(data stored in SCRATCH9089 zone)

SWISSPROT: CAPP_PASMU

ID   CAPP_PASMU              Reviewed;         879 AA.
AC   Q9CN89;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=PM0546;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
DR   EMBL; AE004439; AAK02630.1; -; Genomic_DNA.
DR   RefSeq; WP_005726336.1; NC_002663.1.
DR   SMR; Q9CN89; -.
DR   PRIDE; Q9CN89; -.
DR   EnsemblBacteria; AAK02630; AAK02630; PM0546.
DR   GeneID; 29388785; -.
DR   KEGG; pmu:PM0546; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   BioCyc; PMUL272843:G1FZ8-577-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CN89.
DR   SWISS-2DPAGE; Q9CN89.
KW   Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..879
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166607"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   879 AA;  99397 MW;  59FB7989C6E6C406 CRC64;
     MIQQYSTMRN NISMLGRFLG ETISDAQGSD ILELIENIRV LSRNSRHGDD QARNALLNTL
     ATISNENIIP VARAFSQFLN LTNIAEQYQT ISRHHHDHVA SERSISALFK RLKAQQVPKE
     NVMETVQKLL IELVLTAHPT EVTRRSLVHK HVEINKCLSK LEHTDLTDAE RKAIERRLLQ
     LIAQAWHTNE IRTQRPTPFE EAKWGFAVIE NSLWQAVPEF LRHLNTSAVE YFGFHLPVEL
     NPIRFSSWMG GDRDGNPFVT AEVTRQVLRL ARWKAADLFL TDIQALSDEL SVVKCTPEFQ
     AKYGSHVEPY RTVVKALRSK LTATLAYYDD LLANRTPRVA EEDIITQDAQ LWEPLYDCYQ
     SLQACGMRII ANGLLLDCLR RIRCFGVTLS RLDIRQESTR HAEAIAEITR YIGLGDYAQW
     SESDKQAFLI KELSSRRPLL PREWQPSAAT QEVLDTCRVI AEQPEGVISC YIISMAKTAS
     DVLAVHLLLK ESGVPYHLPV VPLFETLDDL RASEQVMSEL FNIGWYRGVI NNKQMVMIGY
     SDSAKDAGMM AASWAQYCAQ EALVNLCDKC NIELTLFHGR GGTIGRGGAP AHAALLSQPP
     RSLKNGLRVT EQGEMIRFKL GLPAVAVESL GLYASAILEA NLLPPPEPKA QWRTVMDELS
     TISCQIYRDV VRGEKDFVPY FRAATPEQEL SKLPLGSRPA KRNPNGGVES LRAIPWIFAW
     MQNRLMLPAW LGAGASLRQA IEKGQKTVIE DMCKTWPFFS TRIGMLEMVF SKTDTWLSEH
     YDQHLVDPAL WYLGESLREQ LKQDIQTVLS LSHEDQLMSD LPWIAESIAL RNVYTDPLNL
     LQVELLRRLR RNPDNPNPDV EQALMITITG VAAGMRNTG
//

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