PCKA_RHOPB
ID PCKA_RHOPB Reviewed; 537 AA.
AC Q21BR2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=RPC_0599;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000255|HAMAP-Rule:MF_00453}.
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DR EMBL; CP000301; ABD86174.1; -; Genomic_DNA.
DR RefSeq; WP_011471082.1; NC_007925.1.
DR AlphaFoldDB; Q21BR2; -.
DR SMR; Q21BR2; -.
DR STRING; 316056.RPC_0599; -.
DR EnsemblBacteria; ABD86174; ABD86174; RPC_0599.
DR KEGG; rpc:RPC_0599; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_5; -.
DR OMA; MRYAGEM; -.
DR OrthoDB; 146648at2; -.
DR UniPathway; UPA00138; -.
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.
FT CHAIN 1..537
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_1000026344"
FT REGION 312..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 537 AA; 58390 MW; B8E2D8BB460FE47E CRC64;
MQETGVRNGA YGADKFGLKN LKGVKWNLTA PHLYEDALRA GEGVLSGDGS LCVDTGIFTG
RSPKDKYTVR DANTENTMWW GGNQSITAEQ FENLYQDFLK HAEGMSLFAQ DLYGGADPSF
QIKTRVFTEM AWHSLFIRTL LRRPETAELA SFVPELTIID LASFRADPAR HGCKSENVVA
IDFTRKIVLI GGTQYAGEMK KSVFTTLNYY LPDKGVLPMH CSANVGPDGD TAIFFGLSGT
GKTTLSADPN RTLIGDDEHG WGKDGVFNFE GGCYAKCIKL SAEAEPEIFA ASNRFGAILE
NCVLDPITRK PDFNDGSKTE NTRSAYPLES IPNASPTGRA GQPKNVVMLA ADAFGVMPPI
AKLSPAQAMY HFLSGYTAKV AGTERGVTEP TPVFSTCFGS PFLPRDPSVY GNMLRELIAK
HGVDCWLVNT GWTGGMYGTG HRMPIKVTRA LLTAALDGSL RNVEFKTDPY FGFAVPTALP
GVPSEILDPV KTWADKAAFD TTARKLVAMF QKNFTQFEAQ VDAEVRAAQP EAKLAAE
