PCKA_SINFN
ID PCKA_SINFN Reviewed; 536 AA.
AC P43086; C3MBB5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=NGR_c33940;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1720862; DOI=10.1007/bf00290676;
RA Oesteraas M., Finan T.M., Stanley J.;
RT "Site-directed mutagenesis and DNA sequence of pckA of Rhizobium NGR234,
RT encoding phosphoenolpyruvate carboxykinase: gluconeogenesis and host-
RT dependent symbiotic phenotype.";
RL Mol. Gen. Genet. 230:257-269(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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; X63291; CAA44925.1; -; Genomic_DNA.
DR EMBL; CP001389; ACP27124.1; -; Genomic_DNA.
DR RefSeq; WP_012709871.1; NC_012587.1.
DR RefSeq; YP_002827877.1; NC_012587.1.
DR AlphaFoldDB; P43086; -.
DR SMR; P43086; -.
DR STRING; 394.NGR_c33940; -.
DR EnsemblBacteria; ACP27124; ACP27124; NGR_c33940.
DR KEGG; rhi:NGR_c33940; -.
DR PATRIC; fig|394.7.peg.6243; -.
DR eggNOG; COG1866; Bacteria.
DR HOGENOM; CLU_018247_0_1_5; -.
DR OMA; MRYAGEM; -.
DR OrthoDB; 146648at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001054; 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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..536
FT /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT /id="PRO_0000203837"
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 322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT CONFLICT 148
FT /note="A -> G (in Ref. 1; CAA44925)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="G -> A (in Ref. 1; CAA44925)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..418
FT /note="IA -> MP (in Ref. 1; CAA44925)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..462
FT /note="SA -> RP (in Ref. 1; CAA44925)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="G -> AD (in Ref. 1; CAA44925)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="D -> A (in Ref. 1; CAA44925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 58146 MW; CF68F6D6417D5187 CRC64;
MEQLGTRNPS NGLETIGFSD LSVVRYNFEA AELYEEALRR GEAQLTAHGA LCARTGQHTG
RSPKDKYVVR DAATGDQIWW DNNSAISPEN FERLRQDMLA HAKGMSLYVQ DLVGGADQEN
ALPTRVVTEF AWHSLFIRNL LIRPPREALA SFLPKLTIID LPSFKANPER HGCRGETIIA
CDLTKGLVLI GGTSYAGEMK KSVFTVLNYL LPNKAVMPMH CSANVGPAGD TAIFFGLSGT
GKTTLSADPN RTLIGDDEHG WSDKGVFNFE GGCYAKAIRL SEAAEPEIFA TTRRFGTVME
NVVLDERRAP DFDNGSLTEN TRIAYPLDFI PNASETGTAP QPRTIIMLTA DAFGVLPPIA
KLTPEQAMYH FLSGYTAKVA GTEKGVTEPE ATFSTCFGAP FMPRHPSEYG NLLKDLIARN
GVTCWLVNTG WTGGAYGTGS RMPIKVTRAL LSAALDGSLN SAAFRTDANF GFAVPVSVPG
VDDRILDPRS TWSDGQAYDA QARRLVDMFI ANFAKFESHV DGSVRDAAPG TKLAAE
