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Database: UniProt/TrEMBL
Entry: A0A1P8EKY7_9GAMM
LinkDB: A0A1P8EKY7_9GAMM
Original site: A0A1P8EKY7_9GAMM 
ID   A0A1P8EKY7_9GAMM        Unreviewed;       894 AA.
AC   A0A1P8EKY7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   20-DEC-2017, entry version 6.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=BEN76_12985 {ECO:0000313|EMBL:APV36881.1};
OS   Acinetobacter soli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=487316 {ECO:0000313|EMBL:APV36881.1, ECO:0000313|Proteomes:UP000185674};
RN   [1] {ECO:0000313|EMBL:APV36881.1, ECO:0000313|Proteomes:UP000185674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GFJ2 {ECO:0000313|EMBL:APV36881.1,
RC   ECO:0000313|Proteomes:UP000185674};
RA   Tabata M., Kuboki S., Gibu N., Kinouchi Y., Vangnai A., Kasai D.,
RA   Fukuda M.;
RT   "Complete genome sequence of Acinetobacter baylyi strain GFJ2.";
RL   Submitted (AUG-2016) 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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; CP016896; APV36881.1; -; Genomic_DNA.
DR   RefSeq; WP_076033259.1; NZ_CP016896.1.
DR   GeneID; 31756149; -.
DR   KEGG; asol:BEN76_12985; -.
DR   KO; K01595; -.
DR   Proteomes; UP000185674; 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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000185674};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:APV36881.1}.
FT   COILED      149    169       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    143    143       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    556    556       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   894 AA;  101985 MW;  C1E7211A0CD2219F CRC64;
     MIQQIDAPLR EDVRLLGNLL GETLKQHAGQ DLFNQIEQIR ALAKGARDGQ AKVEKQLEKL
     FLNLKDEEIL PLTRAFSYFL NFANIAEQYH VVRSRRQSEF DAHAPSPNPL TRLFEKFQHN
     HITPQQLFDQ VCELNIELVL TAHPTEVSRR TLIQKYDDIN DALSKLDQQK LTPQEREQVL
     TNLKHLICSA WQTDEIRQNK PTPLDEAKWG FTTIEQTLWN AVPKFVRELN TLVHQHCNAT
     LPLDISPIRF ASWMGGDRDG NPNVTHTVTQ EVLWLSRWQA ADLYLRDIES LRWELSIQAC
     SEELSLALGR SHPEPYREYL RTTRERLKAT RHWLSLRLQG LDGDDSQIIR HKQELLEPLL
     LCHRSLIACN LPELANGKLL DFIYRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
     FESWTEQARQ NFLIQELQSK RPLLPKYLKE PEGSLIEHPD VKEVFATMRT LAEQPPESLG
     AYIISMAEYP SDVLAVLLLQ KEAGILHPLR VVPLFETLKD LDGAAKTMET LFNMDWYKQH
     IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAVAKA HNVQLTLFHG RGGSISRGGA
     PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGVALQN LEVYTAATLE ATLLPPPVPK
     AEWRELMHQM TDISVRVYRE TVRENPHFVQ YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
     SLRAIPWVFA WTQIRLMLPA WLGTGAAINQ VIDENKKPLL DEMLAEWPYF QTLIDMLEMV
     LSKADANVAL YYESHLTHDD ELKVLGEMLR ARLNDAVQTL LTMKGESKLL SKNDVLDQAM
     QVRKPYLLPL HLLQAELMKR RREYTAKTNA DHTPVDHALM VSIAGIAAGL RNTG
//
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