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Database: UniProt/TrEMBL
Entry: A0A076LNF7_9GAMM
LinkDB: A0A076LNF7_9GAMM
Original site: A0A076LNF7_9GAMM 
ID   A0A076LNF7_9GAMM        Unreviewed;       877 AA.
AC   A0A076LNF7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   07-JUN-2017, entry version 20.
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:AIJ08153.1};
GN   ORFNames=ETEE_1704 {ECO:0000313|EMBL:AIJ08153.1};
OS   Edwardsiella anguillarum ET080813.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=667120 {ECO:0000313|EMBL:AIJ08153.1, ECO:0000313|Proteomes:UP000028681};
RN   [1] {ECO:0000313|EMBL:AIJ08153.1, ECO:0000313|Proteomes:UP000028681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=080813 {ECO:0000313|EMBL:AIJ08153.1,
RC   ECO:0000313|Proteomes:UP000028681};
RX   PubMed=22590641; DOI=10.1371/journal.pone.0036987;
RA   Yang M., Lv Y., Xiao J., Wu H., Zheng H., Liu Q., Zhang Y., Wang Q.;
RT   "Edwardsiella comparative phylogenomics reveal the new intra/inter-
RT   species taxonomic relationships, virulence evolution and niche
RT   adaptation mechanisms.";
RL   PLoS ONE 7:E36987-E36987(2012).
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; CP006664; AIJ08153.1; -; Genomic_DNA.
DR   RefSeq; WP_034165431.1; NZ_CP006664.1.
DR   EnsemblBacteria; AIJ08153; AIJ08153; ETEE_1704.
DR   KEGG; ete:ETEE_1704; -.
DR   KO; K01595; -.
DR   Proteomes; UP000028681; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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:UP000028681};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AIJ08153.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AIJ08153.1}.
FT   ACT_SITE    137    137       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    544    544       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   877 AA;  98423 MW;  F30877A8AB76C854 CRC64;
     MNEQYSAMRG NVSMLGKLLG DTIKDALGED ILDRVETIRR LSKSSRAGNE ASRQALLNTL
     QNLSNDELLP VARAFSQFLN LANVAEQYHR ISPHGEAASN PDALSHLFTR LKNKNLDEAQ
     IRQAVDNLSI ELVLTAHPTE IARRTLIHKL VEVNTCLSQL DHDDLADYER HQIMRRLRQL
     VAQSWHTDEI RKNRPTPIDE AKWGYAVVEN SLWEGVPAFL REFNEQLEKS LGYQLPVEAV
     PVRFTAWMGG DRDGNPNVTA EVTRRALLLS RWKAAELFLR DVQVLVSELS MTVCTPELRA
     LAGEHAQEPY REVLKRLRQQ LNNTLTYLDA RLRGERLARP ADLLVSNDQL WQPLHTCYRS
     LKACGMGIIA NGQLLDTLRR VHCFGVPLVR IDIRQESTRH TEALAELTRY LGLGDYETWS
     EEDKQTFLLR ELNSKRPLVP RHWTPSPETK EVFDTCQVIA EAPAGAIAAY VISMARTPSD
     VLAVHLLLKE AGCPYNLPVA PLFETLDDLN NAEAVMTQLL SIDWYRGFIQ GKQMVMIGYS
     DSAKDAGVMA ASWAQYRAQE ALVRVCDGAG IALTLFHGRG GSIGRGGAPA HDALLSQPPG
     SLKGGLRVTE QGEMIRFKLG LPEIAVSSLT LYTSAILEAN LLPPPAPKQE WRDVMDELSQ
     TSCALYRRYV RENPDFVPYF RSATPELELG KLPLGSRPAK RRPSGGVESL RAIPWIFAWT
     QNRLMLPAWL GAGAALEEAM AEGRRDALES MYRSWPFFTT RIDMLEMVFA KSDLWLAEYY
     DQRLVDPALW PLGTELRQQV QRDIQAVLAI ANTDHLMADL PWAAESIALR NVYTDPLNVL
     QAELLYRSRH QEQPDANVEQ ALMVTIAGVA AGMRNTG
//
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