(data stored in ACNUC7421 zone)

SWISSPROT: Q75C60_ASHGO

ID   Q75C60_ASHGO            Unreviewed;       247 AA.
AC   Q75C60;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 104.
DE   RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE            EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
GN   ORFNames=AGOS_ACR056W {ECO:0000313|EMBL:AAS51283.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51283.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51283.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; Evidence={ECO:0000256|RuleBase:RU004511};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|RuleBase:RU004511}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|RuleBase:RU004511}.
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DR   EMBL; AE016816; AAS51283.2; -; Genomic_DNA.
DR   RefSeq; NP_983459.2; NM_208812.2.
DR   STRING; 33169.AAS51283; -.
DR   EnsemblFungi; AAS51283; AAS51283; AGOS_ACR056W.
DR   GeneID; 4619584; -.
DR   KEGG; ago:AGOS_ACR056W; -.
DR   HOGENOM; HOG000221682; -.
DR   InParanoid; Q75C60; -.
DR   KO; K01834; -.
DR   OMA; RMLPYWY; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:EnsemblFungi.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:EnsemblFungi.
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   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75C60.
DR   SWISS-2DPAGE; Q75C60.
KW   Glycolysis {ECO:0000256|RuleBase:RU004511};
KW   Isomerase {ECO:0000256|RuleBase:RU004511};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   REGION          116..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  27484 MW;  E0B4F8936A22CF23 CRC64;
     MPKLVLVRHG QSEWNEKNLF TGWVDVKLSA VGEQEAARAG ELLKEHNVNP DILFTSKLTR
     AIQTANIALT KADRIWIPVE RSWRLNERHY GDLQGKDKAA TLAAFGEEKF NTYRRSFDVP
     PPPIADDSEF SQSNDERYRD VDPNVLPKTE SLALVIDRLL PYWQDTISKE LLSGKTVMIT
     AHGNSLRGLV KHLEGISDAD IAKLNIPTGI PLVFELDENL KPTKPSYYLD PEAAAAGAAA
     VANQGKK
//

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