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PCKA_ANASU
ID   PCKA_ANASU              Reviewed;         532 AA.
AC   O09460;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
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};
OS   Anaerobiospirillum succiniciproducens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Succinivibrionaceae; Anaerobiospirillum.
OX   NCBI_TaxID=13335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 29305 / DSM 6400 / LMG 7826 / NCTC 11536 / S411;
RX   PubMed=9172347; DOI=10.1128/aem.63.6.2273-2280.1997;
RA   Laivenieks M., Vieille C., Zeikus J.G.;
RT   "Cloning, sequencing, and overexpression of the Anaerobiospirillum
RT   succiniciproducens phosphoenolpyruvate carboxykinase (pckA) gene.";
RL   Appl. Environ. Microbiol. 63:2273-2280(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-19, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RX   PubMed=8436945; DOI=10.1099/00221287-139-2-223;
RA   Podkovyrov S.M., Zeikus J.G.;
RT   "Purification and characterization of phosphoenolpyruvate carboxykinase,a
RT   catabolic CO2-fixing enzyme, from Anaerobiospirillum succiniciproducens.";
RL   J. Gen. Microbiol. 139:223-228(1993).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP; MANGANESE AND
RP   SUBSTRATE ANALOGS.
RX   PubMed=15890557; DOI=10.1016/j.biocel.2005.03.008;
RA   Cotelesage J.J., Prasad L., Zeikus J.G., Laivenieks M., Delbaere L.T.;
RT   "Crystal structure of Anaerobiospirillum succiniciproducens PEP
RT   carboxykinase reveals an important active site loop.";
RL   Int. J. Biochem. Cell Biol. 37:1829-1837(2005).
CC   -!- FUNCTION: Involved in gluconeogenesis. Catalyzes the conversion of
CC       oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC       phosphoryl transfer between the nucleoside triphosphate and OAA (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:8436945,
CC       ECO:0000269|PubMed:9172347}.
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         ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00453,
CC         ECO:0000269|PubMed:8436945};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453,
CC       ECO:0000269|PubMed:8436945};
CC   -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate.
CC       {ECO:0000269|PubMed:8436945}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.42 mM for ADP (at 37 degrees Celsius and at pH 6.2)
CC         {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC         KM=0.54 mM for PEP (at 37 degrees Celsius and at pH 6.2)
CC         {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC         KM=1.2 mM for OAA (at 37 degrees Celsius and at pH 6.2)
CC         {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC         KM=2.3 mM for ATP (at 37 degrees Celsius and at pH 6.2)
CC         {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC         KM=17 mM for bicarbonate (at 37 degrees Celsius and at pH 6.2)
CC         {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC         Vmax=10 umol/min/mg enzyme (at 37 degrees Celsius and at pH 6.2)
CC         {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC       pH dependence:
CC         Optimum pH is between 6.7 and 7.1. The enzyme is stable from pH 5.0
CC         to 9.0. It completely losing activity at pH values lower than 4.5 and
CC         retaining some activity in the pH range 9-12.
CC         {ECO:0000269|PubMed:8436945, ECO:0000269|PubMed:9172347};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00453,
CC       ECO:0000269|PubMed:15890557, ECO:0000269|PubMed:8436945}.
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; U95960; AAC45394.1; -; Genomic_DNA.
DR   PDB; 1YTM; X-ray; 2.20 A; A/B=1-532.
DR   PDB; 1YVY; X-ray; 2.35 A; A/B=1-532.
DR   PDBsum; 1YTM; -.
DR   PDBsum; 1YVY; -.
DR   AlphaFoldDB; O09460; -.
DR   SMR; O09460; -.
DR   BRENDA; 4.1.1.49; 330.
DR   SABIO-RK; O09460; -.
DR   UniPathway; UPA00138; -.
DR   EvolutionaryTrace; O09460; -.
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   3D-structure; ATP-binding; Cytoplasm; Decarboxylase;
KW   Direct protein sequencing; Gluconeogenesis; Lyase; Manganese;
KW   Metal-binding; Nucleotide-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8436945"
FT   CHAIN           2..532
FT                   /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT                   /id="PRO_0000203801"
FT   BINDING         60
FT                   /ligand="substrate"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         206
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT                   ECO:0000269|PubMed:15890557"
FT   BINDING         206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         225
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT                   ECO:0000269|PubMed:15890557"
FT   BINDING         242..250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:15890557"
FT   BINDING         244
FT                   /ligand="substrate"
FT   BINDING         263
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT                   ECO:0000269|PubMed:15890557"
FT   BINDING         291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT                   ECO:0000269|PubMed:15890557"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         443..444
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT                   ECO:0000269|PubMed:15890557"
FT   BINDING         449
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453,
FT                   ECO:0000269|PubMed:15890557"
FT   HELIX           3..9
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           24..31
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           92..106
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          107..120
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          126..133
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           135..144
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          159..165
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   TURN            171..177
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   TURN            188..191
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          192..197
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           203..215
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           217..219
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          222..231
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          236..241
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           248..252
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          257..267
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          272..275
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          277..282
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   TURN            288..290
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           292..297
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          303..306
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          327..331
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           332..334
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          335..338
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          341..346
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          348..355
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          364..367
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           370..379
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          381..384
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          396..399
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           401..403
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           405..407
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           412..426
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          429..434
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          441..443
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           446..457
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           460..463
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          466..469
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   TURN            470..473
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          474..478
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           486..488
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           490..493
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   STRAND          494..496
FT                   /evidence="ECO:0007829|PDB:1YTM"
FT   HELIX           497..515
FT                   /evidence="ECO:0007829|PDB:1YTM"
SQ   SEQUENCE   532 AA;  58643 MW;  983ABC71930F9E44 CRC64;
     MSLSESLAKY GITGATNIVH NPSHEELFAA ETQASLEGFE KGTVTEMGAV NVMTGVYTGR
     SPKDKFIVKN EASKEIWWTS DEFKNDNKPV TEEAWAQLKA LAGKELSNKP LYVVDLFCGA
     NENTRLKIRF VMEVAWQAHF VTNMFIRPTE EELKGFEPDF VVLNASKAKV ENFKELGLNS
     ETAVVFNLAE KMQIILNTWY GGEMKKGMFS MMNFYLPLQG IAAMHCSANT DLEGKNTAIF
     FGLSGTGKTT LSTDPKRLLI GDDEHGWDDD GVFNFEGGCY AKVINLSKEN EPDIWGAIKR
     NALLENVTVD ANGKVDFADK SVTENTRVSY PIFHIKNIVK PVSKAPAAKR VIFLSADAFG
     VLPPVSILSK EQTKYYFLSG FTAKLAGTER GITEPTPTFS SCFGAAFLTL PPTKYAEVLV
     KRMEASGAKA YLVNTGWNGT GKRISIKDTR GIIDAILDGS IDTANTATIP YFNFTVPTEL
     KGVDTKILDP RNTYADASEW EVKAKDLAER FQKNFKKFES LGGDLVKAGP QL
 
 
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