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Database: UniProt
Entry: A0A1Q3SHB4_9CHLR
LinkDB: A0A1Q3SHB4_9CHLR
Original site: A0A1Q3SHB4_9CHLR 
ID   A0A1Q3SHB4_9CHLR        Unreviewed;       208 AA.
AC   A0A1Q3SHB4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Alpha-ribazole phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO39_04405 {ECO:0000313|EMBL:OJV88750.1};
OS   Chloroflexi bacterium 54-19.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV88750.1, ECO:0000313|Proteomes:UP000186384};
RN   [1] {ECO:0000313|EMBL:OJV88750.1, ECO:0000313|Proteomes:UP000186384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54-19 {ECO:0000313|EMBL:OJV88750.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV88750.1}.
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DR   EMBL; MKTJ01000080; OJV88750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3SHB4; -.
DR   STRING; 1895928.BGO39_04405; -.
DR   Proteomes; UP000186384; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; 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   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-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;
FT   ACT_SITE        9
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        84
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   208 AA;  23364 MW;  D031AA910F508C99 CRC64;
     MPRFILTRHG QTDFNAQQRY QGSLDIPLND TGIAQARFLT PRLNSIKLDA VYSSDLQRAV
     KTAEIALENH PSGLQPKQLK LLREINGGGF EGLSWGEFSS RYPEEALLWR EDRTHVRPPD
     GGENLLDAAE RLDLALKHIL AEVPDPDASI LLVLHGGIIS LLLCKVMGME LERLWQWRID
     NCSVTILDLY EKGAILSVFN DIAHIKTS
//
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