ID F4RJR2_MELLP Unreviewed; 572 AA.
AC F4RJR2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00021932};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN ORFNames=MELLADRAFT_43190 {ECO:0000313|EMBL:EGG07357.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL883104; EGG07357.1; -; Genomic_DNA.
DR RefSeq; XP_007409264.1; XM_007409202.1.
DR AlphaFoldDB; F4RJR2; -.
DR STRING; 747676.F4RJR2; -.
DR EnsemblFungi; EGG07357; EGG07357; MELLADRAFT_43190.
DR GeneID; 18928098; -.
DR KEGG; mlr:MELLADRAFT_43190; -.
DR VEuPathDB; FungiDB:MELLADRAFT_43190; -.
DR eggNOG; ENOG502QQI5; Eukaryota.
DR HOGENOM; CLU_018247_0_1_1; -.
DR InParanoid; F4RJR2; -.
DR OrthoDB; 3740611at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001072; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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 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 PIRSF; PIRSF006294; PEP_crbxkin; 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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001072}.
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63894 MW; A48D67CE59ED2DAD CRC64;
MAHLLHSHTN SPLTRTGTPM HLFEEPGSHV SHAGQPHYHL VGKDLKMFSE AGFDMDKIHI
KRNAPIAQLY EEAIRNEGAI ISASGALINF SGKKTGRSPK DKRIVYEETS KDHVWWGSVN
IKMDEHTFEI NRERAIDYLN TRDNVYVFDG FAGWDPKYRI KVRVICARAY HALFMTNMLI
RPTEKDLEDF GEPDFTIYNA GQFPANRFTS GMTSATSVEI NFKRREMVIL GTEYAGEMKK
GIFSVMHYLQ PVKFGQLSLH SSANEGPDGD VSLFFGLSGT GKTTLSADPA RMLIGDDEHV
WSDNGVFNIE GGCYAKCIGL SAAKEPDIYR AIRFGAILEN VVYDGDSREP CYDDASITEN
TRCAYPIEFI PNAKIPCLST SQPSNVVYLT CDAYGILPPV SKLTREQAQY WFLMGYTSKT
PGTEDGVTEP TPTFSTCFGQ PFIVLHPSKY ATMLAERMDK VQANCWLINT GWVGGKFGTG
ARCSLKYTRK LIDAIHDGSL AKAEYENFDV FNLAIPKTLP DVPDTVLNPM KAWKNTSAFE
NDRKKLAGLF RDAFKKYEKE VSAEVKAAGP KV
//
