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Database: UniProt/TrEMBL
Entry: A0A0A8F8J0_9GAMM
LinkDB: A0A0A8F8J0_9GAMM
Original site: A0A0A8F8J0_9GAMM 
ID   A0A0A8F8J0_9GAMM        Unreviewed;       879 AA.
AC   A0A0A8F8J0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-SEP-2017, entry version 21.
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   ORFNames=W909_00880 {ECO:0000313|EMBL:AJC64742.1};
OS   Dickeya zeae EC1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=1427366 {ECO:0000313|EMBL:AJC64742.1, ECO:0000313|Proteomes:UP000031128};
RN   [1] {ECO:0000313|EMBL:AJC64742.1, ECO:0000313|Proteomes:UP000031128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC1 {ECO:0000313|EMBL:AJC64742.1,
RC   ECO:0000313|Proteomes:UP000031128};
RA   Zhou J., Cheng Y., Liu S., Zhong J., Huang L., Lv M., Liao L., Gu Y.,
RA   Chen Y., Jiang Z., Xiong Y., Zhang L.;
RT   "The Complete Genome Sequence of Dickeya zeae EC1 Reveals Substantial
RT   Divergence from Other Dickeya Strains and Species.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; CP006929; AJC64742.1; -; Genomic_DNA.
DR   RefSeq; WP_016943440.1; NZ_CP006929.1.
DR   EnsemblBacteria; AJC64742; AJC64742; W909_00880.
DR   KEGG; dzc:W909_00880; -.
DR   PATRIC; fig|1427366.4.peg.190; -.
DR   KO; K01595; -.
DR   Proteomes; UP000031128; 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:UP000031128};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AJC64742.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AJC64742.1}.
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   879 AA;  99170 MW;  7B6B2EAA44E3D3A7 CRC64;
     MNEQYSAMRS NVSMLGKLLG DTIKDALGAN ILERVETIRK LSKASRAGSE THRQELLTTL
     QNLSNEELLP VARAFSQFLN LTNTAEQYHS ISPHGEAASN PEALATVFRN LKSRDNLSDK
     DIRNAVESLS IELVLTAHPT EITRRTLIHK LIEVNTCLKQ LDHDDLADYE RHQIMRRLRQ
     LIAQYWHTDE IRKIRPTPVD EAKWGFAVVE NSLWEGVPAF LRELDEQMDK ELGYRLPVDS
     VPVRFTSWMG GDRDGNPNVT SEITRRVLLL SRWKAADLFL RDVQVLVSEL SMTTCTPKLQ
     QLAGGDEVQE PYRELMKNLR AQLTTTLDYL DARLKGEQRV PPNDLLVTND QLWEPLYTCY
     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 WLGAGAALQD VIDKGHQSQL ETMCRDWPFF STRIGMLEMV FAKADLWLAE
     YYDQRLVDEK LWPLGKQLRE QLEKDIQAVL TISNDDHLMA DLPWIAESIA LRNVYTDPLN
     VLQAELLHRS RQQDTTDPQV EQALMVTIAG VAAGMRNTG
//
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