PCKA_VIBPA
ID PCKA_VIBPA Reviewed; 542 AA.
AC Q87TE1;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000255|HAMAP-Rule:MF_00453};
DE Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453};
DE Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453};
GN Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453}; OrderedLocusNames=VP0129;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC phosphoryl transfer between the nucleoside triphosphate and OAA.
CC {ECO:0000255|HAMAP-Rule:MF_00453}.
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:0000255|HAMAP-Rule:MF_00453};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00453};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00453}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000255|HAMAP-Rule:MF_00453}.
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DR EMBL; BA000031; BAC58392.1; -; Genomic_DNA.
DR RefSeq; NP_796508.1; NC_004603.1.
DR RefSeq; WP_005478630.1; NC_004603.1.
DR AlphaFoldDB; Q87TE1; -.
DR SMR; Q87TE1; -.
DR STRING; 223926.28805111; -.
DR EnsemblBacteria; BAC58392; BAC58392; BAC58392.
DR GeneID; 1187596; -.
DR KEGG; vpa:VP0129; -.
DR PATRIC; fig|223926.6.peg.121; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_6; -.
DR OMA; MRYAGEM; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
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 PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR TIGRFAMs; TIGR00224; pckA; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..542
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_0000203855"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 214
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 249..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 450..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
SQ SEQUENCE 542 AA; 60012 MW; 0D16A98AF33AAA47 CRC64;
MTVMEHTKAA TLDLTKHGLH NVKEVVRNPS YELLFEEETR ADLTGYERGV VTELGAVAVD
TGIFTGRSPK DKYIVKDATT EEHMWWTSDT VKNDNKPITQ EVWNDLKELV TNQLSGKRLF
VVDGYCGANP DTRLSIRVIT EVAWQAHFVK NMFIRPTEEE LATFEPDFVV MNGAKCTNPK
WEEQGLNSEN FTVFNLTERT QLIGGTWYGG EMKKGMFAMM NYFLPLKDIA SMHCSANMGK
DGDVAVFFGL SGTGKTTLST DPKRALIGDD EHGWDDDGVF NFEGGCYAKT IKLSKEAEPD
IYNAIRRDAL LENVTVRSDG SIDFDDGSKT ENTRVSYPIY HIENIVKPVS KGGHANKVIF
LSADAFGVLP PVSKLTPEQT KYHFLSGFTA KLAGTERGIT EPTPTFSACF GAAFLTLHPT
KYAEVLVKRM EAAGAEAYLV NTGWNGTGKR ISIQDTRGII DAILDGSIED APTKHIPIFN
LEVPTSLPGV DPSILDPRDT YVDPLQWESK AKDLAERFIN NFDKYTDNAE GKALVAAGPQ
LD
