Entry sw:COBC_ECOLI

ID   COBC_ECOLI              Reviewed;         203 AA.
AC   P52086; P77109;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-NOV-2016, entry version 128.
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; Synonyms=phpB; OrderedLocusNames=b0638, JW0633;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Addinall S.G., Donachie W.D.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Catalyzes the conversion of adenosylcobalamin 5'-
CC       phosphate to adenosylcobalamin (vitamin B12); involved in the
CC       assembly of the nucleotide loop of cobalamin. Also catalyzes the
CC       hydrolysis of the phospho group from alpha-ribazole 5'-phosphate
CC       to form alpha-ribazole. {ECO:0000250|UniProtKB:P39701}.
CC   -!- CATALYTIC ACTIVITY: Adenosylcobalamin 5'-phosphate + H(2)O =
CC       coenzyme B12 + phosphate. {ECO:0000250|UniProtKB:P39701}.
CC   -!- CATALYTIC ACTIVITY: Alpha-ribazole 5'-phosphate + H(2)O = alpha-
CC       ribazole + phosphate. {ECO:0000250|UniProtKB:P39701}.
CC   -!- PATHWAY: Nucleoside biosynthesis; alpha-ribazole biosynthesis;
CC       alpha-ribazole from 5,6-dimethylbenzimidazole: step 2/2.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB40839.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; U23163; AAA64853.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40839.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73739.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35285.1; -; Genomic_DNA.
DR   PIR; D64798; D64798.
DR   RefSeq; NP_415171.1; NC_000913.3.
DR   RefSeq; WP_001241872.1; NZ_LN832404.1.
DR   ProteinModelPortal; P52086; -.
DR   SMR; P52086; -.
DR   IntAct; P52086; 3.
DR   STRING; 511145.b0638; -.
DR   PaxDb; P52086; -.
DR   PRIDE; P52086; -.
DR   EnsemblBacteria; AAC73739; AAC73739; b0638.
DR   EnsemblBacteria; BAA35285; BAA35285; BAA35285.
DR   GeneID; 945246; -.
DR   KEGG; ecj:JW0633; -.
DR   KEGG; eco:b0638; -.
DR   PATRIC; 32116459; VBIEscCol129921_0669.
DR   EchoBASE; EB3029; -.
DR   EcoGene; EG13240; cobC.
DR   eggNOG; ENOG4108TGR; Bacteria.
DR   eggNOG; COG0406; LUCA.
DR   HOGENOM; HOG000221683; -.
DR   InParanoid; P52086; -.
DR   KO; K02226; -.
DR   OMA; EVERSHC; -.
DR   PhylomeDB; P52086; -.
DR   BioCyc; EcoCyc:RIBAZOLEPHOSPHAT-MONOMER; -.
DR   BioCyc; ECOL316407:JW0633-MONOMER; -.
DR   BioCyc; MetaCyc:RIBAZOLEPHOSPHAT-MONOMER; -.
DR   UniPathway; UPA00061; UER00517.
DR   PRO; PR:P52086; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; 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   3: Inferred from homology;
KW   Cobalamin biosynthesis; Complete proteome; Hydrolase;
KW   Reference proteome.
FT   CHAIN         1    203       Adenosylcobalamin/alpha-ribazole
FT                                phosphatase.
FT                                /FTId=PRO_0000179954.
FT   ACT_SITE      8      8       Tele-phosphohistidine intermediate.
FT                                {ECO:0000250|UniProtKB:P62707}.
FT   ACT_SITE     81     81       Proton donor/acceptor.
FT                                {ECO:0000250|UniProtKB:P62707}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         2    156       ismart:PGAM [T]
FT   MYHIT         5     14       ipat:PG_MUTASE [T]
FT   MYHIT         3    194       ipfam:His_Phos_1 [T]
SQ   SEQUENCE   203 AA;  23308 MW;  9034B19DC366E1D0 CRC64;
     MRLWLIRHGE TQANIDGLYS GHAPTPLTAR GIEQAQNLHT LLHGVSFDLV LCSELERAQH
     TARLVLSDRQ LPVQIIPELN EMFFGDWEMR HHRDLMQEDA ENYSAWCNDW QHAIPTNGEG
     FQAFSQRVER FIARLSEFQH YQNILVVSHQ GVLSLLIARL IGMPAEAMWH FRVDQGCWSA
     IDINQKFATL RVLNSRAIGV ENA
//