|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
3-246 |
5.41e-136 |
|
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: 392.51 E-value: 5.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 3 GKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKI 82
Cdd:COG0007 2 GKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 83 VTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGAELNWKSISSL 162
Cdd:COG0007 82 VVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALARP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 163 EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLRDKLN 242
Cdd:COG0007 162 GGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALREKLS 241
|
....
gi 329126735 243 FFEN 246
Cdd:COG0007 242 WFEA 245
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
8-235 |
4.06e-120 |
|
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: 351.35 E-value: 4.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 8 VGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKIVTRLK 87
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 88 GGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGAELNWKSISSLEGTLV 167
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329126735 168 FLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVV 235
Cdd:cd11642 161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
4-238 |
4.65e-117 |
|
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: 343.82 E-value: 4.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 4 KVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKIV 83
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 84 TRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGA-ELNWKSISSL 162
Cdd:TIGR01469 81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKAlEVDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 329126735 163 EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLR 238
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
1-245 |
1.70e-108 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 322.55 E-value: 1.70e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTG 80
Cdd:PRK06136 1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 81 KIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGA--ELNWKS 158
Cdd:PRK06136 81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLepEVNWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 159 ISSLEGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLR 238
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALR 240
|
....*..
gi 329126735 239 DKLNFFE 245
Cdd:PRK06136 241 AKLAWFE 247
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
266-493 |
3.23e-75 |
|
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: 236.45 E-value: 3.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 266 LVERIIELGGNPIEVPAIKIEEIPSNVELDNGIEYINEFNYLIFTSRNAVKIFFERLFELNFDSRKLGNLKVVAIGTGTS 345
Cdd:pfam02602 2 LAELLEALGAEPLELPLIEIVPPEDRAELDEALKDLGEYDWLIFTSANAVRAFFEALKLEGEDLRALANIKIAAVGPKTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 346 DELRHYGIIPDVLPKK-FVAESVVELLKEVLQKeDKVFIPRSSEARTYLVEELNKL-CNVTEVKIYNTIKGSGNKDDIIN 423
Cdd:pfam02602 82 RALREAGLTPDFVPSEeGTAEGLAEELAELLAG-KRVLLLRGNIGRDDLAEALRERgAEVTEVVVYRTVPPEELPEELRE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 424 LLNNKNIDYITFTSSSTVKNFIEIMGKQNIEKLKDTKLVSIGPITSKTIEDFGLKVYNEAEEYTIEGIIK 493
Cdd:pfam02602 161 ALKDGEIDAVTFTSPSTVRNLLELLKDEGLDWLKSVKAAAIGPTTAEALKELGLKVDVVAERPTMEALVA 230
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
249-479 |
5.26e-74 |
|
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: 233.26 E-value: 5.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 249 LFGKNIVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPSNVELDNGIEYINEFNYLIFTSRNAVKIFFERLFELNFD 328
Cdd:COG1587 1 LAGKRVLVTRPAPQAEELAALLEALGAEVVELPLIEIEPLPDPAALRAALERLGDYDWVIFTSANAVRAFFEALEELGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 329 srkLGNLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELLKEVlqKEDKVFIPRSSEARTYLVEELNKL-CNVTEVK 407
Cdd:COG1587 81 ---LAGLKIAAVGPKTAAALRAAGLKVDLVPEGFTSEGLLELLQAL--AGKRVLIPRGDGGREDLAETLRAAgAEVDEVE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 329126735 408 IYNTIKGSGNKDDIINLLNNKNIDYITFTSSSTVKNFIEIMGKQNIEKLKDTKLVSIGPITSKTIEDFGLKV 479
Cdd:COG1587 156 VYRTVPPDDLPEELLEALAAGEIDAVLFTSPSTVRNLLELAPDAGLAALARVRIAAIGPRTAEAARELGLKV 227
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
254-495 |
1.06e-72 |
|
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: 230.27 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 254 IVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEiPSNVELDNGIEYINEFNYLIFTSRNAVKIFFERLFELNfdSRKLG 333
Cdd:cd06578 1 VLVTRPRPQADELAALLEALGAEVLELPLIEIEP-LDDAELDAALADLDEYDWLIFTSPNAVEAFFEALEELG--LRALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 334 NLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELLKEVLQKEDKVFIPRSSEARTYLVEELNKL-CNVTEVKIYNTI 412
Cdd:cd06578 78 GLKIAAVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQDGKGKRILRPRGGRAREDLAEALRERgAEVDEVEVYRTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 413 KGSGNkDDIINLLNNKNIDYITFTSSSTVKNFIEIMGKQNIEKLKDTKLVSIGPITSKTIEDFGLKVYNEAEEYTIEGII 492
Cdd:cd06578 158 PPDLD-AELLELLEEGAIDAVLFTSPSTVRNLLELLGKEGRALLKNVKIAAIGPRTAEALRELGLKVVIVAESPTLEALL 236
|
...
