ID   APGM_PYRAB              Reviewed;         410 AA.
AC   Q9V2M6; G8ZFN0;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 125.
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=PYRAB00490;
GN   ORFNames=PAB2318;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248283; CAB48972.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69421.1; -; Genomic_DNA.
DR   PIR; E75190; E75190.
DR   RefSeq; WP_010867173.1; NC_000868.1.
DR   AlphaFoldDB; Q9V2M6; -.
DR   SMR; Q9V2M6; -.
DR   STRING; 272844.PAB2318; -.
DR   EnsemblBacteria; CAB48972; CAB48972; PAB2318.
DR   GeneID; 1494932; -.
DR   KEGG; pab:PAB2318; -.
DR   PATRIC; fig|272844.11.peg.56; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 17268at2157; -.
DR   PhylomeDB; Q9V2M6; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; -; 1.
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   3: Inferred from homology;
KW   Glycolysis; Isomerase.
FT   CHAIN           1..410
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000138142"
SQ   SEQUENCE   410 AA;  45202 MW;  91C8A89637608826 CRC64;
     MQRKGILIIL DGLGDRPIKE LGGLTPLEYA NTPNMDKLAK IGILGQQDPI KPGQPAGSDT
     AHLSIFGYDP YKTYRGRGFF EALGVGLDLD EDDLAFRVNF ATLKDGIVVD RRAGRISTEE
     AHELAKAIQE EVDVGVDFIF KGATGHRAVL VLKGMADGYR VGDNDPHVEG KPPHKFSWED
     EESKKVAEIL EEFVKKAHEV LERHPINEKR RREGKPVANY LLIRGAGTYP NIPMKFTEQW
     KVKAAAVIAV ALVKGVARAI GFDVYTPEGA TGEYNTNEMA KAKKVVELLK DYDFVFLHFK
     PTDAAGHDNK PKLKAELIER ADKMIGYIID NIDLESTVIA ITGDHSTPCE VKNHSGDPVP
     LLIAGGGVRT DHTERFGERE AMKGGLGRIR GHDIVPIMMD LMNRSEKFGA