|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
2-248 |
1.32e-134 |
|
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: 389.05 E-value: 1.32e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 2 TGLVYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEGK 81
Cdd:COG0007 1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 82 IVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAvsGIHWEGL 161
Cdd:COG0007 81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKL--DLDWAAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 162 ATAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLRE 241
Cdd:COG0007 159 ARPGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALRE 238
|
....*..
gi 497347455 242 QLQWFDN 248
Cdd:COG0007 239 KLSWFEA 245
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
1-246 |
4.78e-127 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 369.93 E-value: 4.78e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEG 80
Cdd:PRK06136 1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 81 KIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSGIHWEG 160
Cdd:PRK06136 81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLEPEVNWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 161 LATAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLR 240
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALR 240
|
....*.
gi 497347455 241 EQLQWF 246
Cdd:PRK06136 241 AKLAWF 246
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
8-237 |
1.26e-121 |
|
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: 355.21 E-value: 1.26e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 8 IGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEGKIVARLK 87
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 88 GGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSgiHWEGLATAVDT 167
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPD--DDAALARPGGT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 168 LCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVV 237
Cdd:cd11642 159 LVIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
5-240 |
2.67e-111 |
|
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273643 Cd Length: 236 Bit Score: 329.57 E-value: 2.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEGKIVA 84
Cdd:TIGR01469 2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 85 RLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSgIHWEGLATA 164
Cdd:TIGR01469 82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALE-VDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497347455 165 VDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLR 240
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
256-498 |
9.25e-68 |
|
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: 217.56 E-value: 9.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 256 IVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLLHgVDRYSCVVFTSAEGVRYFFDALygEGKDARSLG 335
Cdd:cd06578 1 VLVTRPRPQADELAALLEALGAEVLELPLIEIEPLDDAELDAALAD-LDEYDWLIFTSPNAVEAFFEAL--EELGLRALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 336 YAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQHVKPRHTVLLIQPKKAREVIPRELRHLDIDVDILRLYETQ 415
Cdd:cd06578 78 GLKIAAVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQDGKGKRILRPRGGRAREDLAEALRERGAEVDEVEVYRTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 416 QDTSQQEALvDALQHGHVDYITFTSSSTVTNTLDLLGEDALSLLEHTKIACIGPITAATAMSAGLKVDIISPVYTTEGLV 495
Cdd:cd06578 158 PPDLDAELL-ELLEEGAIDAVLFTSPSTVRNLLELLGKEGRALLKNVKIAAIGPRTAEALRELGLKVVIVAESPTLEALL 236
|
...
gi 497347455 496 DTI 498
Cdd:cd06578 237 EAL 239
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
251-484 |
2.07e-67 |
|
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: 216.31 E-value: 2.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 251 LFGKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLLHGVDRYSCVVFTSAEGVRYFFDALYGEGkd 330
Cdd:COG1587 1 LAGKRVLVTRPAPQAEELAALLEALGAEVVELPLIEIEPLPDPAALRAALERLGDYDWVIFTSANAVRAFFEALEELG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 331 aRSLGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQHvkPRHTVLLIQPKKAREVIPRELRHLDIDVDILR 410
Cdd:COG1587 79 -LRLAGLKIAAVGPKTAAALRAAGLKVDLVPEGFTSEGLLELLQAL--AGKRVLIPRGDGGREDLAETLRAAGAEVDEVE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497347455 411 LYETQQDTSQQEALVDALQHGHVDYITFTSSSTVTNTLDLLGEDALSLLEHTKIACIGPITAATAMSAGLKVDI 484
Cdd:COG1587 156 VYRTVPPDDLPEELLEALAAGEIDAVLFTSPSTVRNLLELAPDAGLAALARVRIAAIGPRTAEAARELGLKVVI 229
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
275-496 |
3.10e-62 |
|
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: 202.94 E-value: 3.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 275 QGANVIQAAAIKTEPVELFDEDKRLLHGVDRYSCVVFTSAEGVRYFFDALYGEGKDARSLGYAKVCAIGSATAKALTNYG 354
Cdd:pfam02602 9 LGAEPLELPLIEIVPPEDRAELDEALKDLGEYDWLIFTSANAVRAFFEALKLEGEDLRALANIKIAAVGPKTARALREAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 355 ITPDIIPVD-YKAESVVDALKQHVKPRHtVLLIQPKKAREVIPRELRHLDIDVDILRLYETQQDTSQQEALVDALQHGHV 433
Cdd:pfam02602 89 LTPDFVPSEeGTAEGLAEELAELLAGKR-VLLLRGNIGRDDLAEALRERGAEVTEVVVYRTVPPEELPEELREALKDGEI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497347455 434 DYITFTSSSTVTNTLDLLGEDALSLLEHTKIACIGPITAATAMSAGLKVDIISPVYTTEGLVD 496
Cdd:pfam02602 168 DAVTFTSPSTVRNLLELLKDEGLDWLKSVKAAAIGPTTAEALKELGLKVDVVAERPTMEALVA 230
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
5-216 |
1.27e-46 |
|
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: 161.36 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIVYD-YLADAHLLEWARPDAElIYAGKQCKDHTMHQWEINELLVAKGKEGKIV 83
Cdd:pfam00590 2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDdSRALEILLDLLPEDLY-FPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 84 ARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVsgihWEGLAT 163
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRL----LEALLA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497347455 164 AVDTLCFVMGVGNLPTIAEKLIAHgRPANTPVALVRWGTKPVQEVLVSTLEHV 216
Cdd:pfam00590 157 NGDTVVLLYGPRRLAELAELLLEL-YPDTTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
253-500 |
1.56e-42 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 151.66 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 253 GKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPV--ELFDEDKRLLHGVDrysCVVFTSAEGVRYFFDALYGEGKd 330
Cdd:PRK05928 1 MMKILVTRPSPKAEELVELLRELGFVALHFPLIEIEPGrqLPQLAAQLAALGAD---WVIFTSKNAVEFLLSALKKKKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 331 aRSLGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQHVKPRHTVLLIQPKKAREVIPRELRHLDIDVDILR 410
Cdd:PRK05928 77 -KWPKNKKYAAIGEKTALALKKLGGKVVFVPEDGESSELLLELPELLLKGKRVLYLRGNGGREVLGDTLEERGAEVDECE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 411 LYETQQDTSQQEALVDALQHGHVDYITFTSSSTVTNTLDLLGED-ALSLLEHTKIACIGPITAATAMSAGLKVDIISPVY 489
Cdd:PRK05928 156 VYERVPPKLDGAELLARLQSGEVDAVIFTSPSTVRAFFSLAPELgRREWLLSCKAVVIGERTAEALRELGIKVIIVPDSA 235
|
250
....*....|.
