ID   D8MKP2_ERWBE            Unreviewed;       883 AA.
AC   D8MKP2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
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   ECO:0000313|EMBL:CAX57698.1};
GN   OrderedLocusNames=EbC_01670 {ECO:0000313|EMBL:CAX57698.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX57698.1, ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX57698.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX57698.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FP236843; CAX57698.1; -; Genomic_DNA.
DR   RefSeq; WP_013200205.1; NC_014306.1.
DR   AlphaFoldDB; D8MKP2; -.
DR   STRING; 634500.EbC_01670; -.
DR   KEGG; ebi:EbC_01670; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000008793; 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:CAX57698.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008793}.
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   883 AA;  99006 MW;  9A2C84C7BAC909CD CRC64;
     MNEQYSAMRS NVSMLGKLLG DTIKDALGEN ILERVETIRK LSKSSRAGND AHRKELLSTL
     QNLSNDELLP VARAFSQFLN LTNVAEQYHT ISPKGEGANH PEMLTKVFDR LKQQPHLTEA
     SIREAIESLS LELVLTAHPT EITRRTLIHK LVEVNSCLKQ LDHNDLSDYD RSQIMRRLRQ
     LVAQAWHTDE IRKYRPSPVD EAKWGFAVVE NSLWEGVPNF LRELNEQVEA SFGVKLPVDF
     VPIKFTSWMG GDRDGNPNVT ADITRHVLQL SRWKATDLFL RDIAVLVSEL SMSECTPEVR
     ELCGNPEALE PYREIMKNLR GQLMSTQAYL ERRLKGERLP RPADLLISND QLWDPLYTCY
     QSLQACGMGI IANGQLLDTL RRVKCFGVPL VRIDIRQEST RHTEAIAEIT RFLGLGDYES
     WSEADKQAFL IRELNSKRPL LPRNWEPSAD TREVLETCRV AAEVPKGSIA AYVISMAKVP
     SDVLAVHLLL KEAGIPFTMP VAPLFETLDD LNNANDVMSQ LLNIDWYRGI IQGKQMVMIG
     YSDSAKDAGV MAASWAQYEA QDALIKTCEK AGIALTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEVTISS LSLYTGAILE ANLLPPPEPK KAWCRIMDQL
     SADSCEMYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRASSGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGAALQK AMEAGNQDEL ETMCRDWPFF STRVGMLEMV FSKADLWLAE
     YYDQRLVEPS LWPLGKQLRD QLDSDIKAIL TIANDAHLMA DQPWIAESIA LRNVYTDPLN
     VLQAELLHRS RQQEAKGEPV DPHVEQALMV TIAGVAAGMR NTG
//