位置:首页 > 蛋白库 > GPM_THEAC
GPM_THEAC
ID   GPM_THEAC               Reviewed;         200 AA.
AC   Q9HIJ2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
DE            Short=BPG-dependent PGAM;
DE            Short=PGAM;
DE            Short=Phosphoglyceromutase;
DE            Short=dPGM;
DE            EC=5.4.2.11;
GN   OrderedLocusNames=Ta1347;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
RN   [2]
RP   FUNCTION AS A PHOSPHOGLYCERATE MUTASE, SUBUNIT, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF HIS-9.
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
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=5.4.2.11;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=17 uM for 2,3-diphosphoglycerate {ECO:0000269|PubMed:17576516};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17576516}.
CC   -!- INDUCTION: Inhibited by vanadate. Inhibition can partially be relieved
CC       by EDTA.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The original start site is 14 aa downstream of the start site
CC       shown here. Experiments from PubMed:17576516 were carried out with the
CC       original sequence. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC12468.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL445067; CAC12468.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048162417.1; NC_002578.1.
DR   AlphaFoldDB; Q9HIJ2; -.
DR   SMR; Q9HIJ2; -.
DR   STRING; 273075.Ta1347; -.
DR   PRIDE; Q9HIJ2; -.
DR   EnsemblBacteria; CAC12468; CAC12468; CAC12468.
DR   GeneID; 1456820; -.
DR   KEGG; tac:Ta1347; -.
DR   eggNOG; arCOG01991; Archaea.
DR   HOGENOM; CLU_033323_9_3_2; -.
DR   OMA; RHGESDI; -.
DR   OrthoDB; 61359at2157; -.
DR   SABIO-RK; Q9HIJ2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000001024; Chromosome.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:RHEA.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..200
FT                   /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT                   mutase"
FT                   /id="PRO_0000303675"
FT   ACT_SITE        9
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         9
FT                   /note="H->A: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:17576516"
SQ   SEQUENCE   200 AA;  22322 MW;  3256FA2B51534D72 CRC64;
     MKIAILIRHG ESDINVKGIL SDTIDNNMLT EKGMRQAEHA AAELKGIDIK NFYSSPIKRA
     FDTAQIIADS FNKDVVTDQR LIEIGLGKAR GRKANEFTNG LYSGHITGKI REDLEMEKWD
     SLQKRVVEAI ASREGINVYV THSDPIRAAI SYFLEMGEEE TYGLSIKNAS MTVIDVEIGR
     ILTLGAISMT DSVRKYLNIQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024