PCKA_RHOPA
ID PCKA_RHOPA Reviewed; 537 AA.
AC Q9ZNH4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=RPA0360;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=7;
RX PubMed=10217755; DOI=10.1128/jb.181.9.2689-2696.1999;
RA Inui M., Nakata K., Roh J.H., Zahn K., Yukawa H.;
RT "Molecular and functional characterization of the Rhodopseudomonas
RT palustris no. 7 phosphoenolpyruvate carboxykinase gene.";
RL J. Bacteriol. 181:2689-2696(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels during log phase with 10-
CC 20 fold reduction at onset of stationary phase.
CC {ECO:0000269|PubMed:10217755}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000255|HAMAP-Rule:MF_00453}.
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DR EMBL; AB015618; BAA34956.1; -; Genomic_DNA.
DR EMBL; BX572594; CAE25804.1; -; Genomic_DNA.
DR RefSeq; WP_011155928.1; NC_005296.1.
DR AlphaFoldDB; Q9ZNH4; -.
DR SMR; Q9ZNH4; -.
DR STRING; 258594.RPA0360; -.
DR PRIDE; Q9ZNH4; -.
DR EnsemblBacteria; CAE25804; CAE25804; RPA0360.
DR GeneID; 66891371; -.
DR KEGG; rpa:RPA0360; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_5; -.
DR OMA; MRYAGEM; -.
DR PhylomeDB; Q9ZNH4; -.
DR BioCyc; RPAL258594:TX73_RS01855-MON; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001426; Chromosome.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Decarboxylase; Direct protein sequencing;
KW Gluconeogenesis; Lyase; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..537
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_0000203838"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 220
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 236..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT CONFLICT 41
FT /note="G -> S (in Ref. 1; BAA34956)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> T (in Ref. 1; BAA34956)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="S -> A (in Ref. 1; BAA34956)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..307
FT /note="EL -> DI (in Ref. 1; BAA34956)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="V -> A (in Ref. 1; BAA34956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 58772 MW; 9E43DBDE54089CCB CRC64;
MQETGVHNGA YGTDKFGLKN LKGVYWNFGA PQLYEHALKN GEAVLSSDGA LVADTGVFTG
RSPKDKFTVR DATTENTMWW GGNQSITAEQ FEALYQDFLK HAEGMTLFAQ DLYGGADPTF
RIKTRVYTEL AWHSLFIRTL LRRPERAELE NFVPELTLID LPSFRADPKR HGCRSENVVA
IDFARKIVLI GGTQYAGEMK KSVFTTLNYY LPEKGVLPMH CSANVGPNGD TAIFFGLSGT
GKTTLSADPN RTLIGDDEHG WGKDGVFNFE GGCYAKCIKL SSENEPEIYA ASTRFGAVLE
NVVLGELDRK PDFDDGSKTE NTRSAYPLES IPNASLTGRA GQPKNVVMLA ADAFGVMPPI
AKLTPAQAMY HFLSGYTAKV AGTERGVTEP TPEFSTCFGS PFLPRDPSVY GNMLRELIAK
HNVDCWLVNT GWTGGIYGTG HRMPIKVTRA LLTAALDGSL RNVEFRTDPY FGFAVPTALP
GVPSEILDPV KTWADKAAFD TTARKLVGMF QKNFAKFEAQ VDAEVRAAAP DVKMAVE