gi 329126735 493 KTL 495
Cdd:cd06578 237 EAL 239
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
4-214 |
1.08e-45 |
|
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: 158.66 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 4 KVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKIV 83
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 84 TRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDyASSFHVITGHLKEEGAELnWKSISSLE 163
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGG-EVLSVLFLPGLARIELRL-LEALLANG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 329126735 164 GTLVFLMGVSNLKNICNsLIKEGKNKFTKAAIINWASTTKQKVVVGNLENI 214
Cdd:pfam00590 159 DTVVLLYGPRRLAELAE-LLLELYPDTTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
251-497 |
9.51e-44 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 154.74 E-value: 9.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 251 GKNIVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPsNVELDNGIEYINEFNYLIFTSRNAVKIFFERLfeLNFDSR 330
Cdd:PRK05928 1 MMKILVTRPSPKAEELVELLRELGFVALHFPLIEIEPGR-QLPQLAAQLAALGADWVIFTSKNAVEFLLSAL--KKKKLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 331 KLGNLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELLKEVLQKEDKVFIPRSSEARTYLVEELNKL-CNVTEVKIY 409
Cdd:PRK05928 78 WPKNKKYAAIGEKTALALKKLGGKVVFVPEDGESSELLLELPELLLKGKRVLYLRGNGGREVLGDTLEERgAEVDECEVY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 410 NTIKGSGNKDDIINLLNNKNIDYITFTSSSTVKNFIEIMGKQNIEK-LKDTKLVSIGPITSKTIEDFGLKVYNEAEEYTI 488
Cdd:PRK05928 158 ERVPPKLDGAELLARLQSGEVDAVIFTSPSTVRAFFSLAPELGRREwLLSCKAVVIGERTAEALRELGIKVIIVPDSADN 237
|
....*....
gi 329126735 489 EGIIKTLIR 497
Cdd:PRK05928 238 EALLRALKE 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
3-246 |
5.41e-136 |
|
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: 392.51 E-value: 5.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 3 GKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKI 82
Cdd:COG0007 2 GKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 83 VTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGAELNWKSISSL 162
Cdd:COG0007 82 VVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALARP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 163 EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLRDKLN 242
Cdd:COG0007 162 GGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALREKLS 241
|
....
gi 329126735 243 FFEN 246
Cdd:COG0007 242 WFEA 245
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
8-235 |
4.06e-120 |
|
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: 351.35 E-value: 4.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 8 VGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKIVTRLK 87
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 88 GGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGAELNWKSISSLEGTLV 167
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329126735 168 FLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVV 235
Cdd:cd11642 161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
4-238 |
4.65e-117 |
|
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: 343.82 E-value: 4.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 4 KVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKIV 83
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 84 TRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGA-ELNWKSISSL 162
Cdd:TIGR01469 81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKAlEVDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 329126735 163 EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLR 238
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
1-245 |
1.70e-108 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 322.55 E-value: 1.70e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTG 80
Cdd:PRK06136 1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 81 KIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGA--ELNWKS 158
Cdd:PRK06136 81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLepEVNWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 159 ISSLEGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLR 238
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALR 240
|
....*..
gi 329126735 239 DKLNFFE 245
Cdd:PRK06136 241 AKLAWFE 247
|
|
| PRK07168 |
PRK07168 |
uroporphyrin-III C-methyltransferase; |
1-370 |
9.15e-100 |
|
uroporphyrin-III C-methyltransferase;
Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 308.46 E-value: 9.15e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTG 80
Cdd:PRK07168 1 MNGYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 81 KIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGAELNWKSIS 160
Cdd:PRK07168 81 KIVVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAKGPLTDHGKYNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 161 SLEGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLRDK 240
Cdd:PRK07168 161 HNSDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGDVVSLRNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 241 LNFFENKPLFGKNIVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPSNVEldnGIEYINEFNYLIFTSRNAVKIFFE 320
Cdd:PRK07168 241 IAWKERKPLHGKKVLFTSATNKTSVMKQKLQEAGAEIYQIPTFKKEEYTLTLE---QINEIFNVNRLVFCSAESVEILMQ 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 329126735 321 RLFELNFDSRKLgNLKVVAIGTGTSDELRHYGIIPDvlPKKFVAESVVEL 370
Cdd:PRK07168 318 SCSKYKKDIRSL-QAELQHMNVATQEKLMQYGLLSK--EAKFSSDTTVYL 364
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
1-239 |
1.83e-94 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 287.30 E-value: 1.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTG 80
Cdd:PLN02625 13 GPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSFAEAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 81 KIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGAE--LNWKS 158
Cdd:PLN02625 93 KTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTDplDVAEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 159 ISSLEGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVSLR 238
Cdd:PLN02625 173 AADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEVVALS 252
|
.
