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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
 
 
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