PCKA_MAIZE
ID PCKA_MAIZE Reviewed; 666 AA.
AC Q9SLZ0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP);
DE Short=PEP carboxykinase;
DE Short=PEPCK;
DE EC=4.1.1.49;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. H84; TISSUE=Bundle sheath strand;
RX PubMed=10598098; DOI=10.1023/a:1006317120460;
RA Furumoto T., Hata S., Izui K.;
RT "cDNA cloning and characterization of maize phosphoenolpyruvate
RT carboxykinase, a bundle sheath cell-specific enzyme.";
RL Plant Mol. Biol. 41:301-311(1999).
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;
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000305}.
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DR EMBL; AB018744; BAA36483.1; -; mRNA.
DR AlphaFoldDB; Q9SLZ0; -.
DR SMR; Q9SLZ0; -.
DR STRING; 4577.GRMZM2G001696_P02; -.
DR PaxDb; Q9SLZ0; -.
DR PRIDE; Q9SLZ0; -.
DR eggNOG; ENOG502QQI5; Eukaryota.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9SLZ0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR CDD; cd00484; PEPCK_ATP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 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 PANTHER; PTHR30031; PTHR30031; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR TIGRFAMs; TIGR00224; pckA; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..666
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_0000203864"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 364..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 666 AA; 73314 MW; 813392EF13BF91D3 CRC64;
MATPNGLARI ETTGKKKQDN GVWYDDSSAP VRAQTIDELH SLQRKRSAPT TPNRSAPTTP
IKGGAHSPFA VAISEEERHT QQMQSISASL ASLTRETGPK VVKGDPAAKG EAAAQGAPST
PRAHQQHRHP AAPAIAVSDS SLKFTHVLNN LSPAELYEQA IKYEKGSFIT STGALATLSG
AKTGRSPRDK RVVKDEVTAQ DLWWGKGSPN IEMDEKTFLI NRERAVDYLN SLKVVRQRQL
LNWDPENRIK VRIISARAYH SLFMHNMCIR PTDEELEDFG TPDFTIYNAG QFPCNRYTHY
MTSSTSIDLN LARREMVIMG TQYAGEMKKG LFGVMHYLMP KRGILSLHSG CNMGKDGDVA
LFFGLSGTGK TTLSTDHNGL LIGDDEHCWS DNGVSNIEGG CYAKCIDLAQ EKEPDIWNAI
KFGTVLENVV FDEHTREVDY ADYSVTENTR AAYPIEYIPI AKIPCVGPHP KNVILLACDA
FGVLPPVSKL ILAQTMYHFI SGYTALVAGT EDGIKEPQAT FSACFGAAFI MLHPTKYAAM
LAEKMQKYGA TGWLVNTGWS GGRYGVGKRI RLPYTRKIID AIHSGELLTA NYQKTEVFGL
EIPTEINGVP SEILDPIYTW TDKAAYKENL LRLGGLFKNN FEVFASYKIG DDSSLTDEIL
AAGPNF