gi 329126735 239 D 239
Cdd:PLN02625 253 P 253
|
|
| cysG |
PRK10637 |
siroheme synthase CysG; |
3-247 |
7.41e-86 |
|
siroheme synthase CysG;
Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 271.63 E-value: 7.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 3 GKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKI 82
Cdd:PRK10637 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 83 VTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFHVITGHLKEEGaELNWKSISSL 162
Cdd:PRK10637 296 VVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGG-ELDWENLAAE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 163 EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEkaMAEKISSPSLIVIGEVVSLRDKLN 242
Cdd:PRK10637 375 KQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVSGTLTQLGE--LAQQVNSPSLIIVGRVVGLRDKLN 452
|
....*
gi 329126735 243 FFENK 247
Cdd:PRK10637 453 WFSNH 457
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
266-493 |
3.23e-75 |
|
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: 236.45 E-value: 3.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 266 LVERIIELGGNPIEVPAIKIEEIPSNVELDNGIEYINEFNYLIFTSRNAVKIFFERLFELNFDSRKLGNLKVVAIGTGTS 345
Cdd:pfam02602 2 LAELLEALGAEPLELPLIEIVPPEDRAELDEALKDLGEYDWLIFTSANAVRAFFEALKLEGEDLRALANIKIAAVGPKTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 346 DELRHYGIIPDVLPKK-FVAESVVELLKEVLQKeDKVFIPRSSEARTYLVEELNKL-CNVTEVKIYNTIKGSGNKDDIIN 423
Cdd:pfam02602 82 RALREAGLTPDFVPSEeGTAEGLAEELAELLAG-KRVLLLRGNIGRDDLAEALRERgAEVTEVVVYRTVPPEELPEELRE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 424 LLNNKNIDYITFTSSSTVKNFIEIMGKQNIEKLKDTKLVSIGPITSKTIEDFGLKVYNEAEEYTIEGIIK 493
Cdd:pfam02602 161 ALKDGEIDAVTFTSPSTVRNLLELLKDEGLDWLKSVKAAAIGPTTAEALKELGLKVDVVAERPTMEALVA 230
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
249-479 |
5.26e-74 |
|
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: 233.26 E-value: 5.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 249 LFGKNIVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPSNVELDNGIEYINEFNYLIFTSRNAVKIFFERLFELNFD 328
Cdd:COG1587 1 LAGKRVLVTRPAPQAEELAALLEALGAEVVELPLIEIEPLPDPAALRAALERLGDYDWVIFTSANAVRAFFEALEELGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 329 srkLGNLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELLKEVlqKEDKVFIPRSSEARTYLVEELNKL-CNVTEVK 407
Cdd:COG1587 81 ---LAGLKIAAVGPKTAAALRAAGLKVDLVPEGFTSEGLLELLQAL--AGKRVLIPRGDGGREDLAETLRAAgAEVDEVE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 329126735 408 IYNTIKGSGNKDDIINLLNNKNIDYITFTSSSTVKNFIEIMGKQNIEKLKDTKLVSIGPITSKTIEDFGLKV 479
Cdd:COG1587 156 VYRTVPPDDLPEELLEALAAGEIDAVLFTSPSTVRNLLELAPDAGLAALARVRIAAIGPRTAEAARELGLKV 227
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
254-495 |
1.06e-72 |
|
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: 230.27 E-value: 1.06e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 254 IVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEiPSNVELDNGIEYINEFNYLIFTSRNAVKIFFERLFELNfdSRKLG 333
Cdd:cd06578 1 VLVTRPRPQADELAALLEALGAEVLELPLIEIEP-LDDAELDAALADLDEYDWLIFTSPNAVEAFFEALEELG--LRALA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 334 NLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELLKEVLQKEDKVFIPRSSEARTYLVEELNKL-CNVTEVKIYNTI 412
Cdd:cd06578 78 GLKIAAVGPKTAEALREAGLTADFVPEEGDSEGLLELLELQDGKGKRILRPRGGRAREDLAEALRERgAEVDEVEVYRTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 413 KGSGNkDDIINLLNNKNIDYITFTSSSTVKNFIEIMGKQNIEKLKDTKLVSIGPITSKTIEDFGLKVYNEAEEYTIEGII 492
Cdd:cd06578 158 PPDLD-AELLELLEEGAIDAVLFTSPSTVRNLLELLGKEGRALLKNVKIAAIGPRTAEALRELGLKVVIVAESPTLEALL 236
|
...
