ID   APGM2_METJA             Reviewed;         428 AA.
AC   Q60326;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 130.
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;
DE   AltName: Full=aPGAM-Mj2;
GN   Name=apgM2; OrderedLocusNames=MJ0010;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=12062435; DOI=10.1016/s0014-5793(02)02619-4;
RA   Graham D.E., Xu H., White R.H.;
RT   "A divergent archaeal member of the alkaline phosphatase binuclear
RT   metalloenzyme superfamily has phosphoglycerate mutase activity.";
RL   FEBS Lett. 517:190-194(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate.
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:0000269|PubMed:12062435};
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; L77117; AAB97991.1; -; Genomic_DNA.
DR   PIR; B64301; B64301.
DR   RefSeq; WP_010869503.1; NC_000909.1.
DR   AlphaFoldDB; Q60326; -.
DR   SMR; Q60326; -.
DR   STRING; 243232.MJ_0010; -.
DR   EnsemblBacteria; AAB97991; AAB97991; MJ_0010.
DR   GeneID; 1450849; -.
DR   KEGG; mja:MJ_0010; -.
DR   eggNOG; arCOG01696; Archaea.
DR   HOGENOM; CLU_034906_1_0_2; -.
DR   InParanoid; Q60326; -.
DR   OMA; HIHTKEP; -.
DR   OrthoDB; 17268at2157; -.
DR   PhylomeDB; Q60326; -.
DR   BRENDA; 5.4.2.12; 3260.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000805; 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; -; 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   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.
PE   1: Evidence at protein level;
KW   Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..428
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase 2"
FT                   /id="PRO_0000138135"
SQ   SEQUENCE   428 AA;  49350 MW;  7107678524B1C168 CRC64;
     MRAILILLDG LGDRASEILN NKTPLQFAKT PNLDRLAENG MCGLMTTYKE GIPLGTEVAH
     FLLWGYSLEE FPGRGVIEAL GEDIEIEKNA IYLRASLGFV KKDEKGFLVI DRRTKDISRE
     EIEKLVDSLP TCVDGYKFEL FYSFDVHFIL KIKERNGWIS DKISDSDPFY KNRYVMKVKA
     IRELCKSEVE YSKAKDTARA LNKYLLNVYK ILQNHKINRK RRKLEKMPAN FLLTKWASRY
     KRVESFKEKW GMNAVILAES SLFKGLAKFL GMDFIKIESF EEGIDLIPEL DYDFIHLHTK
     ETDEAAHTKN PLNKVKVIEK IDKLIGNLKL REDDLLIITA DHSTPSVGNL IHSGESVPIL
     FYGKNVRVDN VKEFNEISCS NGHLRIRGEE LMHLILNYTD RALLYGLRSG DRLRYYIPKD
     DEIDLLEG