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Database: UniProt/TrEMBL
Entry: D8MKP2_ERWBE
LinkDB: D8MKP2_ERWBE
Original site: D8MKP2_ERWBE 
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-SEP-2017, entry version 50.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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; Proteobacteria; 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
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; FP236843; CAX57698.1; -; Genomic_DNA.
DR   RefSeq; WP_013200205.1; NC_014306.1.
DR   STRING; 634500.EbC_01670; -.
DR   EnsemblBacteria; CAX57698; CAX57698; EbC_01670.
DR   KEGG; ebi:EbC_01670; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
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   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   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 {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008793};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:CAX57698.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CAX57698.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    546    546       {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
//
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