ID   APGM2_ARCFU             Reviewed;         380 AA.
AC   O28847;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2;
DE            Short=BPG-independent PGAM 2;
DE            Short=Phosphoglyceromutase 2;
DE            Short=aPGAM 2;
DE            EC=5.4.2.12;
GN   Name=apgM2; OrderedLocusNames=AF_1425;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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}.
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DR   EMBL; AE000782; AAB89821.1; -; Genomic_DNA.
DR   PIR; H69427; H69427.
DR   RefSeq; WP_010878922.1; NC_000917.1.
DR   AlphaFoldDB; O28847; -.
DR   SMR; O28847; -.
DR   STRING; 224325.AF_1425; -.
DR   DNASU; 1484649; -.
DR   EnsemblBacteria; AAB89821; AAB89821; AF_1425.
DR   GeneID; 24795037; -.
DR   KEGG; afu:AF_1425; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; FRCNLIT; -.
DR   OrthoDB; 17268at2157; -.
DR   PhylomeDB; O28847; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002199; 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_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   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..380
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase 2"
FT                   /id="PRO_0000138132"
SQ   SEQUENCE   380 AA;  42457 MW;  E90DE95BDE300DF8 CRC64;
     MKYLLLIPDG MADWEVEELD GRTPLEVAET ENMDFLAKEG ACGIAKTVPD GFEPGSDVAN
     LTILGVDVRK HYTGRGPIEA LARGVKGKLV FRCNLVKVED GVMVDYSGGR ISDEEARKVI
     EELNRAKPYD FVKFYAGKSY RNLLVINKDF RDDVKTFPPH DITGKEIDKH LPSGGELAEL
     LKELMGWSAE ILPEITDKAN MIWPWGGGRM PSFPNFGQRY GLRGAMITEV DLLEGIARGM
     GMEVVQVEGI TGYIDTNYRG LVRETARALE EHDFVVLHTE GIDEVGHEGD AELKVRAIEL
     YDSKIVGKLL NKVDLDETRI LLLPDHPTPV KVKTHVAEPV PFTLYGRGRD EVKVYTEKSC
     RRGKFGLVDG LRLMDLLIKK