ID   A4CS09_SYNPV            Unreviewed;       488 AA.
AC   A4CS09;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Possible alpha-ribazole-5'-P phosphatase {ECO:0000313|EMBL:EAR20046.1};
GN   ORFNames=WH7805_14038 {ECO:0000313|EMBL:EAR20046.1};
OS   Synechococcus sp. (strain WH7805).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=59931 {ECO:0000313|EMBL:EAR20046.1, ECO:0000313|Proteomes:UP000001224};
RN   [1] {ECO:0000313|EMBL:EAR20046.1, ECO:0000313|Proteomes:UP000001224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7805 {ECO:0000313|Proteomes:UP000001224};
RA   Scanlan D., Ostrowski M., Mazard S., Wilkinson N., Partensky F.,
RA   Dufresne A., Garczarek L., Hess W., Gierga G., Voss B., Axmann I., Post A.,
RA   Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K., Beeson K.,
RA   Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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:EAR20046.1}.
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DR   EMBL; AAOK01000001; EAR20046.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4CS09; -.
DR   STRING; 59931.WH7805_14038; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_035286_1_0_3; -.
DR   PhylomeDB; A4CS09; -.
DR   Proteomes; UP000001224; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 2.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
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; 2.
DR   SMART; SM00855; PGAM; 2.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 2.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   4: Predicted;
FT   ACT_SITE        280
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        354
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         279..286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            423
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   488 AA;  53281 MW;  987D90DF4728B510 CRC64;
     MDVRKVGWST RRRQLKVILV GDGCSGRGQS KQGLTHTMAA PCTHEAVTLR LLLVRHGLSS
     FNVERRIQGR DDLSTLTETG EDQARRTGTA LADVPITAVY SSPLKRAAST TAGVLAARND
     ALEPCFDDGL LEIDLEPWSG LTAAERAERF PEEYAAWRSD PEQLELTRHD GTRYRPLPEL
     MQQASQFLDA LLARHPVDGN ETVLLVGHNA ILRCLITTLL GNPAGGFRRL RLDNASLSVF
     NLIPQGSDHQ VQIECLNSTA HLNPPLPPKG AGSRMILVRH GETNWNRDGR FQGQIDIPLN
     SNGHAQAEAA RAFLETVSIQ RAYSSAMSRP RQTAEGILRS HPGVPLTVTR GLVEIGHGLW
     EGKLESEIRA EWAELLDEWK RTPETVQMPE GETIQDVWER SVHSWNTIAE SLDRSETALV
     VAHDAVNKTI LCSLLGLSPS DIWAIKQGNG GVTVVDMPTE TGQPAVVACL NLTSHLGGVL
     DRTAAGAL
//