(data stored in ACNUC10043 zone)

SWISSPROT: D1YVN8_METPS

ID   D1YVN8_METPS            Unreviewed;       412 AA.
AC   D1YVN8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 55.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532};
GN   Name=pgk-1 {ECO:0000313|EMBL:BAI60510.1};
GN   Synonyms=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
GN   OrderedLocusNames=MCP_0438 {ECO:0000313|EMBL:BAI60510.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60510.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00145,
CC         ECO:0000256|RuleBase:RU000532};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00145}.
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DR   EMBL; AP011532; BAI60510.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0438; -.
DR   EnsemblBacteria; BAI60510; BAI60510; MCP_0438.
DR   KEGG; mpd:MCP_0438; -.
DR   PATRIC; fig|304371.9.peg.450; -.
DR   eggNOG; arCOG00496; Archaea.
DR   eggNOG; COG0126; LUCA.
DR   HOGENOM; HOG000227108; -.
DR   KO; K00927; -.
DR   OMA; DMIFDIG; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1260; -; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVN8.
DR   SWISS-2DPAGE; D1YVN8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|PIRSR:PIRSR000724-2};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532,
KW   ECO:0000313|EMBL:BAI60510.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00145,
KW   ECO:0000256|RuleBase:RU000532}.
FT   NP_BIND         355..358
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   REGION          60..63
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT   BINDING         39
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT   BINDING         117
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT   BINDING         157
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT   BINDING         330
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   412 AA;  44553 MW;  02738BCB81EF5C23 CRC64;
     MDRDYCTMDD FDLDGKTVIL RAEFNSPIGP DGKILDDKRI RESVPTIKGL EGSKVVLIAH
     QSRPGKKDFT TMEQHAKRLQ RYVKQSVHYV DDIFGSHARA AIVEAEPGDI VMLENVRFYS
     EEVLELKPEA AAKTVMVKKL APLAQVFLND AFGASHRSQD SLVGFTPILP SGSGKLMQKE
     IDSLTEALRG GGEVVYVLGG AKVDDSISVT KNVLEKGIAS RVLVTGVVAN VFLAASGMNI
     GNPNYEFLEK NELTGEIPNA KEVLQKFDGK ILMPSDVAIN KDGKRVEINV RQLPADYPIM
     DIGHETIANF SDIIRHSDKV ILNGPAGVFE NPEFGTGTRD ILMAATKAKF SVVGGGHSSA
     AVEEMGIEDK ITHVSTGGGA AIDFLSGKPM PAIDALKAAK KRMMEHVGAK TH
//

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