gi 497347455 490 TTEGLVDTIVK 500
Cdd:PRK05928 236 DNEALLRALKE 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
2-248 |
1.32e-134 |
|
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: 389.05 E-value: 1.32e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 2 TGLVYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEGK 81
Cdd:COG0007 1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 82 IVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAvsGIHWEGL 161
Cdd:COG0007 81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKL--DLDWAAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 162 ATAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLRE 241
Cdd:COG0007 159 ARPGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALRE 238
|
....*..
gi 497347455 242 QLQWFDN 248
Cdd:COG0007 239 KLSWFEA 245
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
1-246 |
4.78e-127 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 369.93 E-value: 4.78e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEG 80
Cdd:PRK06136 1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 81 KIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSGIHWEG 160
Cdd:PRK06136 81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLEPEVNWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 161 LATAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLR 240
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALR 240
|
....*.
gi 497347455 241 EQLQWF 246
Cdd:PRK06136 241 AKLAWF 246
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
8-237 |
1.26e-121 |
|
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: 355.21 E-value: 1.26e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 8 IGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEGKIVARLK 87
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 88 GGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSgiHWEGLATAVDT 167
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPD--DDAALARPGGT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 168 LCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVV 237
Cdd:cd11642 159 LVIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
5-240 |
2.67e-111 |
|
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273643 Cd Length: 236 Bit Score: 329.57 E-value: 2.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEGKIVA 84
Cdd:TIGR01469 2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 85 RLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSgIHWEGLATA 164
Cdd:TIGR01469 82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALE-VDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497347455 165 VDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLR 240
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
|
|
| PRK07168 |
PRK07168 |
uroporphyrin-III C-methyltransferase; |
1-370 |
2.34e-104 |
|
uroporphyrin-III C-methyltransferase;
Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 320.40 E-value: 2.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEG 80
Cdd:PRK07168 1 MNGYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 81 KIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSGIHWEG 160
Cdd:PRK07168 81 KIVVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAKGPLTDHGKYNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 161 LATavDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLR 240
Cdd:PRK07168 161 HNS--DTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGDVVSLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 241 EQLQWFDNKPLFGKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLLHGVDRyscVVFTSAEGVRYF 320
Cdd:PRK07168 239 NQIAWKERKPLHGKKVLFTSATNKTSVMKQKLQEAGAEIYQIPTFKKEEYTLTLEQINEIFNVNR---LVFCSAESVEIL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 497347455 321 FDALYGEGKDARSLgYAKVCAIGSATAKALTNYGITPDiiPVDYKAESVV 370
Cdd:PRK07168 316 MQSCSKYKKDIRSL-QAELQHMNVATQEKLMQYGLLSK--EAKFSSDTTV 362
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
1-245 |
6.58e-99 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 298.85 E-value: 6.58e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEG 80
Cdd:PLN02625 13 GPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSFAEAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 81 KIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVSGIHWEG 160
Cdd:PLN02625 93 KTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTDPLDVAEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 161 LATAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLR 240
Cdd:PLN02625 173 AADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEVVALS 252
|
....*
gi 497347455 241 EQLQW 245
Cdd:PLN02625 253 PLWPW 257
|
|
| cysG |
PRK10637 |
siroheme synthase CysG; |
3-249 |
2.33e-77 |
|
siroheme synthase CysG;
Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 249.67 E-value: 2.33e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 3 GLVYLIGAGPGDSKLITVKGKECIERADVIVYDYLADAHLLEWARPDAELIYAGKQCKDHTMHQWEINELLVAKGKEGKI 82
Cdd:PRK10637 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 83 VARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHedpTKAVSGIHWEGLA 162
Cdd:PRK10637 296 VVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGH---LKTGGELDWENLA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 163 TAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEdvEKAQLKAPAIIVVGDVVNLREQ 242
Cdd:PRK10637 373 AEKQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVSGTLTQLGE--LAQQVNSPSLIIVGRVVGLRDK 450
|
....*..
gi 497347455 243 LQWFDNK 249
Cdd:PRK10637 451 LNWFSNH 457
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
256-498 |
9.25e-68 |
|
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: 217.56 E-value: 9.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 256 IVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLLHgVDRYSCVVFTSAEGVRYFFDALygEGKDARSLG 335
Cdd:cd06578 1 VLVTRPRPQADELAALLEALGAEVLELPLIEIEPLDDAELDAALAD-LDEYDWLIFTSPNAVEAFFEAL--EELGLRALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 336 YAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQHVKPRHTVLLIQPKKAREVIPRELRHLDIDVDILRLYETQ 415
Cdd:cd06578 78 GLKIAAVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQDGKGKRILRPRGGRAREDLAEALRERGAEVDEVEVYRTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 416 QDTSQQEALvDALQHGHVDYITFTSSSTVTNTLDLLGEDALSLLEHTKIACIGPITAATAMSAGLKVDIISPVYTTEGLV 495
Cdd:cd06578 158 PPDLDAELL-ELLEEGAIDAVLFTSPSTVRNLLELLGKEGRALLKNVKIAAIGPRTAEALRELGLKVVIVAESPTLEALL 236
|
...
