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Database: UniProt/TrEMBL
Entry: A0A1D9LIU8_9NEIS
LinkDB: A0A1D9LIU8_9NEIS
Original site: A0A1D9LIU8_9NEIS 
ID   A0A1D9LIU8_9NEIS        Unreviewed;       898 AA.
AC   A0A1D9LIU8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=BKX93_15160 {ECO:0000313|EMBL:AOZ51208.1};
OS   Chromobacterium vaccinii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=1108595 {ECO:0000313|EMBL:AOZ51208.1, ECO:0000313|Proteomes:UP000178776};
RN   [1] {ECO:0000313|EMBL:AOZ51208.1, ECO:0000313|Proteomes:UP000178776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=21-1 {ECO:0000313|EMBL:AOZ51208.1,
RC   ECO:0000313|Proteomes:UP000178776};
RA   Sparks M.E., Blackburn M.B., Gundersen-Rindal D.E., Mitchell A., Farrar R.,
RA   Kuhar D.;
RT   "Chromobacterium muskegensis sp. nov., an insecticidal bacterium isolated
RT   from Sphagnum bogs.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP017707; AOZ51208.1; -; Genomic_DNA.
DR   RefSeq; WP_070980459.1; NZ_CP017707.1.
DR   AlphaFoldDB; A0A1D9LIU8; -.
DR   STRING; 1108595.BKX93_15160; -.
DR   GeneID; 68842547; -.
DR   KEGG; cvc:BKX93_15160; -.
DR   Proteomes; UP000178776; 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 {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:AOZ51208.1}.
FT   ACT_SITE        134
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        564
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   898 AA;  99136 MW;  0651A3FB53D8E77D CRC64;
     MSDHDKDLPL RADLACLDRL LSEVVGEQEG AVVSGAVQAI ALRRGDERSH PLPQLAPEAA
     ASLLRACGLY AQLFNIAEDL HHNRRRRAHQ LAGSAPQQGS LPRALQRLRQ DGVSFHALHQ
     LLSHARVGAI LTAHPTEVQR QSVLDGHRAV RRFLSQLNAP DLTPEEREEL EAKLKRAILA
     LWQTSEIRHF KMTVRDEITN GVAYHPLAFF EALPALYRRL EREIGQLWGE EARLPSFIRV
     GSWIGGDRDG NPNVDAGLLR HAVTRQAQQA FEHYLQELKS LYRELSLSSR LVEAGAEVLA
     LAEQSPDQAV SRGEEPYRRA LATMQGKLRA TARLRGVELA CRWDERAPYR DHRELIQDLA
     SLSASLRAHG SALLADGRLS RLIRSVDVFG FFLMPLDLRQ HAAVHEGVVA ELFSAAGLEE
     YRALDEAARV RVLTRELATP RLLFSPYLRY GEQAEKELAI FREAAAIQRE FGVEAIGQCI
     ISNCASVSDI LALALLCKEA GLIRLEDGQP RASVNLVPLF ETIADLENSE TVMRALFALP
     WYKQLLDSRE RVQEVMLGYS DSNKDGGYLT SQWQLWQAET RLVRVFADAG ARLQLFHGRG
     GSVGRGGGPS YEAIVAQPAG SVAGRIRITE QGEVITAKYS DPAIAGRNLE ALVAATLEAS
     LGNIPGGEVD TALFDELSAS AFSAYRALVE TPGFMQYFLE ATPVTAIARL NIGSRPASRK
     SLSSIGDLRA IPWVFSWSQS RLMLPGWFGV GSAVAAYVQM HGDAGLAKLQ HLYRHSPFFQ
     VVLSNMEQVL AKADLGIARR FSELVDDREL AARLFGAIEA EWRKTHDAFF AITGQAELLE
     SNPTLRRSLE TRLPFLDALG LLQADLLARL RAEPEDEETL YAIHLTINGT SAGLRNTG
//
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