ID   APGM_AQUAE              Reviewed;         407 AA.
AC   O66820;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable 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=aq_542;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06791.1; -; Genomic_DNA.
DR   PIR; H70348; H70348.
DR   RefSeq; NP_213380.1; NC_000918.1.
DR   RefSeq; WP_010880318.1; NC_000918.1.
DR   AlphaFoldDB; O66820; -.
DR   SMR; O66820; -.
DR   STRING; 224324.aq_542; -.
DR   DNASU; 1193238; -.
DR   EnsemblBacteria; AAC06791; AAC06791; aq_542.
DR   KEGG; aae:aq_542; -.
DR   PATRIC; fig|224324.8.peg.445; -.
DR   eggNOG; COG3635; Bacteria.
DR   HOGENOM; CLU_034906_2_0_0; -.
DR   InParanoid; O66820; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 1293048at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000798; 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_B; ApgM_B; 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..407
FT                   /note="Probable 2,3-bisphosphoglycerate-independent
FT                   phosphoglycerate mutase"
FT                   /id="PRO_0000138152"
FT   REGION          175..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  45006 MW;  263C18ACED69C33F CRC64;
     MDVISELVKK NGSKILLIVL DGLGGLPVKE GKTELELAKT PNLDKLVKNS ATGLHIPVDW
     GITPGSGPGH LGLFGYDPIK YQIGRGILEA LGLGIDVKDT DIAVRGNYAT VEYRNGKPIV
     VDRRAGRIPT EENKRITAKL QEAIKEIDGV QVIIKPGMEH RLAIVFRFPE KLSPGSDAIN
     DTDPQQVGKE PLEPKGENPN AEKVAEVVRK FIQRATEILR NEPKANYILL RGFSQKPDIP
     TMEERFGVKP CCIAVYPMYK GLASLVGMDV IEFEGSTIQD EIDTLKKVWN EYDYFFVHIK
     KTDSYGEDGN YEGKVSVIED FDAHLPQFLE LKPDVLAITG DHSTPSILKG HSWHPVPLLI
     HSPYVLGGTS ERFTERECLK GELGIIPAVK ITQLLLANAL RLKKYGA