ID   COBC_SALTI              Reviewed;         202 AA.
AC   P58652;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   02-SEP-2026, entry version 137.
DE   RecName: Full=Adenosylcobalamin/alpha-ribazole phosphatase;
DE            EC=3.1.3.73 {ECO:0000250|UniProtKB:P39701};
DE   AltName: Full=Adenosylcobalamin phosphatase;
DE   AltName: Full=Alpha-ribazole-5'-phosphate phosphatase;
GN   Name=cobC; OrderedLocusNames=STY0694, t2224;
OS   Salmonella typhi.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Catalyzes the conversion of adenosylcobalamin 5'-phosphate to
CC       adenosylcobalamin (vitamin B12); involved in the assembly of the
CC       nucleotide loop of cobalamin. Also catalyzes the hydrolysis of the
CC       phospho group from alpha-ribazole 5'-phosphate to form alpha-ribazole.
CC       {ECO:0000250|UniProtKB:P39701}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)alamin 5'-phosphate + H2O =
CC         adenosylcob(III)alamin + phosphate; Xref=Rhea:RHEA:30367,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18408, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60493; EC=3.1.3.73;
CC         Evidence={ECO:0000250|UniProtKB:P39701};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-ribazole 5'-phosphate + H2O = alpha-ribazole +
CC         phosphate; Xref=Rhea:RHEA:24456, ChEBI:CHEBI:10329,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57918; EC=3.1.3.73;
CC         Evidence={ECO:0000250|UniProtKB:P39701};
CC   -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC       ribazole from 5,6-dimethylbenzimidazole: step 2/2.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AL513382; CAD05120.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69827.1; -; Genomic_DNA.
DR   RefSeq; WP_001241920.1; NZ_CDCZ01000001.1.
DR   AlphaFoldDB; P58652; -.
DR   SMR; P58652; -.
DR   STRING; 220341.gene:17584701; -.
DR   KEGG; stt:t2224; -.
DR   KEGG; sty:STY0694; -.
DR   PATRIC; fig|220341.7.peg.698; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_033323_8_4_6; -.
DR   OMA; WLTEPAW; -.
DR   UniPathway; UPA00061; UER00517.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0043755; F:alpha-ribazole phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR050275; PGM_Phosphatase.
DR   InterPro; IPR017578; Ribazole_CobC.
DR   NCBIfam; NF011580; PRK15004.1; 1.
DR   NCBIfam; TIGR03162; ribazole_cobC; 1.
DR   PANTHER; PTHR48100:SF59; ADENOSYLCOBALAMIN_ALPHA-RIBAZOLE PHOSPHATASE; 1.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Hydrolase; Reference proteome.
FT   CHAIN           1..202
FT                   /note="Adenosylcobalamin/alpha-ribazole phosphatase"
FT                   /id="PRO_0000179955"
FT   ACT_SITE        8
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   ACT_SITE        81
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   CONFLICT        85
FT                   /note="V -> G (in Ref. 2; AAO69827)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  23109 MW;  8FEA0F235C5C148A CRC64;
     MRLWLVRHGE TEANVAGLYS GHAPTPLTEK GIGQAKTLHT LLRHAPFDRV LCSELERARH
     TARLVLEGRD TPQHILPELN EMYFVDWEMR HHRDLTHEDA ESYAAWCTDW QNAVPTNGEG
     FQAFTRRVER FISRLGAFSD CQNLLIVSHQ GVLSLLIARL LAMPAASLWH FRVEQGCWST
     IDICEGFATL KVLNSRAVWR PE
//