ID H3RBG4_PANSE Unreviewed; 530 AA.
AC H3RBG4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Glucose-1-phosphatase/inositol phosphatase {ECO:0000313|EMBL:EHU01303.1};
DE EC=3.1.3.10 {ECO:0000313|EMBL:EHU01303.1};
DE EC=3.1.3.2 {ECO:0000313|EMBL:EHU01303.1};
GN Name=agp {ECO:0000313|EMBL:EHU01303.1};
GN ORFNames=CKS_4053 {ECO:0000313|EMBL:EHU01303.1};
OS Pantoea stewartii subsp. stewartii DC283.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=660596 {ECO:0000313|EMBL:EHU01303.1, ECO:0000313|Proteomes:UP000005050};
RN [1] {ECO:0000313|EMBL:EHU01303.1, ECO:0000313|Proteomes:UP000005050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:EHU01303.1,
RC ECO:0000313|Proteomes:UP000005050};
RX PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA Wang X., Yang F., von Bodman S.B.;
RT "The genetic and structural basis of two distinct terminal side branch
RT residues in stewartan and amylovoran exopolysaccharides and their potential
RT role in host adaptation.";
RL Mol. Microbiol. 83:195-207(2012).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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:EHU01303.1}.
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DR EMBL; AHIE01000008; EHU01303.1; -; Genomic_DNA.
DR AlphaFoldDB; H3RBG4; -.
DR STRING; 660596.DSJ_09825; -.
DR PATRIC; fig|660596.6.peg.1316; -.
DR eggNOG; ENOG502Z7K9; Bacteria.
DR Proteomes; UP000005050; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008877; F:glucose-1-phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR11567:SF135; GLUCOSE-1-PHOSPHATASE; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EHU01303.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003590596"
FT REGION 424..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 56886 MW; 8EC11CDFCA437A9E CRC64;
MIKKLSLCAL SVLAALPIGT LAHAADNEMQ LQQVLMFSRH NLRAPLADNG SVLAQSTKKS
WPEWEVPGGQ LTTKGGVLEV YMGNYTRQWL AQQGLVKNGA CPDSNSVFVY ANSLQRTVAT
AQFFVNGAFP GCDITVTHQD EMGSMDPVFN PVITDGNEEF IKKALADMTA ANEKLALKPA
YQRLDKIVDY KSSPACNNKK QCDLSSGQNT FIVENGKEPG VNGPLKVGNS LMDAFTLQYY
EGFPLDQVAW GQIKTPEQWQ SLSAIKNGYQ DTLFTTPDVA RNVAAPLVDY IRSQLIDQDK
ADSPKVTLMV GHDSNIASLL SALQVKPYDL PETYEKTPIG GQVVFERWHD AKNNKDLLKM
EYVYQTADQL RDAQVLSLKT PPKRVTLQLA GCPTDANGYC SWEQFTQVLN SALQGTALQP
AAAEQPAASA NAGAANPAES KADDKASADK ATADNAAAQK AADDKVKADK AADEKAKADK
AAAQKAADEK ASADKAAAQK AADDKAKAEN AANAQNKTDN SPAKQPAAAN
//
