ID   APGM_GEOSL              Reviewed;         399 AA.
AC   Q74C57;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=GSU1818;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017180; AAR35195.1; -; Genomic_DNA.
DR   RefSeq; NP_952868.1; NC_002939.5.
DR   RefSeq; WP_010942463.1; NC_002939.5.
DR   AlphaFoldDB; Q74C57; -.
DR   SMR; Q74C57; -.
DR   STRING; 243231.GSU1818; -.
DR   EnsemblBacteria; AAR35195; AAR35195; GSU1818.
DR   KEGG; gsu:GSU1818; -.
DR   PATRIC; fig|243231.5.peg.1855; -.
DR   eggNOG; COG3635; Bacteria.
DR   HOGENOM; CLU_034906_2_0_7; -.
DR   InParanoid; Q74C57; -.
DR   OMA; IAFRCNF; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000577; 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.
DR   TIGRFAMs; TIGR02535; hyp_Hser_kinase; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..399
FT                   /note="Probable 2,3-bisphosphoglycerate-independent
FT                   phosphoglycerate mutase"
FT                   /id="PRO_0000138154"
SQ   SEQUENCE   399 AA;  43249 MW;  A178908E1D948F72 CRC64;
     MKYIVLLGDG MSDEPMQELG GKTPLQAART PHMDAMARRG RIGLARTVPE GYPPGSDVAN
     LSVFGYDPRA CYTGRSPLEA ASMGVELGSA DVAFRVNLVN LAPTRGTLVM NDYSAGHIST
     AEGRELIEAI QGVMGTDEFQ FYPGVGYRHL MVWRNGKCGM TVVPPHDISG QSILEHLPKG
     EGAERLIELM NSSQLVLNNH PQYRRRLEEG KVPANSIWLW GHGKAPRMAS FHEKFGLTGA
     VISAVDLVRG IGVCAGLDVI KVEGATGYID TNYEGKVTAA LEALEAHDYV YLHVEAPDEA
     GHGGNLEHKL KAIEDFDARV VGPIMAGMEK FGSYRILCTP DHPTPLRLKT HTDAPVPFVL
     FSGETSENAG VAGYDEESAR SAGLVVEDGF RLMEMMLDR