ID E1IRB2_ECOLX Unreviewed; 204 AA.
AC E1IRB2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Alpha-ribazole phosphatase {ECO:0000313|EMBL:EFO58132.1};
DE EC=3.1.3.73 {ECO:0000313|EMBL:EFO58132.1};
GN Name=cobC {ECO:0000313|EMBL:EFO58132.1};
GN ORFNames=HMPREF9348_02709 {ECO:0000313|EMBL:EFO58132.1};
OS Escherichia coli MS 145-7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO58132.1, ECO:0000313|Proteomes:UP000003691};
RN [1] {ECO:0000313|EMBL:EFO58132.1, ECO:0000313|Proteomes:UP000003691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO58132.1,
RC ECO:0000313|Proteomes:UP000003691};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO58132.1}.
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DR EMBL; ADWS01000012; EFO58132.1; -; Genomic_DNA.
DR AlphaFoldDB; E1IRB2; -.
DR Proteomes; UP000003691; Unassembled WGS sequence.
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; 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 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EFO58132.1}.
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 204 AA; 23456 MW; DE4C6F1FB9C11AE9 CRC64;
MMRLWLIRHG ETQANVDGLY SGHAPTPLTA RGIEQAQNLH TLLHGVSFDL VLCSELERAQ
HTARLVLSDR QLPVQIIPEL NEMFFGDWEM RHHRDLMQED AENYSAWCND WQHAIPTNGE
GFQAFSQRVE RFIARLSEFQ HYQNILVVSH QGVLSLLIAR LIGMPAEAMW HFRVDQGCWS
TIDINQKFAT LRVLNSRAIG VENA
//