gi 497347455 496 DTI 498
Cdd:cd06578 237 EAL 239
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
251-484 |
2.07e-67 |
|
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: 216.31 E-value: 2.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 251 LFGKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLLHGVDRYSCVVFTSAEGVRYFFDALYGEGkd 330
Cdd:COG1587 1 LAGKRVLVTRPAPQAEELAALLEALGAEVVELPLIEIEPLPDPAALRAALERLGDYDWVIFTSANAVRAFFEALEELG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 331 aRSLGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQHvkPRHTVLLIQPKKAREVIPRELRHLDIDVDILR 410
Cdd:COG1587 79 -LRLAGLKIAAVGPKTAAALRAAGLKVDLVPEGFTSEGLLELLQAL--AGKRVLIPRGDGGREDLAETLRAAGAEVDEVE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497347455 411 LYETQQDTSQQEALVDALQHGHVDYITFTSSSTVTNTLDLLGEDALSLLEHTKIACIGPITAATAMSAGLKVDI 484
Cdd:COG1587 156 VYRTVPPDDLPEELLEALAAGEIDAVLFTSPSTVRNLLELAPDAGLAALARVRIAAIGPRTAEAARELGLKVVI 229
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
275-496 |
3.10e-62 |
|
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: 202.94 E-value: 3.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 275 QGANVIQAAAIKTEPVELFDEDKRLLHGVDRYSCVVFTSAEGVRYFFDALYGEGKDARSLGYAKVCAIGSATAKALTNYG 354
Cdd:pfam02602 9 LGAEPLELPLIEIVPPEDRAELDEALKDLGEYDWLIFTSANAVRAFFEALKLEGEDLRALANIKIAAVGPKTARALREAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 355 ITPDIIPVD-YKAESVVDALKQHVKPRHtVLLIQPKKAREVIPRELRHLDIDVDILRLYETQQDTSQQEALVDALQHGHV 433
Cdd:pfam02602 89 LTPDFVPSEeGTAEGLAEELAELLAGKR-VLLLRGNIGRDDLAEALRERGAEVTEVVVYRTVPPEELPEELREALKDGEI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497347455 434 DYITFTSSSTVTNTLDLLGEDALSLLEHTKIACIGPITAATAMSAGLKVDIISPVYTTEGLVD 496
Cdd:pfam02602 168 DAVTFTSPSTVRNLLELLKDEGLDWLKSVKAAAIGPTTAEALKELGLKVDVVAERPTMEALVA 230
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
5-216 |
1.27e-46 |
|
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: 161.36 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIVYD-YLADAHLLEWARPDAElIYAGKQCKDHTMHQWEINELLVAKGKEGKIV 83
Cdd:pfam00590 2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDdSRALEILLDLLPEDLY-FPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 84 ARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGHEDPTKAVsgihWEGLAT 163
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRL----LEALLA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497347455 164 AVDTLCFVMGVGNLPTIAEKLIAHgRPANTPVALVRWGTKPVQEVLVSTLEHV 216
Cdd:pfam00590 157 NGDTVVLLYGPRRLAELAELLLEL-YPDTTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
5-241 |
1.71e-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: 162.11 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIVY-DYLADAHLLEWARPDAELIYAGkqckdhTMHQWEINELLVAKGKEGKIV 83
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAEVVNSA------GMSLEEIVDIMSDAHREGKDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 84 ARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFaVVTGHEDPTKAVSGIHWEGLAT 163
Cdd:TIGR01465 75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTV-ILTRASGRTPMPEGEKLADLAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497347455 164 AVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVNLRE 241
Cdd:TIGR01465 154 HGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDPRI 231
|
|
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
1-238 |
5.16e-46 |
|
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: 161.00 E-value: 5.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVY-DYLADAHLLEWARPDAELIYAGKqckdhtMHQWEINELLVAKGKE 79
Cdd:COG2875 1 MKGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIVDSAS------MTLEEIIALMKEAAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 80 GKIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAG----IP-VTQramatsFAVVTGHEDPTKAVS 154
Cdd:COG2875 75 GKDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGreltLPeVSQ------TVILTRAEGRTPMPE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 155 GIHWEGLATAVDTLCFVMGVGNLPTIAEKLIAHgRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVG 234
Cdd:COG2875 149 GESLASLAAHGATLAIYLSAHRIDEVVEELLEG-YPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVG 227
|
....
gi 497347455 235 DVVN 238
Cdd:COG2875 228 PALG 231
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
8-238 |
1.07e-45 |
|
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.
Pssm-ID: 381168 [Multi-domain] Cd Length: 225 Bit Score: 159.10 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 8 IGAGPGDSKLITVKGKECIERADVIVY-DYLADAHLLEWARPDAELIyagkqckD-HTMHQWEINELLVAKGKEGKIVAR 85
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV-------DsAGMTLEEIIEVMREAAREGKDVVR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 86 LKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAG----IP-VTQRAMATSFAVVTGHEDPTKAvsgihwEG 160
Cdd:cd11641 74 LHTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGteltLPeVSQTVILTRLEGRTPVPEGESL------RE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497347455 161 LATAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGDVVN 238
Cdd:cd11641 148 LAKHGATLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
253-500 |
1.56e-42 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 151.66 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 253 GKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPV--ELFDEDKRLLHGVDrysCVVFTSAEGVRYFFDALYGEGKd 330
Cdd:PRK05928 1 MMKILVTRPSPKAEELVELLRELGFVALHFPLIEIEPGrqLPQLAAQLAALGAD---WVIFTSKNAVEFLLSALKKKKL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 331 aRSLGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQHVKPRHTVLLIQPKKAREVIPRELRHLDIDVDILR 410
Cdd:PRK05928 77 -KWPKNKKYAAIGEKTALALKKLGGKVVFVPEDGESSELLLELPELLLKGKRVLYLRGNGGREVLGDTLEERGAEVDECE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 411 LYETQQDTSQQEALVDALQHGHVDYITFTSSSTVTNTLDLLGED-ALSLLEHTKIACIGPITAATAMSAGLKVDIISPVY 489
Cdd:PRK05928 156 VYERVPPKLDGAELLARLQSGEVDAVIFTSPSTVRAFFSLAPELgRREWLLSCKAVVIGERTAEALRELGIKVIIVPDSA 235
|
250
....*....|.
