ID N1J6G3_BLUG1 Unreviewed; 654 AA.
AC N1J6G3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00021932};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN ORFNames=BGHDH14_bgh06596 {ECO:0000313|EMBL:CCU75281.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU75281.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU75281.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU75281.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=4.1.1.49; Evidence={ECO:0000256|ARBA:ARBA00001389};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000256|ARBA:ARBA00006052}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCU75281.1}.
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DR EMBL; CAUH01001164; CCU75281.1; -; Genomic_DNA.
DR AlphaFoldDB; N1J6G3; -.
DR STRING; 546991.N1J6G3; -.
DR EnsemblFungi; BLGH_00780-mRNA-1; BLGH_00780-mRNA-1; BLGH_00780.
DR eggNOG; ENOG502QQI5; Eukaryota.
DR HOGENOM; CLU_018247_0_1_1; -.
DR InParanoid; N1J6G3; -.
DR OrthoDB; 3740611at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000015441; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00484; PEPCK_ATP; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 1.
DR HAMAP; MF_00453; PEPCK_ATP; 1.
DR InterPro; IPR001272; PEP_carboxykinase_ATP.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR InterPro; IPR015994; PEPCK_ATP_CS.
DR NCBIfam; TIGR00224; pckA; 1.
DR PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Kinase {ECO:0000313|EMBL:CCU75281.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:CCU75281.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015441};
KW Transferase {ECO:0000313|EMBL:CCU75281.1}.
SQ SEQUENCE 654 AA; 72541 MW; 68AEAD321E67B756 CRC64;
MEAVSVDIVE VRAKSGLITY CKVKDREGFR AVGEEEKGGI RAQEQVNGAL DCTDRDPAPI
LMQNCFITTV ISIDQDLRSN RHARALFLVP NEKERRDVYD LNRILSPLQS DIKSSPIKEH
TRLEEELHDN AHIDYDRVAI VPNPSVAVLY EDALVFETGT AITSTGALTA YSGLKTGRSP
QDKRIVKEPS SEDDIWWGPV NKPMTPEVWR INRERAIDYL NTRNRIYVVD GYAGWDQKYQ
IKVRIVCARA YHALFMRNML IRPEREDLAQ FQPDYTIYNA GSFPANRYTS GMTSATSIAI
NFADKEIVIL GTEYAGEMKK GVFTILFYEM PVKYNVLTLH SSANEGKDGD VTLFFGLSGT
GKTTLSADPL RALIGDDEHC WSENGIFNIE GGCYAKCLGL SVEKEPEIFG AIKFGAVLEN
VVFSAETRFV DYEDSTLTEN TRCAYPIDHI VNAKIPCVSI DHPRNIILLT CDASGVLPPI
SKLNSAQVMF HFISGYTSKM TGTEDGVTEP QATFSACFAQ PFLALHPMRY AEMLAEKIEN
HRANAWLLNT GWVGAAATSG GQRCPLKYTR AILSAIHSGE LTKASYETYE TFNLEVPTSC
SGVPSNLLNP RNAWTAGGNS FGEEVARLGA LFIKNFEKYS GEVSELVKSA GPKL
//
