ID W6MNM2_9ASCO Unreviewed; 558 AA.
AC W6MNM2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00021932};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN ORFNames=KUCA_T00004213001 {ECO:0000313|EMBL:CDK28231.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK28231.1};
RN [1] {ECO:0000313|EMBL:CDK28231.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28231.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK28231.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28231.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; HG793129; CDK28231.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MNM2; -.
DR STRING; 1382522.W6MNM2; -.
DR HOGENOM; CLU_018247_0_1_1; -.
DR OrthoDB; 3740611at2759; -.
DR UniPathway; UPA00138; -.
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}.
SQ SEQUENCE 558 AA; 61820 MW; 7723D5AAF1A432A7 CRC64;
MAPTAIDLHH SYSESLPVSA PSQKASRKDS VIAKLGLNPD AVIHYNSAVP ILYEDALKEK
GTSISSTGAL VAYSGSKTGR SPKDKRIVDE ETSTENIWWG PVNKKVDETT WKISKSRAID
YLRTREKIFI IDAFAGWDPR YRIKVRIVCA RAYHALFMKN MLIQPTEEEL KNFGEPDFTI
WNAGQFPANV FTKGMTSSTS VEINFKDMEM VILGTEYAGE MKKGIFTVMF YLMPIRHKVL
TLHSSANQGT VSGDVTLFFG LSGTGKTTLS ADPNRKLIGD DEHCWSDHGV FNIEGGCYAK
CLDLSAEKEP EIFNAIKFGS VLENIVYDPI SKVVDYENKD ITENTRCAYP IDFIPSAKIP
CLADRHPSNI VLLTCDARGV LPPISKLTNA QVMYHFISGY TSKMAGTEDG VTEPEATFSA
CFGQPFLVLH PMKYAQQLSD KISEHKSNAW LLNTGWTGSS AAKGGKRCPL KYTRRILDAI
HSGELNDAEY ETYPTFGLQI PKSVPGVPAE ILNPSKNWAE GPEKFSGDVR NLAQLFLENF
EKYSSEVTEV VKAAGPQL
//