gi 497347455 490 TTEGLVDTIVK 500
Cdd:PRK05928 236 DNEALLRALKE 246
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
5-235 |
4.42e-33 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 126.41 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIVY-DYLADAHLLEWARPDAEliyagkqCKDHT-MHQWEINELLVAKGKEGKI 82
Cdd:PRK15473 10 VWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAE-------CHDSAeLHLEQIIDLMEAGVKAGKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 83 VARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFaVVTGHEDPTKAVSGIHWEGLA 162
Cdd:PRK15473 83 VVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSL-IITRMEGRTPVPAREQLESFA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497347455 163 TAVDTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKAPAIIVVGD 235
Cdd:PRK15473 162 SHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGN 234
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
8-234 |
8.08e-30 |
|
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: 116.34 E-value: 8.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 8 IGAGPGDSKLITVKGKECIERADVIVYDYlaDAHLLEWARPDAELIyAGKQC--KDHTMHQWEINELLVAKGKEGKIVAR 85
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAED--KDSKLLSLVLRAILK-DGKRIydLHDPNVEEEMAELLLEEARQGKDVAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 86 LKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQramatSFAVVTGHEDPTKAvSGIHWEGLATAV 165
Cdd:cd09815 78 LSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGE-----SFLFVTASDLLENP-RLLVLKALAKER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497347455 166 DTLCFVMGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKaQLKAPAIIVVG 234
Cdd:cd09815 152 RHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAERTE-RGKPLTTILVG 219
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
5-234 |
2.12e-28 |
|
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: 113.03 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIVY---------DYLADAHLLEwaRPDAELIYAGKQCKDHTMHQWEINELLVA 75
Cdd:cd11724 2 LYLVGVGPGDPDLITLRALKAIKKADVVFAppdlrkrfaEYLAGKEVLD--DPHGLFTYYGKKCSPLEEAEKECEELEKQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 76 KGK----------EGKIVARLKGGDPLVFGRGgeeaMALREAGVP--FEFVPGVTSPIAAPAYAGIPVTQrAMATSFAVV 143
Cdd:cd11724 80 RAEivqkirealaQGKNVALLDSGDPTIYGPW----IWYLEEFADlnPEVIPGVSSFNAANAALKRSLTG-GGDSRSVIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 144 TGHEDPTKAVSGIhwEGLATAVDTLCFVMGVGNLPTIAEKLiAHGRPANTPVALVRW-GTKPVQEVLVSTLEHVVEDVEK 222
Cdd:cd11724 155 TAPFALKENEDLL--EDLAATGDTLVIFMMRLDLDELVEKL-KKHYPPDTPVAIVYHaGYSEKEKVIRGTLDDILEKLGG 231
|
250
....*....|..
gi 497347455 223 AQLKAPAIIVVG 234
Cdd:cd11724 232 EKEPFLGLIYVG 243
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
8-220 |
1.84e-20 |
|
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: 89.87 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 8 IGAGPGDSKLITVKGKECIERADVIVY-------DYLADAHLLEWARPDAELIYAG---KQCKDHTMHQWEIN-ELLVAK 76
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggeGSAALIIAAALLIPDKEIIPLEfpmTKDREELEEAWDEAaEEIAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 77 GKEGKIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRamATSFAVVTGHEDPTKavsgi 156
Cdd:cd11645 81 LKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEG--DESLAILPATYDEEE----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497347455 157 hWEGLATAVDTLCFvMGVG-NLPTIAEKLIAHGRPANtpVALVRWGTKPVQEVLVSTLEHVVEDV 220
Cdd:cd11645 154 -LEKALENFDTVVL-MKVGrNLEEIKELLEELGLLDK--AVYVERCGMEGERIYTDLEELKEEKL 214
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
1-233 |
5.29e-20 |
|
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: 88.62 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVY----------------DYLADAHLLEWA---RPDAELIYAgkqckd 61
Cdd:COG2243 1 MMGKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslareivaPYLPPARIVELVfpmTTDYEALVA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 62 htmhQWEIN-ELLVAKGKEGKIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRamATSF 140
Cdd:COG2243 75 ----AWDEAaARIAEELEAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLAEG--DEPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 141 AVVTGHEDPTKavsgihWEGLATAVDTLCFvMGVG-NLPTIAEKLIAHGRPANtpVALVRWGTKPvQEVLVSTLEhvved 219
Cdd:COG2243 149 TVLPGTLLEEE------LERALDDFDTVVI-MKVGrNFPKVREALEEAGLLDR--AWYVERAGMP-DERIVPGLA----- 213
|
250
....*....|....*.