gi 329126735 493 KTL 495
Cdd:cd06578 237 EAL 239
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
4-214 |
1.08e-45 |
|
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: 158.66 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 4 KVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRLLKEAKETCEFIYVGKKSSNHTKTQDEINDIIVHKAKTGKIV 83
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDSRALEILLDLLPEDLYFPMTEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 84 TRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDyASSFHVITGHLKEEGAELnWKSISSLE 163
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGG-EVLSVLFLPGLARIELRL-LEALLANG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 329126735 164 GTLVFLMGVSNLKNICNsLIKEGKNKFTKAAIINWASTTKQKVVVGNLENI 214
Cdd:pfam00590 159 DTVVLLYGPRRLAELAE-LLLELYPDTTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
251-497 |
9.51e-44 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 154.74 E-value: 9.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 251 GKNIVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPsNVELDNGIEYINEFNYLIFTSRNAVKIFFERLfeLNFDSR 330
Cdd:PRK05928 1 MMKILVTRPSPKAEELVELLRELGFVALHFPLIEIEPGR-QLPQLAAQLAALGADWVIFTSKNAVEFLLSAL--KKKKLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 331 KLGNLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELLKEVLQKEDKVFIPRSSEARTYLVEELNKL-CNVTEVKIY 409
Cdd:PRK05928 78 WPKNKKYAAIGEKTALALKKLGGKVVFVPEDGESSELLLELPELLLKGKRVLYLRGNGGREVLGDTLEERgAEVDECEVY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 410 NTIKGSGNKDDIINLLNNKNIDYITFTSSSTVKNFIEIMGKQNIEK-LKDTKLVSIGPITSKTIEDFGLKVYNEAEEYTI 488
Cdd:PRK05928 158 ERVPPKLDGAELLARLQSGEVDAVIFTSPSTVRAFFSLAPELGRREwLLSCKAVVIGERTAEALRELGIKVIIVPDSADN 237
|
....*....
gi 329126735 489 EGIIKTLIR 497
Cdd:PRK05928 238 EALLRALKE 246
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
8-235 |
5.96e-39 |
|
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: 140.99 E-value: 5.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 8 VGAGPGDYKLITLKGMECIKKSDVIVY-DRLASSRLLKEAKETCEFIyvgkksSNHTKTQDEINDIIVHKAKTGKIVTRL 86
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV------DSAGMTLEEIIEVMREAAREGKDVVRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 87 KGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFhVIT---GHLKE-EGAELnwKSISSL 162
Cdd:cd11641 75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTV-ILTrleGRTPVpEGESL--RELAKH 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329126735 163 EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVV 235
Cdd:cd11641 152 GATLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPAL 224
|
|
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
1-235 |
1.33e-36 |
|
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: 135.57 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIVY-DRLASSRLLKEAKETCEFIyvgkKSSNhtKTQDEINDIIVHKAKT 79
Cdd:COG2875 1 MKGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIV----DSAS--MTLEEIIALMKEAAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 80 GKIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFhVIT---GHLKEEGAElnw 156
Cdd:COG2875 75 GKDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTV-ILTraeGRTPMPEGE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 157 kSISSL---EGTLVFLMGVSNLKNICNSLIkEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGE 233
Cdd:COG2875 151 -SLASLaahGATLAIYLSAHRIDEVVEELL-EGYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGP 228
|
..
gi 329126735 234 VV 235
Cdd:COG2875 229 AL 230
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
8-232 |
1.68e-31 |
|
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: 120.58 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 8 VGAGPGDYKLITLKGMECIKKSDVIVYDRLASSRL----LKEAKETCEFIYVgkkssNHTKTQDEINDIIVHKAKTGKIV 83
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLLslvlRAILKDGKRIYDL-----HDPNVEEEMAELLLEEARQGKDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 84 TRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHrdyasSFHVITGHLKEEGAEL-NWKSISSL 162
Cdd:cd09815 76 AFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGE-----SFLFVTASDLLENPRLlVLKALAKE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 329126735 163 EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENI-YEKAMAEKIssPSLIVIG 232
Cdd:cd09815 151 RRHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELrAERTERGKP--LTTILVG 219
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
5-239 |
8.29e-30 |
|
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: 117.04 E-value: 8.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 5 VFLVGAGPGDYKLITLKGMECIKKSDVIVY-DRLASSRLLKEAKETCEFIyvgkKSSNhtKTQDEINDIIVHKAKTGKIV 83
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAEVV----NSAG--MSLEEIVDIMSDAHREGKDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 84 TRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFhVITghlKEEGA----ELnwKSI 159
Cdd:TIGR01465 75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTV-ILT---RASGRtpmpEG--EKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 160 SSL---EGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIGEVVS 236
Cdd:TIGR01465 149 ADLakhGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALD 228
|
...
