIDM------NDVVFTTSHGRGPNFEEL--EDLLK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1589195127 162 TKDTLIFL----MGLRsamQLVEKLLACGMEKATpMAICSHVSMPSQKVLTTTLAE 213
Cdd:PRK05787 141 NGRKVIMLpdprFGPK---EIAAELLERGKLERR-IVVGENLSYPDERIHKLTLSE 192
|
|
| Precorrin_3B_C17_MT |
cd11646 |
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
4-231 |
2.50e-09 |
|
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: 57.42 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 4 VYLVGAGCGDPALLSLKGKACIEEADCIL-YDRLID--PSLLSyakadckliyvGKENHKHTMPQ-------AMIqklLV 73
Cdd:cd11646 1 LYVVGIGPGSADLMTPRAREALEEADVIVgYKTYLDliEDLLP-----------GKEVISSGMGEeverareALE---LA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 74 DAGRTypVTVrLKGGDPYVFGRGaeeGLALAQA-----GIAFEVVCGISSAIGGLAYAGIPVTHrgytnGFRVYTahsqk 148
Cdd:cd11646 67 LEGKR--VAL-VSSGDPGIYGMA---GLVLELLderwdDIEVEVVPGITAALAAAALLGAPLGH-----DFAVIS----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 149 dvLADL--------NFAELAKTKDtliFLMGL---RS---AMQLVE--KLLACGMEKATPMAICSHVSMPSQKVLTTTLA 212
Cdd:cd11646 131 --LSDLltpwevieKRLRAAAEAD---FVIALynpRSkkrPWQLEKalEILLEHRPPDTPVGIVRNAGREGEEVTITTLG 205
|
250
....*....|....*....
gi 1589195127 213 ELHQKDIDTLSspaIIVIG 231
Cdd:cd11646 206 ELDPEDVDMFT---TVIIG 221
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
1-230 |
8.00e-09 |
|
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: 55.88 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 1 MNKVYLVGAGCGDPALLSLKGKACIEEADCILYDRLIDPSlLSYAKADCKLIYVGKENHKHTMPQ--------------- 65
Cdd:COG2243 2 MGKLYGVGVGPGDPELLTLKAVRALREADVIAYPAKGAGK-ASLAREIVAPYLPPARIVELVFPMttdyealvaawdeaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 66 AMIQKLLvDAGRTypVTVrLKGGDP-------YVFGRgaeeglaLAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGytng 138
Cdd:COG2243 81 ARIAEEL-EAGRD--VAF-LTEGDPslystfmYLLER-------LRERGFEVEVIPGITSFSAAAAALGIPLAEGD---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 139 frvytahsqkDVL----ADLNFAELAK---TKDTLIFLMGLRSAMQLVEKLLACGM-EKAtpmAICSHVSMPSQKVlTTT 210
Cdd:COG2243 146 ----------EPLtvlpGTLLEEELERaldDFDTVVIMKVGRNFPKVREALEEAGLlDRA---WYVERAGMPDERI-VPG 211
|
250 260
....*....|....*....|
gi 1589195127 211 LAELHQKDIDTLSspaIIVI 230
Cdd:COG2243 212 LAEVDIEEAPYFS---LILV 228
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
7-208 |
1.41e-08 |
|
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: 55.21 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 7 VGAGCGDPALLSLKGKACIEEADCILY--DRLIDPSLLSYAKAdcKLIYVGKENHKHTMP---------------QAMIQ 69
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFVpvSKGGEGSAALIIAA--ALLIPDKEIIPLEFPmtkdreeleeawdeaAEEIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 70 KLLvDAGRT--YpVTVrlkgGDP-------YVFGRgaeeglaLAQAGIAFEVVCGISSAIGGLAYAGIPVTHRGytNGFR 140
Cdd:cd11645 79 EEL-KEGKDvaF-LTL----GDPslystfsYLLER-------LRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1589195127 141 VYTAHSQKDVLadlnfAELAKTKDTLIFLMGLRSAMQLVEKLLACGMEKatPMAICSHVSMPSQKVLT 208
Cdd:cd11645 144 ILPATYDEEEL-----EKALENFDTVVLMKVGRNLEEIKELLEELGLLD--KAVYVERCGMEGERIYT 204
|
|
| PRK05990 |
PRK05990 |
precorrin-2 C(20)-methyltransferase; Reviewed |
7-133 |
5.01e-06 |
|
precorrin-2 C(20)-methyltransferase; Reviewed
Pssm-ID: 180341 Cd Length: 241 Bit Score: 47.67 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 7 VGAGCGDPALLSLKGKACIEEADCILY---------DRLIDPSLLSYAKADCKLIY-VGKENHKHTMP-----------Q 65