gi 497347455 220 vEKAQLKAP--AIIVV 233
Cdd:COG2243 214 -EVDIEEAPyfSLILV 228
|
|
| Precorrin_3B_C17_MT |
cd11646 |
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
5-219 |
3.45e-19 |
|
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: 86.70 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIV-YD-YLAdahLLEWARPDAELIYAGkqckdhtMHQwEIN--ELLVAKGKEG 80
Cdd:cd11646 1 LYVVGIGPGSADLMTPRAREALEEADVIVgYKtYLD---LIEDLLPGKEVISSG-------MGE-EVEraREALELALEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 81 KIVARLKGGDPLVFGRGGE--EAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQramatSFAVV------TGHEDPTKA 152
Cdd:cd11646 70 KRVALVSSGDPGIYGMAGLvlELLDERWDDIEVEVVPGITAALAAAALLGAPLGH-----DFAVIslsdllTPWEVIEKR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497347455 153 VSgihwegLATAVDtlcFVMGVGN---------LPTIAEKLIAHgRPANTPVALVRWGTKPVQEVLVSTLEHVVED 219
Cdd:cd11646 145 LR------AAAEAD---FVIALYNprskkrpwqLEKALEILLEH-RPPDTPVGIVRNAGREGEEVTITTLGELDPE 210
|
|
| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
3-235 |
9.20e-19 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 85.61 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 3 GLVYLIGAGPGDSKLITVKGKECIERADVIV-YDYLADAhllewarpdAELIYAGKQCKDHTMHQwEI--NELLVAKGKE 79
Cdd:PRK05765 2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgYNTYLRL---------ISDLLDGKEVIGARMKE-EIfrANTAIEKALE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 80 GKIVARLKGGDPLVFGRGGE--EAMALREAGVPFEFVPGVTSPIAAPAYAGIPvtqraMATSFAVVTGHEDPTKAVSGIH 157
Cdd:PRK05765 72 GNIVALVSSGDPQVYGMAGLvfELISRRKLDVDVEVIPGVTAALAAAARLGSP-----LSLDFVVISLSDLLIPREEILH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 158 WEGLATAVDtlcFVMGVGN-----LPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDVEKAQLKapAIIV 232
Cdd:PRK05765 147 RVTKAAEAD---FVIVFYNpinenLLIEVMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWKEHMDEIGMT--TTMI 221
|
...
gi 497347455 233 VGD 235
Cdd:PRK05765 222 IGN 224
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
3-219 |
1.98e-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: 84.28 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 3 GLVYLIGAGPGDSKLITVKGKECIERADVIVYDY-------LADAHLLEWARPDA----ELIYAGKQCKDHTMHQW-EIN 70
Cdd:TIGR01467 1 GKLYGVGVGPGDPELITVKALEALRSADVIAVPAskkgresLARKIVEDYLKPNDtrilELVFPMTKDRDELEKAWdEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 71 ELLVAKGKEGKIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRamATSFAVVTGHEDPT 150
Cdd:TIGR01467 81 EAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEG--DESLAILPATAGEA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 151 KAVSGIHWeglataVDTlCFVMGVG-NLPTIAEKLIAHGRPANTpvALVRWGTKPvQEVLVSTLEHVVED 219
Cdd:TIGR01467 159 ELEKALAE------FDT-VVLMKVGrNLPQIKEALAKLGRLDAA--VVVERATMP-DEKIVDLVREAIDD 218
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
221-373 |
7.87e-17 |
|
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: 79.66 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 221 EKAQLKAPAIIVVGDVVNLreqLQWFDNKPLFGKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLL 300
Cdd:cd06578 93 REAGLTADFVPEEGDSEGL---LELLELQDGKGKRILRPRGGRAREDLAEALRERGAEVDEVEVYRTVPPDLDAELLELL 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497347455 301 HGVDRySCVVFTSAEGVRYFFDALYGEGKDArsLGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDAL 373
Cdd:cd06578 170 EEGAI-DAVLFTSPSTVRNLLELLGKEGRAL--LKNVKIAAIGPRTAEALRELGLKVVIVAESPTLEALLEAL 239
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
5-220 |
1.11e-16 |
|
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: 79.27 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIV-YD-YLadaHLLEWARPDAELIYAGkqckdhtMHQwEIN--ELLVAKGKEG 80
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIVgYKtYL---DLIEDLIPGKEVVTSG-------MRE-EIAraELAIELAAEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 81 KIVARLKGGDPLVFGRGGE--EAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAvvtgheDPTKAVSGIhw 158
Cdd:TIGR01466 70 RTVALVSSGDPGIYGMAALvfEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHDFCVISLS------DLLTPWPEI-- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 159 EGLATAVDTLCFVMGVGNLP--------TIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVVEDV 220
Cdd:TIGR01466 142 EKRLRAAAEADFVIAIYNPRskrrpeqfRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAELDEEL 211
|
|
| CobJ |
COG1010 |
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ... |
1-219 |
2.55e-16 |
|
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: 78.57 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIV-YD-YLAdahLLEWARPDAELIYAGkqckdhtMHQwEIN--ELLVAK 76
Cdd:COG1010 2 MRGKLYVVGLGPGSAELMTPRARAALAEADVVVgYGtYLD---LIPPLLPGKEVHASG-------MRE-EVEraREALEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 77 GKEGKIVARLKGGDPLVFGRGG---EEAMALREA-GVPFEFVPGVTSPIAAPAYAGIPVTQramatSFAVVTghedptka 152
Cdd:COG1010 71 AAEGKTVAVVSSGDPGVYGMAGlvlEVLEEGGAWrDVEVEVVPGITAAQAAAARLGAPLGH-----DFCVIS-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 153 VSGIH--WE------GLATAVDtlcFVMGVGN---------LPTIAEKLIAHgRPANTPVALVRWGTKPVQEVLVSTLEH 215
Cdd:COG1010 138 LSDLLtpWEviekrlRAAAEAD---FVIALYNprsrkrpwqLERALEILLEH-RPPDTPVGIVRNAGRPDESVTVTTLGE 213
|
....