gi 329126735 237 LRD 239
Cdd:TIGR01465 229 PRI 231
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
4-232 |
8.80e-29 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 114.47 E-value: 8.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 4 KVFLVGAGPGDYKLITLKGMECIKKSDVIVY-DRLASSRLLKEAKETCEfiyvgKKSSNHTkTQDEINDIIVHKAKTGKI 82
Cdd:PRK15473 9 CVWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAE-----CHDSAEL-HLEQIIDLMEAGVKAGKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 83 VTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDYASSFhVITghlKEEG-----AELNWK 157
Cdd:PRK15473 83 VVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSL-IIT---RMEGrtpvpAREQLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 329126735 158 SISSLEGTLVFLMGVSNLKNICNSLIKEGKNKFTKAAIINWASTTKQKVVVGNLENIYEKAMAEKISSPSLIVIG 232
Cdd:PRK15473 159 SFASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVG 233
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
4-232 |
1.43e-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: 113.42 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 4 KVFLVGAGPGDYKLITLKGMECIKKSDVIVYD---RLASSRLLKEaKETCE-----FIYVGKKSSNHTKT---------- 65
Cdd:cd11724 1 KLYLVGVGPGDPDLITLRALKAIKKADVVFAPpdlRKRFAEYLAG-KEVLDdphglFTYYGKKCSPLEEAekeceelekq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 66 QDEINDIIVHKAKTGKIVTRLKGGDPYVFGRGG---EEGEYLNkkgvkFEVIPGITS------AIgglcyaGIPITHrDY 136
Cdd:cd11724 80 RAEIVQKIREALAQGKNVALLDSGDPTIYGPWIwylEEFADLN-----PEVIPGVSSfnaanaAL------KRSLTG-GG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 137 ASSFHVITGHLKEEGAELNWKSISSLEGTLVFLMGVSNLKNicnsLIKEGKNKF---TKAAIINWA-STTKQKVVVGNLE 212
Cdd:cd11724 148 DSRSVILTAPFALKENEDLLEDLAATGDTLVIFMMRLDLDE----LVEKLKKHYppdTPVAIVYHAgYSEKEKVIRGTLD 223
|
250 260
....*....|....*....|
gi 329126735 213 NIYEKAMAEKISSPSLIVIG 232
Cdd:cd11724 224 DILEKLGGEKEPFLGLIYVG 243
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
8-231 |
2.24e-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: 89.49 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 8 VGAGPGDYKLITLKGMECIKKSDVIVY-------DRLASSRLLKEAKETCEFIYV----GKKSSNHTKTQDEINDIIVHK 76
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggeGSAALIIAAALLIPDKEIIPLefpmTKDREELEEAWDEAAEEIAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 77 AKTGKIVTRLKGGDP-------YVFgrggeegEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDyaSSFHVITGHLKE 149
Cdd:cd11645 81 LKEGKDVAFLTLGDPslystfsYLL-------ERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLAILPATYDE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 150 EgaelNWKSISSLEGTLVFLMGVSNLKNICNSLIKEGKNKftKAAIINWASTTKQKVVVGNleniyEKAMAEKISSPSLI 229
Cdd:cd11645 152 E----ELEKALENFDTVVLMKVGRNLEEIKELLEELGLLD--KAVYVERCGMEGERIYTDL-----EELKEEKLPYFSLI 220
|
..
gi 329126735 230 VI 231
Cdd:cd11645 221 IV 222
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
1-209 |
1.94e-15 |
|
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: 75.52 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIVY-------DRLASS---RLLKEAKE-TCEFIYvgkkssnhTKTQDEI 69
Cdd:COG2243 1 MMGKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkASLAREivaPYLPPARIvELVFPM--------TTDYEAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 70 ND-------IIVHKAKTGKIVTRLKGGDP-------YVFGRggeegeyLNKKGVKFEVIPGITSAIGGLCYAGIPITHRD 135
Cdd:COG2243 73 VAawdeaaaRIAEELEAGRDVAFLTEGDPslystfmYLLER-------LRERGFEVEVIPGITSFSAAAAALGIPLAEGD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 329126735 136 yaSSFHVITGHLKEEGaelnWKSISSLEGTLVFLMGVSNLKNICNSLIKEGknKFTKAAIINWASTTKQKVVVG 209
