ID   APGM_THEMA              Reviewed;         401 AA.
AC   Q9X295;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=TM_1774;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD36837.1; -; Genomic_DNA.
DR   PIR; E72213; E72213.
DR   RefSeq; NP_229571.1; NC_000853.1.
DR   RefSeq; WP_004082320.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X295; -.
DR   SMR; Q9X295; -.
DR   STRING; 243274.THEMA_05355; -.
DR   EnsemblBacteria; AAD36837; AAD36837; TM_1774.
DR   KEGG; tma:TM1774; -.
DR   eggNOG; COG3635; Bacteria.
DR   InParanoid; Q9X295; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 1293048at2; -.
DR   BioCyc; MetaCyc:MON-402; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000008183; 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..401
FT                   /note="Probable 2,3-bisphosphoglycerate-independent
FT                   phosphoglycerate mutase"
FT                   /id="PRO_0000138155"
SQ   SEQUENCE   401 AA;  44275 MW;  9B2FB45F1C154411 CRC64;
     MFDKQEFVSK LVTEEKAKIV LLVMDGLGDI PVNGKTPLQA ANTPNLDNLA KESDLGQTIP
     VLPGITPGSG PGHLSLFGYD PIKYQIGRGI LEALGIGVEV GEKDVVARAN FATWDGKVVL
     DRRAGRPATE ESAKVVQLLS EKIKKIEDVE ITFYPGKEHR FVVKFTGEGL GDKVTDADPQ
     KEGHPMVWAE GLDEPSKKTA RIVNELIKKI AEVLKDNPKI NFALIRGFSK YPDLPKFPQV
     YKMKAGAIAT YPMYRGLAKL VGMEIIETGQ TVADEIKTLK EKWNDYDFFY VHVKKTDSYG
     EDGKFEEKVK VIEEVDAIIP EIVSLNPDVL VITGDHSTPV PLKAHSWHPV PLLIWSKYTR
     RGLSQAFNEF ECARGTLGTI HASDVMTLAL AYAGKLEKFG A