ID   APGM_METMA              Reviewed;         397 AA.
AC   Q8PX04;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 131.
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=MM_1418;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000250}.
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;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM31114.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM31114.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011033364.1; NC_003901.1.
DR   AlphaFoldDB; Q8PX04; -.
DR   SMR; Q8PX04; -.
DR   STRING; 192952.MM_1418; -.
DR   EnsemblBacteria; AAM31114; AAM31114; MM_1418.
DR   GeneID; 24879587; -.
DR   KEGG; mma:MM_1418; -.
DR   PATRIC; fig|192952.21.peg.1641; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; FRCNLIT; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000595; 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.
DR   TIGRFAMs; TIGR02535; hyp_Hser_kinase; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..397
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000138137"
SQ   SEQUENCE   397 AA;  43175 MW;  FFB8BC932E9E15EC CRC64;
     MKYAILIGDG MADYPIEKLG NRTILQAART PAMDSIAARG RAGLAKTVPD SFPPGSDVAN
     MSILGYDPAT YYSGRAPLEA ASMGVALAAD DVAFRCNLIT TEHGMIKDYS AGHISSDEAE
     ILIDTLDYEL STENIRFYPG ISYRHLIVAG NNLGAETECT PPHDITGEKI DKYLPRGKDG
     EFFSELIEAS KVVLELHPVN LKRVEEGKNP ANSIWVWGQG YAPKFTAFMK LYGKKGAVIS
     AVDLLKGIGI YAGLDVIEVH GATGYLDTNY EGKVRAAIEA LKTRDLVFVH VEAPDEAGHE
     GSIEKKLKAV EDFDSRIVAP ILEYAENSDE PFTILVLPDH PTPISVKTHT RDPIPFAIYR
     TDKPETDNVE AFDEESVKNG SMGLVKASDL IGILIKS