ID   CAPP_AZOSB              Reviewed;         917 AA.
AC   A1K454;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=azo0992;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; Evidence={ECO:0000255|HAMAP-
CC         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; AM406670; CAL93609.1; -; Genomic_DNA.
DR   RefSeq; WP_011764726.1; NZ_CP016210.1.
DR   AlphaFoldDB; A1K454; -.
DR   SMR; A1K454; -.
DR   STRING; 62928.azo0992; -.
DR   KEGG; aoa:dqs_1093; -.
DR   KEGG; azo:azo0992; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002588; 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..917
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025548"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        578
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   917 AA;  101775 MW;  5786E67108799AA7 CRC64;
     MTPDKDAPLR EDIRLLGRLL GDTVRDQQGA ASFDLIERIR QTSVRFRRDE DLAARRELED
     TLDALSREQT IQVVRAFSYF SHLANIAEDQ HHIRRSRAHL LAGSAPREGS LAHAVGHALD
     EQRLDPTDLA AFFDTALISP VLTAHPTEVQ RKSILNCQTV IARLLDERDR MQLTPDEAEA
     NLDALRRAVL TLWQTRMLRP AKLSVIDEVN NGLSYFETTF LRELPRLYAA LEDRLAGAQP
     ALANHELPAF LQVGSWIGGD RDGNPYVTAD VLEEALAMQA RVALDYYLDE LHTLGSQLSL
     SQGLVGASDA LLALADRSPD QSPHRSDEPY RRAIAGIYAR LSATYRNLLG HPPARHAVAE
     AEPYADVAAL ADDLDTLHRS LVANGTAALA RGRLRHLRRA VRVFGFHLAP IDLRQNSDVH
     ERVVAELLEV ARPGAAYLAQ DEAGRCALLL DELATARPLA SPHVRYSDDS EGELAIFRAA
     RRAHLRYGRG AIHNCIISKT DDLSDLLELA VLLKEAGLLR PLEKALDVNI VPLFETIGDL
     ENAAGVMDRL FSIPVYRELL AARDQTQEVM LGYSDSNKDG GFLTSGWALY KAEGELVEVF
     GRHGVRLRLF HGRGGSVGRG GGPSYQAILA QPDGAVQGQI RLTEQGEVIA AKYGNPEVGR
     RNLEVLVAAT LETSLRRDGG DATPRTFLDT MQALSDAAFT CYRGLVYETP GFEQYFWEST
     VISEIAGLNI GSRPASRKKG TRIDDLRAIP WVFSWSQCRL MLPGWFGFGS AVKQWLAAHP
     KDGLGLLQRM YREWSFFATL LSNMDMVLSK TDLAIASRYA ELVKDPVLRD SIFERIRSEW
     KDTVDALLAI TEQVELLDAN PLLKRSIRNR FPYLDPLNHV QVELLRRHRE GNGEDARIRN
     GIHISINGIA AGLRNSG
//