COBC_SALTY
ID COBC_SALTY Reviewed; 202 AA.
AC P39701;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Adenosylcobalamin/alpha-ribazole phosphatase;
DE EC=3.1.3.73 {ECO:0000269|PubMed:17209023, ECO:0000269|PubMed:7929373};
DE AltName: Full=Adenosylcobalamin phosphatase;
DE AltName: Full=Alpha-ribazole-5'-phosphate phosphatase;
GN Name=cobC; OrderedLocusNames=STM0643;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=7929373; DOI=10.1016/s0021-9258(18)47223-7;
RA O'Toole G.A., Trzebiatowski J.R., Escalante-Semerena J.C.;
RT "The cobC gene of Salmonella typhimurium codes for a novel phosphatase
RT involved in the assembly of the nucleotide loop of cobalamin.";
RL J. Biol. Chem. 269:26503-26511(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17209023; DOI=10.1128/jb.01665-06;
RA Zayas C.L., Escalante-Semerena J.C.;
RT "Reassessment of the late steps of coenzyme B12 synthesis in Salmonella
RT enterica: evidence that dephosphorylation of adenosylcobalamin-5'-phosphate
RT by the CobC phosphatase is the last step of the pathway.";
RL J. Bacteriol. 189:2210-2218(2007).
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:0000269|PubMed:17209023, ECO:0000269|PubMed:7929373}.
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:0000269|PubMed:17209023, ECO:0000269|PubMed:7929373};
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:0000269|PubMed:17209023, ECO:0000269|PubMed:7929373};
CC -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-
CC ribazole from 5,6-dimethylbenzimidazole: step 2/2.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62874.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U12808; AAA62874.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL19594.1; -; Genomic_DNA.
DR PIR; A55367; A55367.
DR RefSeq; NP_459635.1; NC_003197.2.
DR RefSeq; WP_001241924.1; NC_003197.2.
DR AlphaFoldDB; P39701; -.
DR SMR; P39701; -.
DR STRING; 99287.STM0643; -.
DR PaxDb; P39701; -.
DR EnsemblBacteria; AAL19594; AAL19594; STM0643.
DR GeneID; 1252163; -.
DR KEGG; stm:STM0643; -.
DR PATRIC; fig|99287.12.peg.679; -.
DR HOGENOM; CLU_033323_8_4_6; -.
DR OMA; WLTEPAW; -.
DR PhylomeDB; P39701; -.
DR BioCyc; MetaCyc:MON-13213; -.
DR BioCyc; SENT99287:STM0643-MON; -.
DR BRENDA; 3.1.3.73; 5542.
DR UniPathway; UPA00061; UER00517.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043755; F:alpha-ribazole phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 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 Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR03162; ribazole_cobC; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Cobalamin biosynthesis; Hydrolase; Reference proteome.
FT CHAIN 1..202
FT /note="Adenosylcobalamin/alpha-ribazole phosphatase"
FT /id="PRO_0000179956"
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 46..59
FT /note="PFDRVLCSELERAR -> HLTGCYRASWSARA (in Ref. 1;
FT AAA62874)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="V -> C (in Ref. 1; AAA62874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 23123 MW; CBE887F066510B9D CRC64;
MRLWLVRHGE TEANVAGLYS GHAPTPLTEK GIGQAKTLHT LLRHAPFDRV LCSELERARH
TARLVLEGRD VPQHILPELN EMYFGDWEMR HHRDLTHEDA ESYAAWCTDW QNAVPTNGEG
FQAFTRRVER FISRLDAFSD CQNLLIVSHQ GVLSLLIARL LTMPAASLWH FRVEQGCWSA
IDICEGFATL KVLNSRAVWR PE
