COBS_BRUSU
ID COBS_BRUSU Reviewed; 260 AA.
AC Q8G156; G0K994;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
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};
GN OrderedLocusNames=BR0866, BS1330_I0862;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00719}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00719}.
CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000255|HAMAP-
CC Rule:MF_00719}.
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DR EMBL; AE014291; AAN29794.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18211.1; -; Genomic_DNA.
DR RefSeq; WP_002963996.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G156; -.
DR EnsemblBacteria; AEM18211; AEM18211; BS1330_I0862.
DR GeneID; 45051930; -.
DR GeneID; 55590572; -.
DR KEGG; bms:BR0866; -.
DR KEGG; bsi:BS1330_I0862; -.
DR PATRIC; fig|204722.21.peg.2579; -.
DR HOGENOM; CLU_057426_1_0_5; -.
DR OMA; GHTGDTY; -.
DR PhylomeDB; Q8G156; -.
DR UniPathway; UPA00148; UER00238.
DR Proteomes; UP000007104; Chromosome I.
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 inner membrane; Cell membrane; Cobalamin biosynthesis; Magnesium;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..260
FT /note="Adenosylcobinamide-GDP ribazoletransferase"
FT /id="PRO_0000146868"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00719"
SQ SEQUENCE 260 AA; 26404 MW; E0D7957924301DF0 CRC64;
MQRNGLIGDT IRSLGFLSRL PLPQGWFDNT DDSLPRNARA FPLAGGILGL LAGVALLIAN
AISLPPLAAA LIAIGALAAM TGALHEDGLG DTADGFFGAS TPDRRLDIMK DSRIGTFAAL
TLVIWTGVKA SLLMAIIARA GAGYALLALI GTEAASRAGM LAFWHALPSA RPGGLADSMG
QPQWETVVCG CGLGLALLAI GFLPSGGMVA LINALVLMTV VLFGFARLCM AKIGGQTGDT
LGAAQQIGSL AALIGLVMAL