gi 497347455 216 VVED 219
Cdd:COG1010 214 LDPE 217
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
3-188 |
1.18e-13 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 70.33 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 3 GLVYLIGAGPGDSKLITVKGKECIERADVIV-------YDYLADAHLLEWARPDAELIyagkqCKDHTM--------HQW 67
Cdd:PRK05576 2 GKLYGIGLGPGDPELLTVKAARILEEADVVYapasrkgGGSLALNIVRPYLKEETEIV-----ELHFPMskdeeekeAVW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 68 -EINELLVAKGKEGKIVARLKGGDPLVFGRGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAVVTGH 146
Cdd:PRK05576 77 kENAEEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGDESLAIIPATRE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497347455 147 EDPTKAVSGIhweglatavDTLCFVMGVGNLPTIAEKLIAHG 188
Cdd:PRK05576 157 ALIEQALTDF---------DSVVLMKVYKNFALIEELLEEGY 189
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
253-378 |
1.58e-12 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 67.30 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 253 GKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLLHGVDRYSCVVFTSAEGVRYFFdALYGEGKDAR 332
Cdd:PRK05928 125 GKRVLYLRGNGGREVLGDTLEERGAEVDECEVYERVPPKLDGAELLARLQSGEVDAVIFTSPSTVRAFF-SLAPELGRRE 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 497347455 333 SLGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQHVK 378
Cdd:PRK05928 204 WLLSCKAVVIGERTAEALRELGIKVIIVPDSADNEALLRALKELLK 249
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
383-501 |
4.94e-11 |
|
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: 62.71 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 383 VLLIQPKKAREVIPRELRHLDIDVDILRLYETQQdtSQQEALVDALQH-GHVDYITFTSSSTVTNTLDLLGEDALSLLEH 461
Cdd:cd06578 1 VLVTRPRPQADELAALLEALGAEVLELPLIEIEP--LDDAELDAALADlDEYDWLIFTSPNAVEAFFEALEELGLRALAG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 497347455 462 TKIACIGPITAATAMSAGLKVDIISPVYTTEGLVDTIVKD 501
Cdd:cd06578 79 LKIAAVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQ 118
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
8-188 |
6.83e-11 |
|
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: 61.74 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 8 IGAGPGDSKLITVKGKECIERADVIVYdylADAHLLEWARPDAELIYagkqckdhtMHQWEINELLVAKGKEGKIVARLK 87
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVIG---AKRLLELFPDLGAEKIP---------LPSEDIAELLEEIAEAGKRVVVLA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 88 GGDPLVFgrGGEEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVtQRAmatsfAVVTGHedptkavsGIHWEGLATAV-- 165
Cdd:cd11644 69 SGDPGFY--GIGKTLLRRLGGEEVEVIPGISSVQLAAARLGLPW-EDA-----RLVSLH--------GRDLENLRRALrr 132
|
170 180
....*....|....*....|....*
gi 497347455 166 -DTLCFVMGVGNLP-TIAEKLIAHG 188
Cdd:cd11644 133 gRKVFVLTDGKNTPaEIARLLLERG 157
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
234-371 |
1.36e-10 |
|
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: 61.18 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 234 GDVVNLREQLQwfdnKPLFGKTIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDED-KRLL--HGVDRyscVV 310
Cdd:pfam02602 99 GTAEGLAEELA----ELLAGKRVLLLRGNIGRDDLAEALRERGAEVTEVVVYRTVPPEELPEElREALkdGEIDA---VT 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497347455 311 FTSAEGVRYFFDALYGEGKDarSLGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVD 371
Cdd:pfam02602 172 FTSPSTVRNLLELLKDEGLD--WLKSVKAAAIGPTTAEALKELGLKVDVVAERPTMEALVA 230
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
5-146 |
4.39e-09 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 56.42 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIV-----YDYLADAHllewaRPDAELIYAGKQckdhtmhqwEINELLVAKGKE 79
Cdd:PRK05787 2 IYIVGIGPGDPEYLTLKALEAIRKADVVVgskrvLELFPELI-----DGEAFVLTAGLR---------DLLEWLELAAKG 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497347455 80 GKIVArLKGGDPLVFGRGGEEaMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQramatsFAVVTGH 146
Cdd:PRK05787 68 KNVVV-LSTGDPLFSGLGKLL-KVRRAVAEDVEVIPGISSVQYAAARLGIDMND------VVFTTSH 126
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
255-479 |
4.23e-08 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 55.88 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 255 TIVVTRARSQASKFRDMLMNQGANVIQAAAIKTEPVELFDEDKRLLHGVDRYSCVVFTSAEGVRYFFDALYGEGKDArsl 334
Cdd:PRK06975 5 TVVVTRPDGQSAALAAQLAAAGLDVLDFPLLDIAPVADDAPLRAALARLSDYALVVFVSPNAVDRALARLDAIWPHA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 335 gyAKVCAIGSATAKALTNYGITPDIIPV------------DYKAESV---VDALKQHVKPRHtVLLIQPKKAREVIPREL 399
Cdd:PRK06975 82 --LPVAVVGPGSVAALARHGIAAPAHRViapdapadggeaRYDSEALfaeIDAAFGALAGKR-VLIVRGDGGREWLAERL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 400 RHLDIDVDILRLYE---TQQDTSQQEAlVDALQHGHVDYITFTSSSTVTNtLDLLGEDALS-----LLEHTKIACIGPIT 471
Cdd:PRK06975 159 REAGAEVELVEAYRrvvPEPSIGAWER-VHALLSGAPHAWLLTSSEAVRN-LDELARAHLNpaeidALKHAPLVAPHARI 236
|
....*...
