ID   CAPP_AROAE              Reviewed;         916 AA.
AC   Q5P7H5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 98.
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=AZOSEA06140;
GN   ORFNames=ebA1167;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI06736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR555306; CAI06736.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041645647.1; NC_006513.1.
DR   AlphaFoldDB; Q5P7H5; -.
DR   SMR; Q5P7H5; -.
DR   STRING; 76114.ebA1167; -.
DR   KEGG; eba:ebA1167; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000006552; 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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 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..916
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166579"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        578
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   916 AA;  101239 MW;  4A45C86CF16B69EC CRC64;
     MTEDKDAPLR EDIRLLGRVL GDTVRDQHGE AAFALIERIR QTSVRFRRDD DNAARLELEG
     ILDALSREQT IEVVRAFSYF SHLSNIAEDQ HHIRRSRAHL IAGSAPREGS VAHALVRALA
     SGLPPARLAA FFDTALISPV LTAHPTEVQR KSILNCETDI AHLLDARDRM TLTPEERQES
     DEALRRTVLT LWQTRMLRPA KLSVVDEVAN GLSYFDATFL RELPHLYANL EDQLVSRDPA
     LAGLELPAFL QVGSWIGGDR DGNPFVTADV LERTLAMQAG AVLGFYLDEL HALGARLSLA
     LGLVTASDAL LALAARSPDH SPHRNDEPYR RAISGIYARL AATHHALLGT EPPRHPVAVA
     EPYAAVAELA DDLDVIHRSL VANGSAALAR GQLRRLRRAV RVFGFHLAPI DLRQNSEVHE
     RVVAELLATA RTGTDYATLD EAARVELLIE ELATPRPLAS PHVRYSDETE GELAIFRTAR
     AAHRRYGGPA IPNCIISKTD DVSDLLELAL LLKEAGLLRP HERALDVNIV PLFETIEDLA
     NAPSVMDRLF ALPGYMNLLA ASRDRTHEVM LGYSDSNKDG GFLTSGWALY KAEIGLIEVF
     ARHGIRLRLF HGRGGSVGRG GGPSYEAILA QPGGAVQGQI RLTEQGEVIA AKYGNPEVGR
     RNLEVIVAAT LEASLLADRA PAPRVEFLDT MQALSDVAFA AYRGLVYDTE GFERYFWEST
     VISEIAELNI GSRPASRKKG TRIEDLRAIP WVFSWSQCRL MLPGWFGFGS AVKTWLAAHA
     DDGIARLQAM HREWSFFAAL LSNMDMVLAK TDLAIASRYA GLVKDVNLRD AIFERIRNEW
     HDTVDALLAI TGQRELLDGN PLLKRSIRNR FPYLDPLNHV QVELLRRHRE THDDARIRLG
     IHISINGIAA GLRNSG
//