ID Q94LX8_FLATR Unreviewed; 662 AA.
AC Q94LX8;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN Name=pck3-19 {ECO:0000313|EMBL:BAB43908.1};
OS Flaveria trinervia (Clustered yellowtops) (Oedera trinervia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Tageteae; Flaveria.
OX NCBI_TaxID=4227 {ECO:0000313|EMBL:BAB43908.1};
RN [1] {ECO:0000313|EMBL:BAB43908.1}
RP NUCLEOTIDE SEQUENCE.
RA Izumida A., Furumoto T., Toh H., Hata S., Izui K.;
RT "Elevated expression of the gene for phosphoenolpyruvate carboxykinase in
RT leaves of Flaveria trinervia, an NADP-dependent malic enzyme-type C4 dicot
RT and its possible implication in the evolution of C4 photosynthesis in
RT Flaveria.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAB43908.1}
RP NUCLEOTIDE SEQUENCE.
RA Izumida A., Furumoto T., Toh H., Shingo H., Izui K.;
RT "Elevated expression of the gene for phosphoenolpyruvate carboxykinase in
RT leaves of Flaveria trinervia, an NADP-dependent malic enzyme-type C4 dicot
RT and its possible implication in the evolution of C4 photosynthesis in
RT Flaveria.";
RL Submitted (OCT-2000) 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; AB050472; BAB43908.1; -; mRNA.
DR AlphaFoldDB; Q94LX8; -.
DR UniPathway; UPA00138; -.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Kinase {ECO:0000313|EMBL:BAB43908.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:BAB43908.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:BAB43908.1};
KW Transferase {ECO:0000313|EMBL:BAB43908.1}.
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 73153 MW; 9833D4B175141E74 CRC64;
MASSGNGNVA GKGNAVSGGR NGLPKIQTQK RQNGICHDDS SAPVKVQTID ELHSLQRKKS
APTTPLDGVQ GAFANMSEDD RQKQQLQSIS ASLASLTRET GPKVVRGDPA RRPETPRVAH
GPDHYFTPTF AASDSSLKFT HVLYNLSPAE LYEQAIKYEK GSFITSSGAL ATLSGAKTGR
SPKDKRVVRD DVTENELWWG KGSPNIEMDE QTFLVNRERA VDYLNSLEKV FVNDQFLNWD
PENRIKVRIV SARAYHSLFM HNMCIRPSPE ELENFGTPDF TIYNAGQFPC NRYTHYMTSS
TSIDLNLGRR EMVILGTQYA GEMKKGLFGV MHYLMPKRQI LSLHSGCNMG KDGDVALFFG
LSGTGKTTLS TDHNRYLIGD DEHCWSDKGV SNIEGGCYAK CIDLSKEKEP DIWNAIKFGT
VLENVVFDEH TREVDYLDKS VTENTRAAYP IEYIPNAKIP CVGPHPKNVI LLACDAFGVL
PPVSKLSLAQ TMYHFISGYT ALVAGTEEGV KEPRATFSAC FGAAFIMLHP TKYAEMLASK
MEKHGATGWL VNTGWSGGSY GAGSRMKLAY TRKIIDAIHS GKLLNANYKK TEVFGLEIPT
EVESVPSEIL DPVNTWSNKK AYKETLLKLA GLFKNNFEVF VNHKIGKDDK LTQEILAAGP
NF
//