Cdd:COG2243 146 --EPLTVLPGTLLEEE----LERALDDFDTVVIMKVGRNFPKVREALEEAG--LLDRAWYVERAGMPDERIVPG 211
|
|
| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
3-144 |
7.39e-14 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 71.35 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 3 GKVFLVGAGPGDYKLITLKGMECIKKSDVIV-YDRLAssRLLKEAKETCEFIyvgkkssnHTKTQDEI--NDIIVHKAKT 79
Cdd:PRK05765 2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgYNTYL--RLISDLLDGKEVI--------GARMKEEIfrANTAIEKALE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 329126735 80 GKIVTRLKGGDPYVFGRGGEEGEYLNKKG--VKFEVIPGITSAIGGLCYAGIPIthrdyASSFHVIT 144
Cdd:PRK05765 72 GNIVALVSSGDPQVYGMAGLVFELISRRKldVDVEVIPGVTAALAAAARLGSPL-----SLDFVVIS 133
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
2-191 |
7.60e-14 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 70.72 E-value: 7.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 2 NGKVFLVGAGPGDYKLITLKGMECIKKSDVIV-------YDRLASS---RLLKEAKE--TCEFIyVGKKSSNHTKTQDEI 69
Cdd:PRK05576 1 MGKLYGIGLGPGDPELLTVKAARILEEADVVYapasrkgGGSLALNivrPYLKEETEivELHFP-MSKDEEEKEAVWKEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 70 NDIIVHKAKTGKIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITS--AIGGLcyAGIPITHRDYASSFHVITGHL 147
Cdd:PRK05576 80 AEEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSftAIASR--AGVPLAMGDESLAIIPATREA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 329126735 148 KEEGAelnwksiSSLEGTLVFLMGVSNLKNIcNSLIKEGKNKFT 191
Cdd:PRK05576 158 LIEQA-------LTDFDSVVLMKVYKNFALI-EELLEEGYLDAL 193
|
|
| Precorrin_3B_C17_MT |
cd11646 |
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
5-138 |
8.04e-12 |
|
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: 65.13 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 5 VFLVGAGPGDYKLITLKGMECIKKSDVIV-YDRLAssRLLKEAKETCEFIyvgkKSSNHtktqDEIN--DIIVHKAKTGK 81
Cdd:cd11646 1 LYVVGIGPGSADLMTPRAREALEEADVIVgYKTYL--DLIEDLLPGKEVI----SSGMG----EEVEraREALELALEGK 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 82 IVTRLKGGDPYVFGRGG---EEGEYLNkKGVKFEVIPGITSAIGGLCYAGIPITHrDYAS 138
Cdd:cd11646 71 RVALVSSGDPGIYGMAGlvlELLDERW-DDIEVEVVPGITAALAAAALLGAPLGH-DFAV 128
|
|
| CobJ |
COG1010 |
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ... |
1-137 |
1.72e-11 |
|
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: 64.32 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIV----Y-DRLA---------SSRLLKE---AKETCEfiyvgkkssnht 63
Cdd:COG1010 2 MRGKLYVVGLGPGSAELMTPRARAALAEADVVVgygtYlDLIPpllpgkevhASGMREEverAREALE------------ 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329126735 64 ktqdeindiivhKAKTGKIVTRLKGGDPYVFGRGG---EEGE-YLNKKGVKFEVIPGITSAIGGLCYAGIPITHrDYA 137
Cdd:COG1010 70 ------------LAAEGKTVAVVSSGDPGVYGMAGlvlEVLEeGGAWRDVEVEVVPGITAAQAAAARLGAPLGH-DFC 134
|
|
| PRK05990 |
PRK05990 |
precorrin-2 C(20)-methyltransferase; Reviewed |
1-150 |
6.01e-10 |
|
precorrin-2 C(20)-methyltransferase; Reviewed
Pssm-ID: 180341 Cd Length: 241 Bit Score: 59.62 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 1 MNGKVFLVGAGPGDYKLITLKGMECIKKSDVIVY----DRLASSR-----LLKEAKETCEFIY--VGKKSSNHTKTQDEI 69
Cdd:PRK05990 1 AKGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYfvakGKKGNAFgiveaHLSPGQTLLPLVYpvTTEILPPPLCYETVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 70 NDIIVHKAKT-------GKIVTRLKGGDPYVFGrggeEGEYLNKK-GVKF--EVIPGITSAIGGLCYAGIPITHRDyaSS 139
Cdd:PRK05990 81 ADFYDTSAEAvaahldaGRDVAVICEGDPFFYG----SYMYLHDRlAPRYetEVIPGVCSMLGCWSVLGAPLVYRN--QS 154
|
170
....*....|.
