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Database: UniProt
Entry: A0A0Q4H0F2_9BURK
LinkDB: A0A0Q4H0F2_9BURK
Original site: A0A0Q4H0F2_9BURK 
ID   A0A0Q4H0F2_9BURK        Unreviewed;       213 AA.
AC   A0A0Q4H0F2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KQM78976.1};
GN   ORFNames=ASE76_16435 {ECO:0000313|EMBL:KQM78976.1};
OS   Xylophilus sp. Leaf220.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX   NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM78976.1, ECO:0000313|Proteomes:UP000051325};
RN   [1] {ECO:0000313|EMBL:KQM78976.1, ECO:0000313|Proteomes:UP000051325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf220 {ECO:0000313|EMBL:KQM78976.1,
RC   ECO:0000313|Proteomes:UP000051325};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM78976.1, ECO:0000313|Proteomes:UP000051325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf220 {ECO:0000313|EMBL:KQM78976.1,
RC   ECO:0000313|Proteomes:UP000051325};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQM78976.1}.
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DR   EMBL; LMKO01000003; KQM78976.1; -; Genomic_DNA.
DR   RefSeq; WP_055836474.1; NZ_LMKO01000003.1.
DR   AlphaFoldDB; A0A0Q4H0F2; -.
DR   STRING; 1735686.ASE76_16435; -.
DR   OrthoDB; 9783269at2; -.
DR   Proteomes; UP000051325; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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   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   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051325}.
FT   ACT_SITE        11
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         10..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   213 AA;  23436 MW;  FCA3F69BA0974A86 CRC64;
     MHATRIIAIR HGETAWNVDT RIQGQIDIPL NDTGEWQAAR LAEALADEPI AAVYASDLLR
     AHRTAEHVAR SQGLPVRADT GLRERAFGSF EGLTFDEIHA TLPDDARRWR TREPEFVPGG
     TGESLIVFRA RVVETVHAIA ARHPGEQVVV VGHGGVLDVL YRAATRQELQ APRTWKVGNA
     AINRLLWTPD GLSLVGWADD AHLARQELDD GTV
//
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