ID   C6CND5_DICC1            Unreviewed;       879 AA.
AC   C6CND5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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   OrderedLocusNames=Dd1591_3928 {ECO:0000313|EMBL:ACT08728.1};
OS   Dickeya chrysanthemi (strain Ech1591) (Dickeya zeae (strain Ech1591)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=561229 {ECO:0000313|EMBL:ACT08728.1, ECO:0000313|Proteomes:UP000002735};
RN   [1] {ECO:0000313|EMBL:ACT08728.1, ECO:0000313|Proteomes:UP000002735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech1591 {ECO:0000313|EMBL:ACT08728.1,
RC   ECO:0000313|Proteomes:UP000002735};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya zeae Ech1591.";
RL   Submitted (JUN-2009) 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, ECO:0000256|HAMAP-
CC         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; CP001655; ACT08728.1; -; Genomic_DNA.
DR   RefSeq; WP_015848226.1; NC_012912.1.
DR   AlphaFoldDB; C6CND5; -.
DR   STRING; 561229.Dd1591_3928; -.
DR   KEGG; dze:Dd1591_3928; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002735; 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:ACT08728.1}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        546
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   879 AA;  99069 MW;  8F6A07FAFCE67DBE CRC64;
     MNEQYSAMRS NVSMLGKLLG DTIKEALGAN ILERVETIRK LSKASRAGSE THRQELLTTL
     QNLSNEELLP VARAFSQFLN LTNTAEQYHS ISPHGEAASN PEALATVFRN LKNRDNLSDK
     DIRDAVESLS IELVLTAHPT EITRRTLIHK LVEVNTCLKQ LDHDDLADYE RHQIMRRLRQ
     LIAQYWHTDE IRKIRPTPVD EAKWGFAVVE NSLWEGVPAF LRELDEQMDK ELGYRLPVDS
     VPVRFTSWMG GDRDGNPNVT AEITRRVLLL SRWKAADLFL RDVQVLVSEL SMTTCTPELQ
     QLAGGDEIQE PYRELMKALR AQLTSTLDYL DARLKGEQRV PPKDLLVTNE QLWQPLYACY
     QSLHACGMGI IADGQLLDTL RRVRCFGVPL VRIDVRQEST RHTDALAEIT RYLGLGDYES
     WSESDKQAFL IRELNSKRPL LPRQWEPSAD TQEVLETCRV IAETPRDSIA AYVISMARTP
     SDVLAVHLLL KEAGCPYALP VAPLFETLDD LNNADSVMIQ LLNIDWYRGF IQGKQMVMIG
     YSDSAKDAGV MAASWAQYRA QDALIKTCEK YGIALTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK FGLPEVTISS LSLYTSAILE ANLLPPPEPK PEWHHIMDEL
     SRISCDMYRG YVRENPDFVP YFRAATPELE LGKLPLGSRP AKRRPNGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGAALQK VIDDGNQNQL EAMCRDWPFF STRIGMLEMV FAKADLWLAE
     YYDQRLVEEK LWSLGKQLRE QLAKDIKAVL TISNDDHLMA DLPWIAESIA LRNVYTDPLN
     VLQAELLHRS RQQDTLDPQV EQALMVTIAG VAAGMRNTG
//