CAPP_HAEIE
ID CAPP_HAEIE Reviewed; 879 AA.
AC A5UCN0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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};
GN OrderedLocusNames=CGSHiEE_05850;
OS Haemophilus influenzae (strain PittEE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374930;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittEE;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; CP000671; ABQ98531.1; -; Genomic_DNA.
DR RefSeq; WP_012054432.1; NC_009566.1.
DR AlphaFoldDB; A5UCN0; -.
DR SMR; A5UCN0; -.
DR KEGG; hip:CGSHiEE_05850; -.
DR HOGENOM; CLU_006557_2_0_6; -.
DR OMA; PWVFGWT; -.
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.
FT CHAIN 1..879
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000025560"
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; 100163 MW; 857594007A8619FE CRC64;
MTQEYSTLRN NISMLGRFLG ETINDAQGED ILELIENIRK LSRNSRAGDD KARQALLDTL
GSISNENIIP VARAFSQFLN LTNIAEQYQT ISREHSLAQS SSQSLSELFK RLKEQNASVE
EVHKTVEKLL IELVLTAHPT ETTRRSLIHK HIEINKCLSK LEHHDLTEKE RNIIERLLLR
LIAEAWHTNE IRTVRPTPFD EAKWGFAMLE NSLWQAVPEF LRQLNETARE FLGYDLPVGL
KPVRISSWMG GDRDGNPFVT AQITKKVLYF ARWKAADLFL QDISKLADEL SMMKCSDEFR
DKYGEHLEPY RFVVKNLRNQ LTATLAYFDD HLSNRTPRVS ESEIILEDNQ LWEPLYDCYQ
SLIQYGMRII ANGSLLNILH RISCFGVTLS QMDIRQESTR HTDAIAEITR YIGLGDYAQW
TEDDKQAFLI RELSSRRPLI PQNWTPSPET QEILDTCKVI AQQKQGVIAC YVISMARNAS
DVLAVHLLLK EAGVPYHIPV VPLFETLEDL DAAEKVMTQL FNVGWYRGVI NNRQMVMIGY
SDSAKDAGMM AASWAQYRAQ EALVNLTEKL GIELTLFHGR GGTIGRGGAP AHAALLSQPP
RSLKNGLRVT EQGEMIRFKL GLPTVAVETF DLYASAILEA NLLPPPEPKP EWRNIMDELS
TISCDIYRGV VRGDKDFVPY FRSATPEQEL SKLPLGSRPA KRNPNGGVES LRAIPWIFAW
MQNRLMLPAW LGAGASIRQI IEQGKGDIIH KMCENWPFFS TRIGMLEMVF SKSDTWLSQQ
YDQRLVKKEL WYLGENLRKQ LEDDIQTVLS LSHQSELMSD LPWIADSIAL RNIYTDPLNL
LQVELLHRFR ENPEQVNPDV EQALMITITG IAAGMRNTG