gi 329126735 140 FHVITGHLKEE 150
Cdd:PRK05990 155 LSVLSGVLPEE 165
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
5-138 |
6.17e-10 |
|
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: 59.62 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 5 VFLVGAGPGDYKLITLKGMECIKKSDVIV-YDRLAssRLLKEAKETCEFIyvgkkSSNHTKTQDEINDIIVhKAKTGKIV 83
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIVgYKTYL--DLIEDLIPGKEVV-----TSGMREEIARAELAIE-LAAEGRTV 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 329126735 84 TRLKGGDPYVFGRGGEEGEYLNKKG--VKFEVIPGITSAIGGLCYAGIPITHrDYAS 138
Cdd:TIGR01466 73 ALVSSGDPGIYGMAALVFEALEKKGaeVDIEVIPGITAASAAASLLGAPLGH-DFCV 128
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
241-371 |
6.38e-10 |
|
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: 59.63 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 241 LNFFENKPLFGKNIVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPSNVELdngIEYINE--FNYLIFTSRNAVKIF 318
Cdd:cd06578 112 LELLELQDGKGKRILRPRGGRAREDLAEALRERGAEVDEVEVYRTVPPDLDAEL---LELLEEgaIDAVLFTSPSTVRNL 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 329126735 319 FERLFELNFDSrkLGNLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELL 371
Cdd:cd06578 189 LELLGKEGRAL--LKNVKIAAIGPRTAEALRELGLKVVIVAESPTLEALLEAL 239
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
4-187 |
1.33e-09 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 57.96 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 4 KVFLVGAGPGDYKLITLKGMECIKKSDVIVydrlASSRLLKEAKE--TCEFIYVGKkssnhtKTQDEINdiIVHKAKTGK 81
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVV----GSKRVLELFPEliDGEAFVLTA------GLRDLLE--WLELAAKGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 82 IVTRLKGGDPYVFGRGGEEGEYlNKKGVKFEVIPGITSAIGGLCYAGIPIThrDYAssfhVITGHLKEEGAELNWKSISS 161
Cdd:PRK05787 69 NVVVLSTGDPLFSGLGKLLKVR-RAVAEDVEVIPGISSVQYAAARLGIDMN--DVV----FTTSHGRGPNFEELEDLLKN 141
|
170 180
....*....|....*....|....*.
gi 329126735 162 LEGTLVFLMGVSNLKNICNSLIKEGK 187
Cdd:PRK05787 142 GRKVIMLPDPRFGPKEIAAELLERGK 167
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
3-187 |
1.60e-09 |
|
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: 58.09 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 3 GKVFLVGAGPGDYKLITLKGMECIKKSDVIVYDRLASSR----------LLKEAKE---TCEFIYVGKKSSNhTKTQDEI 69
Cdd:TIGR01467 1 GKLYGVGVGPGDPELITVKALEALRSADVIAVPASKKGReslarkivedYLKPNDTrilELVFPMTKDRDEL-EKAWDEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 70 NDIIVHKAKTGKIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEVIPGITSAIGGLCYAGIPITHRDyaSSFHVITGHLKE 149
Cdd:TIGR01467 80 AEAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEGD--ESLAILPATAGE 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 329126735 150 EgaELnwKSISSLEGTLVFLMGVSNLKNICNSLIKEGK 187
Cdd:TIGR01467 158 A--EL--EKALAEFDTVVLMKVGRNLPQIKEALAKLGR 191
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
8-231 |
7.92e-09 |
|
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: 55.58 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 8 VGAGPGDYKLITLKGMECIKKSDVIVydrlASSRLLKEAKE-TCEFIYVGKkssnhtktqDEINDIIVHKAKTGKIVTRL 86
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVI----GAKRLLELFPDlGAEKIPLPS---------EDIAELLEEIAEAGKRVVVL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 87 KGGDPYVFGRGGEEGEYLnkKGVKFEVIPGITSaiggLCYA----GIPITHrdyassFHVITGHlkeeGAELN--WKSIS 160
Cdd:cd11644 68 ASGDPGFYGIGKTLLRRL--GGEEVEVIPGISS----VQLAaarlGLPWED------ARLVSLH----GRDLEnlRRALR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 329126735 161 SLEGTLVFLMGVSNLKNICNSLIKEGKNKFtKAAIINWASTTKQKVVVGNLENIyekaMAEKISSPSLIVI 231
Cdd:cd11644 132 RGRKVFVLTDGKNTPAEIARLLLERGLGDS-RVTVGENLGYPDERITEGTAEEL----AEEEFSDLNVVLI 197
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
381-496 |
3.78e-07 |
|
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: 51.15 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 381 VFIPRSSEARTYLVEELNKLCnvTEVKIYNTIK-GSGNKDDIINLLNN-KNIDYITFTSSSTVKNFIEIMGKQNIEKLKD 458
Cdd:cd06578 1 VLVTRPRPQADELAALLEALG--AEVLELPLIEiEPLDDAELDAALADlDEYDWLIFTSPNAVEAFFEALEELGLRALAG 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 329126735 459 TKLVSIGPITSKTIEDFGLKVYNEAEEYTIEGIIKTLI 496
Cdd:cd06578 79 LKIAAVGPKTAEALREAGLTADFVPEEGDSEGLLELLE 116
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
251-376 |
1.27e-06 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 49.58 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 251 GKNIVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPSNVELDNGIEYINEFNYLIFTSRNAVKIFFeRLFELNFDSR 330
Cdd:PRK05928 125 GKRVLYLRGNGGREVLGDTLEERGAEVDECEVYERVPPKLDGAELLARLQSGEVDAVIFTSPSTVRAFF-SLAPELGRRE 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 329126735 331 KLGNLKVVAIGTGTSDELRHYGIIPDVLPKKFVAESVVELLKEVLQ 376
Cdd:PRK05928 204 WLLSCKAVVIGERTAEALRELGIKVIIVPDSADNEALLRALKELLK 249
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
254-356 |
1.93e-06 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 50.49 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 254 IVVTRSRVQSSNLVERIIELGGNPIEVPAIKIEEIPSNVELDNGIEYINEFNYLIFTSRNAVKIFFERLFELNFDSrklg 333
Cdd:PRK06975 6 VVVTRPDGQSAALAAQLAAAGLDVLDFPLLDIAPVADDAPLRAALARLSDYALVVFVSPNAVDRALARLDAIWPHA---- 81
|
90 100
....*....|....*....|...
