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Database: UniProt
Entry: A0A0Q7S7E9_9BACL
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ID   A0A0Q7S7E9_9BACL        Unreviewed;       197 AA.
AC   A0A0Q7S7E9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Phosphoglycerate kinase {ECO:0000313|EMBL:KQY79575.1};
GN   ORFNames=ASD24_19770 {ECO:0000313|EMBL:KQY79575.1};
OS   Paenibacillus sp. Root52.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736552 {ECO:0000313|EMBL:KQY79575.1, ECO:0000313|Proteomes:UP000051734};
RN   [1] {ECO:0000313|Proteomes:UP000051734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root52 {ECO:0000313|Proteomes:UP000051734};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY79575.1, ECO:0000313|Proteomes:UP000051734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root52 {ECO:0000313|EMBL:KQY79575.1,
RC   ECO:0000313|Proteomes:UP000051734};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KQY79575.1}.
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DR   EMBL; LMFO01000034; KQY79575.1; -; Genomic_DNA.
DR   RefSeq; WP_056703866.1; NZ_LMFO01000034.1.
DR   AlphaFoldDB; A0A0Q7S7E9; -.
DR   STRING; 1736552.ASD24_19770; -.
DR   OrthoDB; 9782128at2; -.
DR   Proteomes; UP000051734; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; 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; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR   PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KQY79575.1};
KW   Transferase {ECO:0000313|EMBL:KQY79575.1}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        9
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        83
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   197 AA;  22045 MW;  D12ED2B37E420520 CRC64;
     MTQLTLIRHG STAWNKEKRS QGQTDNPLDQ EGREQALLLA ARLSSDSWDA IYASDLERAS
     ETARIIGDRL GIKEIHLDPR LREMGGGQVE GTTEEERLSR WGEDWSSIEL GRETADAGTS
     RGMEVIEEIC RKHPHDRVLV VSHGAILRNT LRGLLPELDV SVKLSNTSVT RIEKKAEAWG
     CELYNCSVHL NTTEGTR
//
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