APGM1_METJA
ID APGM1_METJA Reviewed; 411 AA.
AC Q59007;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1;
DE Short=BPG-independent PGAM 1;
DE Short=Phosphoglyceromutase 1;
DE Short=aPGAM 1;
DE EC=5.4.2.12;
DE AltName: Full=aPGAM-Mj1;
GN Name=apgM1; OrderedLocusNames=MJ1612;
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 FUNCTION, AND 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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=12076796; DOI=10.1111/j.1574-6968.2002.tb11253.x;
RA van der Oost J., Huynen M.A., Verhees C.H.;
RT "Molecular characterization of phosphoglycerate mutase in archaea.";
RL FEMS Microbiol. Lett. 212:111-120(2002).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000269|PubMed:12062435,
CC ECO:0000269|PubMed:12076796}.
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 ECO:0000269|PubMed:12076796};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:12076796};
CC -!- ACTIVITY REGULATION: Inhibited to approximately 20% by EDTA.
CC {ECO:0000269|PubMed:12076796}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:12076796};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000269|PubMed:12076796}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:12076796}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000305}.
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DR EMBL; L77117; AAB99632.1; -; Genomic_DNA.
DR PIR; C64501; C64501.
DR RefSeq; WP_010871137.1; NC_000909.1.
DR AlphaFoldDB; Q59007; -.
DR SMR; Q59007; -.
DR STRING; 243232.MJ_1612; -.
DR DNASU; 1452521; -.
DR EnsemblBacteria; AAB99632; AAB99632; MJ_1612.
DR GeneID; 1452521; -.
DR KEGG; mja:MJ_1612; -.
DR eggNOG; arCOG01696; Archaea.
DR HOGENOM; CLU_034906_2_0_2; -.
DR InParanoid; Q59007; -.
DR OMA; IAFRCNF; -.
DR OrthoDB; 17268at2157; -.
DR PhylomeDB; Q59007; -.
DR BioCyc; MetaCyc:MON-4905; -.
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; -; 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.
PE 1: Evidence at protein level;
KW Glycolysis; Isomerase; Magnesium; Reference proteome.
FT CHAIN 1..411
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase 1"
FT /id="PRO_0000138134"
SQ SEQUENCE 411 AA; 45226 MW; 47A986FD09BA1099 CRC64;
MKKGKCVIFI IDGLGDRPNE KGLTPLKEAK TPTMDKIAKE GICGLMNAID IGIRPGSDTA
HLAILGYNPY EVYTGRGPLE AFGVGLDLKE GDIAFRCNFA TVDENFVVLD RRAGRISPEE
AEELEKEIDG LEIDGVKVIF KSSKGYRGAL VLRGEGLSCR VSDGDPHEEG VKVSEIKPLD
DSEEAKRTAE ILNKLLKIVY EKLNNHPINE ERRKKGLPPA NIILPRGAGV VPKIEKFSEK
YNMKGACICG TGLIKGMAKM IGLDVIEVEG ATGTPKTNFM GKAKALVEAL KEYDFVLVNV
KGADEASHDG NYELKKEVLE KIDEMLAYVF EHINKDEVYF VLTGDHSTPI EMKDHSADPI
PIVIWGKSVR VDDVTEFNEF ACAKGALHWI KGEHVMKILL DLTGRNEKFG A