gi 329126735 334 nLKVVAIGTGTSDELRHYGIIPD 356
Cdd:PRK06975 82 -LPVAVVGPGSVAALARHGIAAP 103
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
6-125 |
5.27e-06 |
|
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells.
Pssm-ID: 381174 Cd Length: 241 Bit Score: 47.80 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 6 FLVGAGPGDYKLITLKGMECIKKSDVIVYDRLaSSRLLKEAKETCEFIYvGKKSSNHTKTQDEIN-DIIVHKAKTGKIVT 84
Cdd:cd11647 3 YLIGLGLGDEKDITLEGLEALKKADKVYLEAY-TSILPGSKLEELEKLI-GKKIILLDREDLEEEsEEILEEAKKKDVAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 329126735 85 rLKGGDP---------YVfgrggeegeYLNKKGVKFEVIPG--ITSAIGGLC 125
Cdd:cd11647 81 -LVPGDPliatthidlRL---------EAKKRGIKVKVIHNasILSAAGSTS 122
|
|
| cbiH |
PRK15478 |
precorrin-3B C(17)-methyltransferase; |
7-133 |
2.07e-05 |
|
precorrin-3B C(17)-methyltransferase;
Pssm-ID: 185375 [Multi-domain] Cd Length: 241 Bit Score: 46.03 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 7 LVGAGPGDYKLITLKGMECIKKSDVIV----YDRLASSrllkeaketcefiYVGKKSSNHTKTQDEIN--DIIVHKAKTG 80
Cdd:PRK15478 4 VIGIGPGSQAMMTMEAIEALQAAEIVVgyktYTHLVKA-------------FTGDKQVIKTGMCKEIErcQAAIELAQAG 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 329126735 81 KIVTRLKGGDPYVFGRGGEEGEYLNKKGVKFEV--IPGITSAIGGLCYAGIPITH 133
Cdd:PRK15478 71 HNVALISSGDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLGAPLMH 125
|
|
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
6-122 |
1.01e-03 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 41.10 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 6 FLVGAGPGDYKLITLKGMECIKKSDViVYDRLASSRLLKEAKETCEFIYvGKKssnhTKTQDEI-----NDIIVHKAKTG 80
Cdd:PTZ00175 4 YIIGLGLGDEKDITVKGLEAVKSADV-VYLESYTSILINSNKEKLEEFY-GKP----VIEADREmveegCDEILEEAKEK 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 329126735 81 KIVTrLKGGDPyvFGRGGEEGEYL--NKKGVKFEVI--PGITSAIG 122
Cdd:PTZ00175 78 NVAF-LVVGDP--FCATTHTDLYLraKKKGIEVEVIhnASIMNAIG 120
|
|
| YabN_N_like |
cd11723 |
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and ... |
8-117 |
5.95e-03 |
|
N-terminal S-AdoMet-dependent tetrapyrrole methylase domain of Bacillus subtilis YabN and similar domains; This family includes the S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent tetrapyrrole methylase (TP-methylase) domain of Bacillus subtilis YabN, and similar domains. YabN is a fusion of an N-terminal TP-methylase and a C-terminal MazG-type nucleotide pyrophosphohydrolase domain. MazG-like NTP-PPases have been implicated in house-cleaning functions such as degrading abnormal (d)NTPs. TP-methylases use S-AdoMet in the methylation of diverse substrates. Most TP-methylase family members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis, other members like diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) act on other substrates. The specific function of YabN's TP-methylase domain is not known.
Pssm-ID: 381177 Cd Length: 218 Bit Score: 38.24 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329126735 8 VGAGPGDYKLITLKGMECIKKSDViVYDRLA---SSRLLKEAK---ETCEFIYvgKKSSNHTKTQDEINDIIVHKAKTGK 81
Cdd:cd11723 4 VGLGPGDPDLLTLGALEALKSADK-VYLRTArhpVVEELKEEGiefESFDDLY--EEAEDFEEVYEAIAERLLEAAEHGD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 329126735 82 IVtrlkgGDPYVfgrgGEEG-EYLNKK---GVKFEVIPGI 117
Cdd:cd11723 81 VVya-vpGHPLV----AERTvQLLLERaeeGIEVEIIPGV 115
|
|
| |
