ID   GPMA_METVS              Reviewed;         235 AA.
AC   A6US15;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN   Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039}; OrderedLocusNames=Mevan_1390;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01039};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_01039}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR   EMBL; CP000742; ABR55287.1; -; Genomic_DNA.
DR   RefSeq; WP_012066201.1; NC_009634.1.
DR   AlphaFoldDB; A6US15; -.
DR   SMR; A6US15; -.
DR   STRING; 406327.Mevan_1390; -.
DR   EnsemblBacteria; ABR55287; ABR55287; Mevan_1390.
DR   GeneID; 5324802; -.
DR   KEGG; mvn:Mevan_1390; -.
DR   eggNOG; arCOG01993; Archaea.
DR   HOGENOM; CLU_033323_1_4_2; -.
DR   OMA; RMLPYWY; -.
DR   OrthoDB; 61359at2157; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001107; 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; -; 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   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
PE   3: Inferred from homology;
KW   Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..235
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000064076"
FT   ACT_SITE        9
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   ACT_SITE        110
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         8..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         21..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         110..113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         137..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   BINDING         181..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT   SITE            180
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ   SEQUENCE   235 AA;  27055 MW;  EA969213092C37D6 CRC64;
     MANLVFLRHG ESIWNKMNIF TGWVDVPLSK GGVKEAKIAG KLLKSYKFDV AYSSELIRAL
     NTLILVMQEN KASNFIKINH DSVKMKEWGK VYGAESINYT PVYKSWELNE RYYGKLQGLN
     KERAKEIYGK DDVFLWRRSY ETAPPNGESL KDTYERTVPY LKRYILPTLT YGKDVIVTAH
     GNSLRSIIAY LEKLNSEEVL KLEIPTGVPL VYNLDEKGLK RLGYLNKKGF DNELI