ID E1SIZ3_PANVC Unreviewed; 578 AA.
AC E1SIZ3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Glucose-1-phosphatase {ECO:0000313|EMBL:ADO08995.1};
DE EC=3.1.3.10 {ECO:0000313|EMBL:ADO08995.1};
GN Name=agp {ECO:0000313|EMBL:ADO08995.1};
GN OrderedLocusNames=Pvag_0795 {ECO:0000313|EMBL:ADO08995.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO08995.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO08995.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO08995.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; CP002206; ADO08995.1; -; Genomic_DNA.
DR AlphaFoldDB; E1SIZ3; -.
DR KEGG; pva:Pvag_0795; -.
DR eggNOG; ENOG502Z7K9; Bacteria.
DR HOGENOM; CLU_030561_2_1_6; -.
DR OrthoDB; 395886at2; -.
DR Proteomes; UP000006631; Chromosome.
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; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ADO08995.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..578
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003151340"
FT REGION 423..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 61297 MW; BD01A40487912794 CRC64;
MNGIGTMIKK LSLCALSVLA ALPVGTVAFA ADGDMQLQQV LMLSRHNLRA PLADNGSVLE
QSTKKSWPQW DVPGGQLTTK GGVLEVYMGN YTRQWLAQQG LVKNGSCPDS NNVFVYANSL
QRTVATAQFF VNGAFPGCDV AVTHQDEMGA MDPVFNPVIT DDSEAFNKKA LAAMAAANEK
LSLKPAFQRL EKIVDYKASP ACNNKKQCDL SSGQNTFSAE NGKEPTVSGP LKVGNSLMDA
FTLQYYEGFP LDQVAWGQIK TPEQWKELSA IKNGYQDTLF TSPDVSREVA APLVDYIRSQ
LVDQDKANAP KITLMVGHDS NIASLLSALQ VKPYELPDTY EKTPIGGQVV FERWHDAKND
KDLLKVEYVY QTADQLRNAD VLSLKNPPKR VTLQLAGCEA DANGYCSWDQ FSQVLNAALQ
GTPMQPAAAP QPAAQADDDS AKAAATQDAA ADKAEADKAT AAKEKSDADK AAAEKSEADK
AAAEKAKADK AAADKAAAEK AKAEKAKADK AAADKAAAEK AKADKAAAEE KAAAEKAKAD
NAAESASDNK ATTDKADAAN APATAHNDNS TSAAVATQ
//
