ID   APGM_METPE              Reviewed;         411 AA.
AC   B8GFN7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Mpal_2656;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
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; CP001338; ACL17920.1; -; Genomic_DNA.
DR   RefSeq; WP_012619239.1; NC_011832.1.
DR   AlphaFoldDB; B8GFN7; -.
DR   SMR; B8GFN7; -.
DR   STRING; 521011.Mpal_2656; -.
DR   PRIDE; B8GFN7; -.
DR   EnsemblBacteria; ACL17920; ACL17920; Mpal_2656.
DR   GeneID; 7272478; -.
DR   KEGG; mpl:Mpal_2656; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 17268at2157; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002457; 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; Reference proteome.
FT   CHAIN           1..411
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_1000184574"
SQ   SEQUENCE   411 AA;  43261 MW;  66B09742B17D6AE4 CRC64;
     MTAHKIVMLV LDGIGDRPCG ELAGMTPLQA AKTPILDQLA AEGITGIMDT IGPGIRPGSD
     TSHLSLLGYP PESYYTGRGP LEAEGCGIHM EHGMIGFRAN FATQNDHGLV TDRRAGRIHD
     TRLLSAAITD QVDLSAFGVT FSFASGAGHR AALALSGEGL GAGVTSNDPK EDGVAPHQVM
     PVSANPEDQK TAAVCNEFIR QSTAILADHP MNRARVLNGE SPASVVLIRG AGEMGGFEPF
     QQRYDLSGAV IAAATLVTGI GKAVGLEYIP VEGVTGSTTT NLTGKVQTLM ATLDTHDFVL
     LNIKGADEAG HDGHAIEKRD FIERIDAALA LLLERNDCII AVMGDHSTPC PIKEHSADPV
     PVLIRGDGVR VDLVQAYDEI ACAAGGLNRI RGADILWILL DLIDKTHKYG T