gi 497347455 472 AATAMSAG 479
Cdd:PRK06975 237 AEQARALG 244
|
|
| PRK05990 |
PRK05990 |
precorrin-2 C(20)-methyltransferase; Reviewed |
1-189 |
4.40e-08 |
|
precorrin-2 C(20)-methyltransferase; Reviewed
Pssm-ID: 180341 Cd Length: 241 Bit Score: 53.84 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVY----------DYLADAHLlewaRPDAE---LIY--AGKQCKDHTMH 65
Cdd:PRK05990 1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYfvakgkkgnaFGIVEAHL----SPGQTllpLVYpvTTEILPPPLCY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 66 QWEIN-------ELLVAKGKEGKIVARLKGGDPLVFGrggeEAMAL--REAG-VPFEFVPGVTSPIAAPAYAGIPVTQRa 135
Cdd:PRK05990 77 ETVIAdfydtsaEAVAAHLDAGRDVAVICEGDPFFYG----SYMYLhdRLAPrYETEVIPGVCSMLGCWSVLGAPLVYR- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497347455 136 mATSFAVVTG---HEDPTkavsgihwEGLATAvdTLCFVMGVG-NLPTIAEKLIAHGR 189
Cdd:PRK05990 152 -NQSLSVLSGvlpEEELR--------RRLADA--DAAVIMKLGrNLDKVRRVLAALGL 198
|
|
| PRK05948 |
PRK05948 |
precorrin-2 C(20)-methyltransferase; |
1-132 |
6.17e-08 |
|
precorrin-2 C(20)-methyltransferase;
Pssm-ID: 180320 Cd Length: 238 Bit Score: 53.49 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERADVIVYDY-------LADAHLLEWARPDAE---LIYAGKQCKDHTMHQW-EI 69
Cdd:PRK05948 2 TLGTLYGISVGPGDPELITLKGLRLLQSAPVVAFPAglagqpgLAEQIIAPWLSPQQIklpLYFPYVQDEEQLEQAWqAA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497347455 70 NELLVAKGKEGKIVARLKGGDPLVFGRGGEEAMALRE--AGVPFEFVPGVTSPIAAPAYAGIPVT 132
Cdd:PRK05948 82 ADQVWHYLEQGEDVAFACEGDVSFYSTFTYLAQTLQElyPQVAIQTIPGVCSPLAAAAALGIPLT 146
|
|
| PRK07239 |
PRK07239 |
bifunctional uroporphyrinogen-III synthetase/response regulator domain protein; Validated |
247-487 |
9.58e-08 |
|
bifunctional uroporphyrinogen-III synthetase/response regulator domain protein; Validated
Pssm-ID: 235981 [Multi-domain] Cd Length: 381 Bit Score: 54.21 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 247 DNKPLFGKTIVVTRARsQASKFRDMLMNQGANVIQAAAIKTEPV----ELFDEDKRLL-HGVDrysCVVFTSAEGVRYFF 321
Cdd:PRK07239 5 DSAPLAGFTVGVTAAR-RAEELAALLERRGARVVHAPALRIVPLadddELRAATRALIaAPPD---IVVATTGIGFRGWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 322 DAL--YGEGKDARS-LGYAKVCAIGSATAKALTNYGITPDIIPVDYKAESVVDALKQH--VKPRHTVLLIQPKKAREVIP 396
Cdd:PRK07239 81 EAAdgWGLADELLEaLSSARLLARGPKATGAIRAAGLREEWSPASESSAEVLEYLLEEgvAGKRIAVQLHGATDEWEPLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 397 R---ELRHLDIDVDILRLY--ETQQDTSQQEALVDALQHGHVDYITFTSSSTVTNTLDLLGE-----DALSLLEHTKIA- 465
Cdd:PRK07239 161 EfleALRAAGAEVVPVPVYrwVPPPDPGPLDRLVDAIASRGLDAVTFTSAPAVAALLERAREmglldQLLAALRTDVLAa 240
|
250 260
....*....|....*....|..
gi 497347455 466 CIGPITAATAMSAGlkVDIISP 487
Cdd:PRK07239 241 CVGPVTAAPLVRAG--VPTSAP 260
|
|
| cbiH |
PRK15478 |
precorrin-3B C(17)-methyltransferase; |
4-213 |
2.49e-07 |
|
precorrin-3B C(17)-methyltransferase;
Pssm-ID: 185375 [Multi-domain] Cd Length: 241 Bit Score: 51.81 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 4 LVYLIGAGPGDSKLITVKGKECIERADVIVyDYLADAHLLEWARPDAELIYAGkQCKdhtmhqwEINELLVA--KGKEGK 81
Cdd:PRK15478 1 MLSVIGIGPGSQAMMTMEAIEALQAAEIVV-GYKTYTHLVKAFTGDKQVIKTG-MCK-------EIERCQAAieLAQAGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 82 IVARLKGGDPLVFGRGG--EEAMALREAGVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFA-VVTGHEDPTKAVSGIhw 158
Cdd:PRK15478 72 NVALISSGDAGIYGMAGlvLELVSKQKLDVEVRLIPGMTASIAAASLLGAPLMHDFCHISLSdLLTPWPVIEKRIVAA-- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497347455 159 eglATAVDTLCFV----MGVGNLPTIAEKLIAHGRPANTPVALVRWGTKPVQEVLVSTL 213
Cdd:PRK15478 150 ---GEADFVICFYnprsRGREGHLARAFDLLAASKSAQTPVGVVKSAGRKKEEKWLTTL 205
|
|
| PRK05752 |
PRK05752 |
uroporphyrinogen-III synthase; Validated |
287-412 |
4.95e-07 |
|
uroporphyrinogen-III synthase; Validated
Pssm-ID: 235590 Cd Length: 255 Bit Score: 50.87 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 287 TEPVELFDEDKRLLHGVDRYSCVVFTSAEGVRYFFDALYGEGKDARSLGYakvCAIGSATAKALTNYGITPDIIPVDYKA 366
