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 03-AUG-2022, entry version 152.
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., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40839.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 PDB; 6E4B; X-ray; 2.55 A; A/B/C/D=1-203.
DR PDBsum; 6E4B; -.
DR AlphaFoldDB; 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; fig|1411691.4.peg.1630; -.
DR EchoBASE; EB3029; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_8_4_6; -.
DR InParanoid; P52086; -.
DR OMA; WLTEPAW; -.
DR PhylomeDB; P52086; -.
DR BioCyc; EcoCyc:RIBAZOLEPHOSPHAT-MON; -.
DR BioCyc; MetaCyc:RIBAZOLEPHOSPHAT-MON; -.
DR UniPathway; UPA00061; UER00517.
DR PRO; PR:P52086; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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 3D-structure; Cobalamin biosynthesis; Hydrolase; Reference proteome.
FT CHAIN 1..203
FT /note="Adenosylcobalamin/alpha-ribazole phosphatase"
FT /id="PRO_0000179954"
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 STRAND 1..7
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:6E4B"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:6E4B"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:6E4B"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:6E4B"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6E4B"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:6E4B"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:6E4B"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:6E4B"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:6E4B"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:6E4B"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:6E4B"
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
