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 13-SEP-2023, entry version 108.
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; Pseudomonadota; 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; 3.90.228.20; -; 1.
DR Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 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 NCBIfam; TIGR00224; pckA; 1.
DR PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 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
//
