COBS_SULIL
ID COBS_SULIL Reviewed; 253 AA.
AC C3MJX7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000255|HAMAP-Rule:MF_00719};
DE EC=2.7.8.26 {ECO:0000255|HAMAP-Rule:MF_00719};
DE AltName: Full=Cobalamin synthase {ECO:0000255|HAMAP-Rule:MF_00719};
DE AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00719};
GN Name=cobS {ECO:0000255|HAMAP-Rule:MF_00719}; OrderedLocusNames=LS215_2295;
OS Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=429572;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.S.2.15 / Lassen #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC -!- FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate
CC adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin
CC 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole =
CC adenosylcob(III)alamin + GMP + H(+); Xref=Rhea:RHEA:16049,
CC ChEBI:CHEBI:10329, ChEBI:CHEBI:15378, ChEBI:CHEBI:18408,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487; EC=2.7.8.26;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00719};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate =
CC adenosylcob(III)alamin 5'-phosphate + GMP + H(+);
CC Xref=Rhea:RHEA:23560, ChEBI:CHEBI:15378, ChEBI:CHEBI:57918,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:60487, ChEBI:CHEBI:60493; EC=2.7.8.26;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00719};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00719};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
CC {ECO:0000255|HAMAP-Rule:MF_00719}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00719};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00719}.
CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000255|HAMAP-
CC Rule:MF_00719}.
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DR EMBL; CP001399; ACP36280.1; -; Genomic_DNA.
DR RefSeq; WP_012714214.1; NC_012589.1.
DR AlphaFoldDB; C3MJX7; -.
DR EnsemblBacteria; ACP36280; ACP36280; LS215_2295.
DR GeneID; 7809007; -.
DR GeneID; 8762251; -.
DR KEGG; sis:LS215_2295; -.
DR HOGENOM; CLU_057426_2_0_2; -.
DR OMA; CACCGIP; -.
DR OrthoDB; 108934at2157; -.
DR UniPathway; UPA00148; UER00238.
DR Proteomes; UP000001747; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051073; F:adenosylcobinamide-GDP ribazoletransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00719; CobS; 1.
DR InterPro; IPR003805; CobS.
DR PANTHER; PTHR34148; PTHR34148; 1.
DR Pfam; PF02654; CobS; 1.
DR TIGRFAMs; TIGR00317; cobS; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cobalamin biosynthesis; Magnesium; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..253
FT /note="Adenosylcobinamide-GDP ribazoletransferase"
FT /id="PRO_1000212698"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ SEQUENCE 253 AA; 27840 MW; 9B4BF8CB37678327 CRC64;
MRLKGVLALF SFFTAIPIKS NASLEEIAEY SYISPLIIGI SLALIESAVY VLLYRILEAL
AGIVLLGVVE LLRGFNHLDG LLDLGDALMI KGDRERKIKA LKDVEIGSGG IGLLLVYLSI
QIVALLKLGF SFYTIFHLIS SNVLSMTIGL YILSTISPIP ESNLGKIFHN KLKGKSTVLL
LELIPFISLY NIIVFLVFYM IMHKICRSLG GSSGDIAGAS ITLSFPLFLL TNEITNLNYS
LLSILCYLFL HLH