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 25-MAY-2022, entry version 107.
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}.
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DR EMBL; AE004439; AAK02630.1; -; Genomic_DNA.
DR RefSeq; WP_005726336.1; NC_002663.1.
DR AlphaFoldDB; Q9CN89; -.
DR SMR; Q9CN89; -.
DR STRING; 747.DR93_1323; -.
DR EnsemblBacteria; AAK02630; AAK02630; PM0546.
DR KEGG; pmu:PM0546; -.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
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;
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