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 27-MAR-2024, entry version 127.
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; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC 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; NP_455219.1; NC_003198.1.
DR RefSeq; WP_001241920.1; NZ_QXGZ01000014.1.
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; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0043755; F:alpha-ribazole phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
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; IPR017578; Ribazole_CobC.
DR NCBIfam; TIGR03162; ribazole_cobC; 1.
DR PANTHER; PTHR48100:SF71; 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.
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
//