Cdd:PRK05752 37 IEPLPETPEQRALLLELDRYCAVIVVSKPAARLGLELLDRYWPQPPQQPW---FSVGAATAAILQDYGLDVSYPEQGDDS 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 497347455 367 ESVVD--ALKQHVK-PRHTVLLIQPKKAREVIPRELRHLDIDVDILRLY 412
Cdd:PRK05752 114 EALLAlpALRQALAvPDPRVLIMRGEGGRELLAERLREQGASVDYLELY 162
|
|
| PRK05991 |
PRK05991 |
precorrin-3B C17-methyltransferase; Provisional |
1-231 |
6.78e-06 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 180342 [Multi-domain] Cd Length: 250 Bit Score: 47.43 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 1 MTGLVYLIGAGPGDSKLITVKGKECIERA-DVIVYD-YLADAHLlewaRPDaeliyagkQCKDHTMHQWEIN--ELLVAK 76
Cdd:PRK05991 1 MSGRLFVIGTGPGNPEQMTPEALAAVEAAtDFFGYGpYLDRLPL----RAD--------QLRHASDNREELDraGAALAM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 77 GKEGKIVARLKGGDPLVFGRggeeAMALREA---------GVPFEFVPGVTSPIAAPAYAGIPVTQRAMATSFAvvtghe 147
Cdd:PRK05991 69 AAAGANVCVVSGGDPGVFAM----AAAVCEAiengpaawrAVDLTIVPGVTAMLAVAARIGAPLGHDFCAISLS------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 148 DPTKAVSGIHWEGLATAvdTLCFVMGVGNLPTIAE--------KLIAHGRPANTPVALVRWGTKPVQEVLVSTLEHVveD 219
Cdd:PRK05991 139 DNLKPWELIEKRLRLAA--EAGFVIALYNPISRARpwqlgeafDLLREHLPATVPVIFGRAAGRPDERIAVAPLAEA--D 214
|
250
....*....|..
gi 497347455 220 VEKAQLKAPAII 231
Cdd:PRK05991 215 ASMADMATCVII 226
|
|
| CobL |
COG2241 |
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ... |
5-188 |
1.52e-05 |
|
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441842 [Multi-domain] Cd Length: 207 Bit Score: 45.91 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 5 VYLIGAGPGDSKLITVKGKECIERADVIV-----YDYLAD--AHLLEWARPDAELIyagkqckdhtmhqweinELLVAKG 77
Cdd:COG2241 4 LTVVGIGPGGPDGLTPAAREAIAEADVVVggkrhLELFPDlgAERIVWPSPLSELL-----------------EELLALL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 78 KEGKIVArLKGGDPLVFGRGGeeamALRE--AGVPFEFVPGVTSPIAAPAYAGIPVtQRAmatsfAVVTGHedptkavsG 155
Cdd:COG2241 67 RGRRVVV-LASGDPLFYGIGA----TLARhlPAEEVRVIPGISSLQLAAARLGWPW-QDA-----AVVSLH--------G 127
|
170 180 190
....*....|....*....|....*....|....*..
gi 497347455 156 IHWEGLATAV---DTLCFVMGVGNLP-TIAEKLIAHG 188
Cdd:COG2241 128 RPLERLLPALapgRRVLVLTDDGNTPaAIARLLLERG 164
|
|
| PRK09189 |
PRK09189 |
uroporphyrinogen-III synthase; Validated |
312-494 |
5.12e-05 |
|
uroporphyrinogen-III synthase; Validated
Pssm-ID: 169701 Cd Length: 240 Bit Score: 44.65 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 312 TSAEGVRyffdALYGEGKDARSLGYAKVCAIGSATAKALTNYGITpDIIPVDYKAESVVDALKQHVKPRHTVLLIQPKKA 391
Cdd:PRK09189 55 TSAEAVR----HLAALGERLLPHLALPLFAVGEATAEAARELGFR-HVIEGGGDGVRLAETVAAALAPTARLLYLAGRPR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 392 REVIPRELRHLDIDVDILRLYETQQDTSQQEALVDALQHGHVDYITFTSSSTVTNTLDLLGED-ALSLLEHTKIACIGPI 470
Cdd:PRK09189 130 APVFEDRLAAAGIPFRVAECYDMLPVMYSPATLSAILGGAPFDAVLLYSRVAARRFFALMRLSiAPPADEKTRFLCLSAR 209
|
170 180
....*....|....*....|....*
gi 497347455 471 TAAtAMSAGLKVDI-ISPVYTTEGL 494
Cdd:PRK09189 210 VAA-ALPASLRAQAlIAAMPDEKSL 233
|
|
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
6-92 |
5.01e-04 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 41.87 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 6 YLIGAGPGDSKLITVKGKECIERADVIvydYL-ADAHLLEWARPDAELIYAGKQCK--DHTMHQWEINELLvAKGKEgKI 82
Cdd:PTZ00175 4 YIIGLGLGDEKDITVKGLEAVKSADVV---YLeSYTSILINSNKEKLEEFYGKPVIeaDREMVEEGCDEIL-EEAKE-KN 78
|
90
....*....|
gi 497347455 83 VARLKGGDPL 92
Cdd:PTZ00175 79 VAFLVVGDPF 88
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
6-117 |
1.27e-03 |
|
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: 40.48 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497347455 6 YLIGAGPGDSKLITVKGKECIERADVIVYD-YLADahLLEWARPDAELIYaGKQCK--DHTMHQWEINELLvAKGKEGKi 82
Cdd:cd11647 3 YLIGLGLGDEKDITLEGLEALKKADKVYLEaYTSI--LPGSKLEELEKLI-GKKIIllDREDLEEESEEIL-EEAKKKD- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 497347455 83 VARLKGGDPLVfgrggeeA---MALR----EAGVPFEFVPGV 117
Cdd:cd11647 78 VALLVPGDPLI-------AtthIDLRleakKRGIKVKVIHNA 112
|
|
| |