Cdd:PRK05990 8 LGVGPGDPELLTLKALRLLQAAPVVAYfvakgkkgnAFGIVEAHLSPGQTLLPLVYpVTTEILPPPLCyetviadfydtS 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1589195127 66 AMIQKLLVDAGRTYPVtvrLKGGDPYVFGRGAEEGLALAQAGIAfEVVCGISSAIGGLAYAGIPVTHR 133
Cdd:PRK05990 88 AEAVAAHLDAGRDVAV---ICEGDPFFYGSYMYLHDRLAPRYET-EVIPGVCSMLGCWSVLGAPLVYR 151
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
302-364 |
1.31e-05 |
|
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyzes the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as Swiss:Q59294 with pfam00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 426866 [Multi-domain] Cd Length: 230 Bit Score: 46.54 E-value: 1.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589195127 302 VVFTSAQVVHILMKQLQEAGFDSriLYQCKLCVMGKGTKKALAQYGLCADLMPNIHDSKHMAE 364
Cdd:pfam02602 170 VTFTSPSTVRNLLELLKDEGLDW--LKSVKAAAIGPTTAEALKELGLKVDVVAERPTMEALVA 230
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
4-231 |
5.48e-05 |
|
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: 44.60 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 4 VYLVGAGCGDPALLSLKGKACIEEADCI----LYDRLIDPsLLSyakadckliyvGKENHKHTMPQ----AMIQKLLVDA 75
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIvgykTYLDLIED-LIP-----------GKEVVTSGMREeiarAELAIELAAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 76 GRTYPVtvrLKGGDPYVFGRGAE--EGLALAQAGIAFEVVCGISSAIGGLAYAGIPVTHRgytngfrvYTAHSQKDVLAD 153
Cdd:TIGR01466 69 GRTVAL---VSSGDPGIYGMAALvfEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHD--------FCVISLSDLLTP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 154 LNFAE----LAKTKDTLIFLM---------GLRSAMQLVekLLACGMEkaTPMAICSHVSMPSQKVLTTTLAELHQKDID 220
Cdd:TIGR01466 138 WPEIEkrlrAAAEADFVIAIYnprskrrpeQFRRAMEIL--LEHRKPD--TPVGIVRNAGREGEEVEITTLAELDEELID 213
|
250
....*....|.
gi 1589195127 221 TLSspaIIVIG 231
Cdd:TIGR01466 214 MLT---TVIIG 221
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
266-352 |
8.16e-05 |
|
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III synthase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 441195 Cd Length: 229 Bit Score: 44.12 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 266 AKLLREQGAWCEEVQCgYcKAIAHTWTKEAF------QSFTHVVFTSAQVVHILMKQLQEAGfdSRILYQCKLCVMGKGT 339
Cdd:COG1587 141 AETLRAAGAEVDEVEV-Y-RTVPPDDLPEELlealaaGEIDAVLFTSPSTVRNLLELAPDAG--LAALARVRIAAIGPRT 216
|
90
....*....|...
gi 1589195127 340 KKALAQYGLCADL 352
Cdd:COG1587 217 AEAARELGLKVVI 229
|
|
| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
3-231 |
1.46e-04 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 43.23 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 3 KVYLVGAGCGDPALLSLKGKACIEEADCIL----YDRLIDpSLLSyakadckliyvGKENHKHTMPQAMIQ-KLLVDAGR 77
Cdd:PRK05765 3 KLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgyntYLRLIS-DLLD-----------GKEVIGARMKEEIFRaNTAIEKAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 78 TYPVTVRLKGGDPYVFGRGAEEGLALAQAGIA--FEVVCGISSAIGGLAYAGIPVthrgyTNGFRVYtahSQKDVL---- 151
Cdd:PRK05765 71 EGNIVALVSSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGSPL-----SLDFVVI---SLSDLLipre 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589195127 152 ADLNFAELAKTKDTLIFLMG------LRSAMQLVEKLlacgMEKATPMAICSHVSMPSQKVLTTTLAELhQKDIDTLSSP 225
Cdd:PRK05765 143 EILHRVTKAAEADFVIVFYNpinenlLIEVMDIVSKH----RKPNTPVGLVKSAYRNNENVVITTLSSW-KEHMDEIGMT 217
|
....*.
gi 1589195127 226 AIIVIG 231
Cdd:PRK05765 218 TTMIIG 223
|
|
| |
