(data stored in SCRATCH zone)

SWISSPROT: D1YVJ8_METPS

ID   D1YVJ8_METPS            Unreviewed;       776 AA.
AC   D1YVJ8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 50.
DE   RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|PIRNR:PIRNR000854};
DE            Short=PEP synthase {ECO:0000256|PIRNR:PIRNR000854};
DE            EC=2.7.9.2 {ECO:0000256|PIRNR:PIRNR000854};
DE   AltName: Full=Pyruvate, water dikinase {ECO:0000256|PIRNR:PIRNR000854};
GN   Name=ppsA-1 {ECO:0000313|EMBL:BAI60470.1};
GN   OrderedLocusNames=MCP_0398 {ECO:0000313|EMBL:BAI60470.1};
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:BAI60470.1, 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   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000854};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000854};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|PIRNR:PIRNR000854}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|PIRNR:PIRNR000854}.
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DR   EMBL; AP011532; BAI60470.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0398; -.
DR   EnsemblBacteria; BAI60470; BAI60470; MCP_0398.
DR   KEGG; mpd:MCP_0398; -.
DR   PATRIC; fig|304371.9.peg.408; -.
DR   eggNOG; arCOG01111; Archaea.
DR   eggNOG; COG0574; LUCA.
DR   HOGENOM; HOG000230912; -.
DR   KO; K01007; -.
DR   OMA; RRFVQMY; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR006319; PEP_synth.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_PEP-bd.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR43030; PTHR43030; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   PIRSF; PIRSF000854; PEP_synthase; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   TIGRFAMs; TIGR01418; PEP_synth; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVJ8.
DR   SWISS-2DPAGE; D1YVJ8.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000854};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000854};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000854};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000854};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000854};
KW   Pyruvate {ECO:0000313|EMBL:BAI60470.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000854}.
FT   DOMAIN          34..343
FT                   /note="PPDK_N"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
FT   DOMAIN          380..449
FT                   /note="PEP-utilizers"
FT                   /evidence="ECO:0000259|Pfam:PF00391"
FT   DOMAIN          465..763
FT                   /note="PEP-utilizers_C"
FT                   /evidence="ECO:0000259|Pfam:PF02896"
SQ   SEQUENCE   776 AA;  85222 MW;  2333BF40CA3AC4FF CRC64;
     MIVAAKTKSV SKEAVRPSNR LVVWLEDVRN SDIPIVGGKG ASLGEMINAE LPVPRGFVVT
     AQAFREFIEV TGIMDRLFKM LEVNVDDPKA LDRASADAKK LIMDTPMPKN IEKAIRDYYA
     TLCKREGEEV YVAARSSATA EDLPEASFAG QQETFLNVKG ADDLVRDVQK CWASLYGARA
     IYYRVEQKFP HEQVSIAVVV QKMVDAEEAG VMFTNHMTTG EDVTIIEAAW GLGESVVSGA
     VSPDTYLVDN KTFEIRQKKI ATKQTMITRD KKSRKSKQIA VPEAKKNVQV LPDDVIVKLA
     KLGQIVLDHY GKPQDIEWAV KDGELYLLQS RPITTIQKRE AKEGLASGEV ILEGLGASPG
     VVSGTVKIIH GRDELDKVLE GDILVTKMTE PDMVPAMKRS AAIVTDEGGM TCHAAIVSRE
     LGTPAVVGTR EATRLLKDGQ MVTVDGQKGH VLLGALKTTE EKPSEEAKVT AVAVATKPIT
     ATEVKVNVSI PEAAERAKAT MADGVGLLRI EHMILGLNTH PQVYIKGGRS DEYVNELVKG
     IRTVADAFYP KPVWVRTLDA PTDEFRAMKG GEGEPYEHNP MLGMRGIRRD LRETEHFKLE
     MAAFKKLFDL GYDNIGIMLP LVQHPVELKR AKQMMLECGI DIEKVDVGIM VEIPASALII
     DDFIKEGIDF VSFGTNDLTQ YTLAVDRNNE LVADLYNELH PAVLKLIEYV IERCNKAGVK
     TSICGQAGSR PEVARRLVGM GITSISANID AVEAVREMVA RTEHEIILDA ARKRVV
//

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