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COBS_BREBN
ID   COBS_BREBN              Reviewed;         246 AA.
AC   C0Z7H6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=BBR47_12420;
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599;
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; AP008955; BAH42219.1; -; Genomic_DNA.
DR   RefSeq; WP_012684970.1; NC_012491.1.
DR   AlphaFoldDB; C0Z7H6; -.
DR   STRING; 358681.BBR47_12420; -.
DR   EnsemblBacteria; BAH42219; BAH42219; BBR47_12420.
DR   KEGG; bbe:BBR47_12420; -.
DR   eggNOG; COG0368; Bacteria.
DR   HOGENOM; CLU_057426_3_1_9; -.
DR   OMA; FMDSMDG; -.
DR   OrthoDB; 1996371at2; -.
DR   UniPathway; UPA00148; UER00238.
DR   Proteomes; UP000001877; 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;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..246
FT                   /note="Adenosylcobinamide-GDP ribazoletransferase"
FT                   /id="PRO_1000212687"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        167..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        193..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ   SEQUENCE   246 AA;  26515 MW;  66CB166EF82F92F7 CRC64;
     MNAFLHAISF FTRIPVPWLR PSEEAWRKSV NWYPAVGLVI GLLLWGVHQA GLVLFSPWIA
     AILTLIAWVY VTGGLHMDGW MDLADGLGSS RPREQILAIM KDSRVGAMGV LAAIMLLLIK
     AGAVAELAHP GWGSFLIVAP VAARTHVLLS IKLWPYLSAD KGIGKGISSG LSVSSIIVSY
     IIVFAAGWYL GGLQVMTAIF LSLLFALWFS RSVAKKLGGL NGDCYGAVIE SSEAVVLLVL
     VGSWWL
 
 
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