ID   APGM_METVS              Reviewed;         406 AA.
AC   A6UQ84;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE            Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE            Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE            Short=aPGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE            EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01402};
GN   Name=apgM {ECO:0000255|HAMAP-Rule:MF_01402}; OrderedLocusNames=Mevan_0750;
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_01402}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC         Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC         EC=5.4.2.12; Evidence={ECO:0000255|HAMAP-Rule:MF_01402};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_01402}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01402}.
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DR   EMBL; CP000742; ABR54656.1; -; Genomic_DNA.
DR   RefSeq; WP_011972558.1; NC_009634.1.
DR   AlphaFoldDB; A6UQ84; -.
DR   SMR; A6UQ84; -.
DR   STRING; 406327.Mevan_0750; -.
DR   EnsemblBacteria; ABR54656; ABR54656; Mevan_0750.
DR   GeneID; 5325430; -.
DR   KEGG; mvn:Mevan_0750; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 17268at2157; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001107; Chromosome.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16011; iPGM_like; 1.
DR   Gene3D; 3.40.720.10; -; 2.
DR   HAMAP; MF_01402_A; ApgM_A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR023665; ApgAM_prokaryotes.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR   PANTHER; PTHR31209; PTHR31209; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   Pfam; PF10143; PhosphMutase; 1.
DR   PIRSF; PIRSF006392; IPGAM_arch; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
DR   TIGRFAMs; TIGR00306; apgM; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Isomerase.
FT   CHAIN           1..406
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000087367"
SQ   SEQUENCE   406 AA;  44562 MW;  1C1C4BC8E2EF6FAB CRC64;
     MKAVIFVIDG LGDRPDEFGN TPLKEANTHT MDKIAKEGIC GIMNAIDIGV RPGSDTAHLA
     LLGYDPYETY TGRGPFEACG VGITVKPGDI AFRCNFSSVD KEFIVTDRRA GRIEDTSLLE
     KELDGLKIDD VEVIFKESGG YRAALLLRGP NLSDKISDAD PKKEGKKVKE IIPLDDSKEA
     EKTANILNRL LKVAYEKLDG HPVNQKRRTN NLPVANMIIP RGVGKVPEII PFDKKYGLKG
     ACIAGTGLIK GIAKMVNLDV IEVKGATGTP DSNFMAKAKA LVETLKTHDF VLINVKGADE
     AGHDGNYEVK KQVIEKIDEM LTYIMENIDR KDVYFVLTGD HSTPIEEMDH SADPLPIVIW
     GKSVRVDDVE KFDEFSTCKG GLNWIKGKNI MPILIDLMGL SKKYGA