CAPP_CHRVO
ID CAPP_CHRVO Reviewed; 898 AA.
AC Q7P206;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=CV_0055;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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; AE016825; AAQ57735.1; -; Genomic_DNA.
DR RefSeq; WP_011133610.1; NC_005085.1.
DR AlphaFoldDB; Q7P206; -.
DR SMR; Q7P206; -.
DR STRING; 243365.CV_0055; -.
DR EnsemblBacteria; AAQ57735; AAQ57735; CV_0055.
DR KEGG; cvi:CV_0055; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_4; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 398146at2; -.
DR Proteomes; UP000001424; 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..898
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166587"
FT ACT_SITE 134
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 564
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 898 AA; 98931 MW; 1F909AFD9E6C085E CRC64;
MSEHDKDLPL RADLACLDRL LSEVVGEQEG AVVSGAVQAI ALRRGDERSH PLPQLAPEAA
ASLLRACGLY AQLFNIAEDL HHNRRRRAHQ LAGSAPQQGS LPRALQRLRQ DGVSFHALHQ
LLSHAKVGAI LTAHPTEVQR QSVLDGHRAV RRFLSQLNAA DLTPEEREAL EAKLKRAILA
LWQTSEIRHF KMTVRDEITN GVAYHPLAFF EALPALYRRL EREIGQLWGE EARLPSFIRV
GSWIGGDRDG NPNVDAGLLR HAVTRQSQQA FEYYLQELKS LYRELSLSSR LVEAGAEVLA
LAEQSPDQAV SRGEEPYRRA LATMQGKLRA TARLRGVELA CRWDERAPYR DHRELIQDLA
SLSASLRAHG SALLADGRLS RLIRSVDVFG FFLMPLDLRQ HAAVHEGVVA ELFSAAGLEE
YRALDEAARV RVLIRELATP RLLFSPYLRY GEQAEKELAI FREAAAIQRD FGVEAIGQCI
ISNCASVSDI LALALLCKEA GLIRLEDGQP RASVNLVPLF ETIADLENSE AVMRALFALP
WYKQLLDSRE RVQEVMLGYS DSNKDGGYLT SQWQLWQAET RLVKVFADAG ARLQLFHGRG
GSVGRGGGPS YEAIVAQPAG SVAGRIRITE QGEVITAKYS DPAIAGRNLE ALVAATLEAS
LGNIPGGEVD TALFDELSAS AFAAYRALVE TPGFMQYFLE ATPVTAIARL NIGSRPASRK
SLSSIGDLRA IPWVFSWSQS RLMLPGWFGV GSAVAAYVQK HGDAGLAKLQ HLYRHSPFFQ
VMLSNMEQVL AKADLGIARR FSELVADREL AARLFGAIEA EWRKTHDAFF AITGQAELLE
GNPTLRRSLE TRLPFLDALG LLQADLLARL RAEPDDEDTL YAIHLTINGT SAGLRNTG
