ID   APGM_PYRFU              Reviewed;         411 AA.
AC   P58814;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
DE            Short=BPG-independent PGAM;
DE            Short=Phosphoglyceromutase;
DE            Short=aPGAM;
DE            EC=5.4.2.12;
GN   Name=apgM; OrderedLocusNames=PF1959;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=12076796; DOI=10.1111/j.1574-6968.2002.tb11253.x;
RA   van der Oost J., Huynen M.A., Verhees C.H.;
RT   "Molecular characterization of phosphoglycerate mutase in archaea.";
RL   FEMS Microbiol. Lett. 212:111-120(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000269|PubMed:12076796}.
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:0000269|PubMed:12076796};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:12076796};
CC   -!- ACTIVITY REGULATION: Inhibited to approximately 20% by EDTA.
CC       {ECO:0000269|PubMed:12076796}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:12076796};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000269|PubMed:12076796}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:12076796}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily. {ECO:0000305}.
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DR   EMBL; AE009950; AAL82083.1; -; Genomic_DNA.
DR   RefSeq; WP_011013101.1; NZ_CP023154.1.
DR   AlphaFoldDB; P58814; -.
DR   SMR; P58814; -.
DR   STRING; 186497.PF1959; -.
DR   PRIDE; P58814; -.
DR   EnsemblBacteria; AAL82083; AAL82083; PF1959.
DR   GeneID; 41713781; -.
DR   KEGG; pfu:PF1959; -.
DR   PATRIC; fig|186497.12.peg.2032; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 17268at2157; -.
DR   PhylomeDB; P58814; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001013; 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; 3.30.70.2130; -; 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   InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
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   1: Evidence at protein level;
KW   Glycolysis; Isomerase; Magnesium; Reference proteome.
FT   CHAIN           1..411
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000138144"
SQ   SEQUENCE   411 AA;  45314 MW;  870587E630C2B104 CRC64;
     MKQRKGVLII LDGLGDRPIK ELGGKTPLEY ANTPTMDYLA KIGILGQQDP IKPGQPAGSD
     TAHLSIFGYD PYKSYRGRGY FEALGVGLEL DEDDLAFRVN FATLENGVIT DRRAGRISTE
     EAHELAKAIQ ENVDIPVDFI FKGATGHRAV LVLKGMAEGY KVGENDPHEA GKPPHPFTWE
     DEASKKVAEI LEEFVKKAHE VLDKHPINEK RRKEGKPVAN YLLIRGAGTY PNIPMKFTEQ
     WKVKAAAVVA VALVKGVAKA IGFDVYTPKG ATGEYNTDEM AKARKAVELL KDYDFVFIHF
     KPTDAAGHDN NPKLKAELIE RADRMIKYIV DHVDLEDVVI AITGDHSTPC EVMNHSGDPV
     PLLIAGGGVR ADYTEKFGER EAMRGGLGRI RGHDIVPIMM DLMNRTEKFG A