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Database: UniProt
Entry: W6L415_9TRYP
LinkDB: W6L415_9TRYP
Original site: W6L415_9TRYP 
ID   W6L415_9TRYP            Unreviewed;       527 AA.
AC   W6L415;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN   ORFNames=GSHART1_T00004884001 {ECO:0000313|EMBL:CCW68183.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW68183.1, ECO:0000313|Proteomes:UP000053358};
RN   [1] {ECO:0000313|EMBL:CCW68183.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW68183.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW68183.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW68183.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
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|ARBA:ARBA00000642,
CC         ECO:0000256|RuleBase:RU000532};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|RuleBase:RU000532}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR   EMBL; HF955201; CCW68183.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6L415; -.
DR   EnsemblProtists; CCW68183; CCW68183; GSHART1_T00004884001.
DR   OrthoDB; 5477183at2759; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000053358; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053358};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   DOMAIN          3..60
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
SQ   SEQUENCE   527 AA;  57320 MW;  06E1BC671F6999F3 CRC64;
     MFHVSKLEVI FMSLRDIVVL SDNEMVITDM NKPAVNFYGW KADEVKGKSI TFLIPTHPLD
     VPSSPVTLTA RLASGKDLIA VIQATRDPHG ELLAWTILPI ALPHVYEFGV HINIRAALTP
     KLSISDLDFE GRRVFIRVDF NVPFEHQTGK IRDDSRIRAA IPTIKKIMGE GGRVIIGSHL
     GRPKKPNPKQ SLQRILPRLK ELLDTEVGFV PDVFQAADEV KKLKNGEVLL LENLRFFKGE
     DSKKSEDHRV LSRALASFSD IYVCDAFGTV HRVSASMTGI PRALGAGVTG YLIEKEIKAI
     KMVMLNPAQP LVAVIGGSKV SDKINILASI FNFAQIVVIG GSMAFTFLEA MGHNLGASKV
     ERAIKEKAGV VDLHVKAREL LALAKSRHVE IILPVDHSCA TSFKDETPHI TDTADVPPNY
     MALDYGPKTI ALAAKAVQEA RTLIWNGPVG VFEFPNFSRG TTAIAEGVKA NRKLVSIVGG
     GDTAASTKSY RSYFTHVSTG GGAFLELLEG KALPGLVCLT ARAAPKL
//
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