APGM1_ARCFU
ID APGM1_ARCFU Reviewed; 408 AA.
AC O28523;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
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;
GN Name=apgM1; OrderedLocusNames=AF_1751;
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).
RN [2]
RP FUNCTION AS A PHOSPHOGLYCERATE MUTASE, SUBUNIT, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=17576516; DOI=10.1007/s00792-007-0094-x;
RA Johnsen U., Schoenheit P.;
RT "Characterization of cofactor-dependent and cofactor-independent
RT phosphoglycerate mutases from Archaea.";
RL Extremophiles 11:647-657(2007).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000269|PubMed:17576516}.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17576516};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for 3-phosphoglycerate {ECO:0000269|PubMed:17576516};
CC KM=0.2 mM for 2-phosphoglycerate {ECO:0000269|PubMed:17576516};
CC Vmax=3.3 umol/min/mg enzyme toward 3-phosphoglycerate
CC {ECO:0000269|PubMed:17576516};
CC Vmax=0.8 umol/min/mg enzyme toward 2-phosphoglycerate
CC {ECO:0000269|PubMed:17576516};
CC pH dependence:
CC Optimum pH is 7.1. {ECO:0000269|PubMed:17576516};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Does not lose activity
CC after 120 minutes at 60 degrees Celsius at pH7 with 50 uM of
CC manganese chloride and 5 mM of magnesium chloride.
CC {ECO:0000269|PubMed:17576516};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17576516}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000305}.
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DR EMBL; AE000782; AAB89499.1; -; Genomic_DNA.
DR PIR; F69468; F69468.
DR RefSeq; WP_010879247.1; NC_000917.1.
DR AlphaFoldDB; O28523; -.
DR SMR; O28523; -.
DR STRING; 224325.AF_1751; -.
DR DNASU; 1484974; -.
DR EnsemblBacteria; AAB89499; AAB89499; AF_1751.
DR GeneID; 24795495; -.
DR KEGG; afu:AF_1751; -.
DR eggNOG; arCOG01696; Archaea.
DR HOGENOM; CLU_034906_2_0_2; -.
DR OMA; IAFRCNF; -.
DR OrthoDB; 17268at2157; -.
DR PhylomeDB; O28523; -.
DR SABIO-RK; O28523; -.
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.
PE 1: Evidence at protein level;
KW Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..408
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase 1"
FT /id="PRO_0000138131"
SQ SEQUENCE 408 AA; 44096 MW; 5A2228F3264B370E CRC64;
MPVLLIVVDG LSDRPIDGKT PLSVARKPNL DRLAEMGING IMDTIAPGIR PGSDTSHLAL
LGYDPYKYYS GRGPIEAAGV GIEIKPGDVA FRANFATVEG EGSIFDKTVV DRRAGRIEDT
SELIKALREI ELPVELLVER GTGHRAAVVF RGEGLSDRVS DTDPKAVGKK VKRCVPLADD
AKAKKTAEIV NEFMQKAHEV LENHPLNRER AEKGLLKANA LLLRGAGEMP HVPSFKDKTG
LRLCVIAATA LIKGVGRVVG ADVITPEGAT GNKNTNLEAK VKAAINALES YDVVLLHIKA
TDELGHDGDF EGKKAFIEKL DEKIAPLLDL DFSKTCLILT ADHSTPIKVK DHTADPVPVV
IVHEDVRRDE VSSFSEFEAY KGGLCRIRGM DLLNIALDLL NIAKKFGA
