ID   D2C1B8_DICZ5            Unreviewed;       879 AA.
AC   D2C1B8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=Dd586_0182 {ECO:0000313|EMBL:ACZ75079.1};
OS   Dickeya zeae (strain Ech586) (Dickeya dadantii (strain Ech586)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya; Dickeya parazeae.
OX   NCBI_TaxID=590409 {ECO:0000313|EMBL:ACZ75079.1, ECO:0000313|Proteomes:UP000001446};
RN   [1] {ECO:0000313|EMBL:ACZ75079.1, ECO:0000313|Proteomes:UP000001446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech586 {ECO:0000313|EMBL:ACZ75079.1,
RC   ECO:0000313|Proteomes:UP000001446};
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., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya dadantii Ech586.";
RL   Submitted (DEC-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; CP001836; ACZ75079.1; -; Genomic_DNA.
DR   RefSeq; WP_012882931.1; NC_013592.1.
DR   AlphaFoldDB; D2C1B8; -.
DR   STRING; 590409.Dd586_0182; -.
DR   KEGG; ddc:Dd586_0182; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001446; 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:ACZ75079.1}.
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;  99131 MW;  249D12D84E419A9B CRC64;
     MNEQYSAMRS NVSMLGKLLG DTIKDALGAN ILERVETIRK LSKASRAGSE THRQELLTTL
     QNLSNEELLP VARAFSQFLN LTNTAEQYHS ISPHGEAASN PEALATVFRN LKSRDNLSDK
     DIRNAVESLS IELVLTAHPT EITRRTLIHK LVEVNTCLKQ LDHNDLADYE RHQIMRRLRQ
     LIAQYWHTDE IRKIRPTPVD EAKWGFAVVE NSLWEGVPAF LRELDEQMDK ELGYRLPVDS
     VPVRFTSWMG GDRDGNPNVT SEITRRVLLL SRWKAADLFL RDVQVLVSEL SMTTCTPKLQ
     QLAGGDEVQE PYRELMKNLR AQLTATLDYL DARLKGEQRV PPNDLLVTND QLWEPLYACY
     QSLHACGMGI IADGQLLDTL RRVRCFGVPL VRIDVRQEST RHTDALAEIT RYLGLGDYES
     WSESDKQAFL IRELNSKRPL LPRQWEPSAD TQEVLETCRV IAETPRDSIA AYVISMARTP
     SDVLAVHLLL KEAGCPYSLP VAPLFETLDD LNNADSVMIQ LLNIDWYRGF IQGKQMVMIG
     YSDSAKDAGV MAASWAQYRA QDALIKTCEK YGIALTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK FGLPEVTISS LSLYTSAILE ANLLPPPEPK PEWHHIMDEL
     SRISCDMYRG YVRENPDFVP YFRAATPELE LGKLPLGSRP AKRRPNGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGAALQD VIDKGHQSQL ETMCRDWPFF STRIGMLEMV FAKADLWLAE
     YYDQRLVDEK LWSLGKQLRE QLEKDIQAVL TISNDDHLMA DLPWIAESIA LRNVYTDPLN
     VLQAELLHRS RQQDMTDPQV EQALMVTIAG VAAGMRNTG
//