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Database: UniProt/TrEMBL
Entry: A0A0A1D113_9MICC
LinkDB: A0A0A1D113_9MICC
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ID   A0A0A1D113_9MICC        Unreviewed;       248 AA.
AC   A0A0A1D113;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039};
GN   Name=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN   ORFNames=ART_3314 {ECO:0000313|EMBL:AIY02913.1};
OS   Arthrobacter sp. PAMC 25486.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY02913.1, ECO:0000313|Proteomes:UP000030301};
RN   [1] {ECO:0000313|EMBL:AIY02913.1, ECO:0000313|Proteomes:UP000030301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY02913.1,
RC   ECO:0000313|Proteomes:UP000030301};
RA   Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT   "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT   Arctic.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.11; Evidence={ECO:0000256|HAMAP-Rule:MF_01039};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC       Rule:MF_01039}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|HAMAP-Rule:MF_01039}.
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DR   EMBL; CP007595; AIY02913.1; -; Genomic_DNA.
DR   RefSeq; WP_038466307.1; NZ_CP007595.1.
DR   AlphaFoldDB; A0A0A1D113; -.
DR   STRING; 1494608.ART_3314; -.
DR   KEGG; arm:ART_3314; -.
DR   HOGENOM; CLU_033323_1_1_11; -.
DR   OrthoDB; 9781415at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000030301; Chromosome.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   NCBIfam; TIGR01258; pgm_1; 1.
DR   PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030301}.
FT   ACT_SITE        10
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        88
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         9..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         22..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         88..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         115..116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         183..184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-2"
FT   SITE            182
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT                   ECO:0000256|PIRSR:PIRSR613078-3"
SQ   SEQUENCE   248 AA;  27687 MW;  C6264A2ADDF05440 CRC64;
     MTYTLILLRH GHSEWNAKNL FTGWVDVDLN DQGRTEAVRG GELLVENNLL PDVLYTSRLK
     RAINTANLAL EKADRGWIDV KRDWRLNERH YGALQGKDKA QTLAEYGEEQ FMEWRRSYDT
     PPPPLSDDSE FSQAHDPRYA DLGDALPRTE CLKDVLVRLL PYWESDIKAD LKAGKTVLVT
     AHGNSLRALV KHLDGISDEA IAALNIPTGI PLVYELDENF APITPGGKYL DPEAAAAAIQ
     AVANQGKK
//
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