ID   APGM_METS3              Reviewed;         412 AA.
AC   A5UKY4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Msm_0657;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86862.1; -; Genomic_DNA.
DR   RefSeq; WP_004032416.1; NC_009515.1.
DR   AlphaFoldDB; A5UKY4; -.
DR   SMR; A5UKY4; -.
DR   STRING; 420247.Msm_0657; -.
DR   PRIDE; A5UKY4; -.
DR   EnsemblBacteria; ABQ86862; ABQ86862; Msm_0657.
DR   GeneID; 5216097; -.
DR   KEGG; msi:Msm_0657; -.
DR   PATRIC; fig|420247.28.peg.654; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; IAFRCNF; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001992; 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..412
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000087365"
SQ   SEQUENCE   412 AA;  44903 MW;  CF998AE7A7953467 CRC64;
     MKGIVLVMDG MGDRPLKEFD NQTPLQAANT PNMDEMAKNG ITGIMDSIAP GIIPGSDTAH
     LSILGYDPYE VYTGRGPFEA AGVGVDVIPG DIAFRCNFST ADENGIVTDR RAGRIREGTH
     EIVEVLNTMV LEDYPDIKII FKESTGHRAV LVLRGEGLSD KVSDADPKVE GNKPKEVIPL
     DDSVEAKKTA DILNKLVVKS YEMIKDHPVN LERIENNEPP ANIIIPRGAG EVPVVEALND
     KYEVNSACIA ETGLIMGIGR FAGMDIIEME DVTGGIDTNL ENIRDTIIDQ VKNSDHDFFL
     INIDGADEAG HDGQAVEKRD FIEKVDRVVM SELKKLEDVY IFLTADHSTP ISVLNHSGDP
     VPVIITGPEV RVDDVCEYSE VAVAKGGLCR IRGADVMNIM MDLMNYAHKF GA