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Database: UniProt/TrEMBL
Entry: F0KI55_ACICP
LinkDB: F0KI55_ACICP
Original site: F0KI55_ACICP 
ID   F0KI55_ACICP            Unreviewed;       894 AA.
AC   F0KI55;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-NOV-2017, entry version 43.
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   ECO:0000313|EMBL:ADY83508.1};
GN   OrderedLocusNames=BDGL_002922 {ECO:0000313|EMBL:ADY83508.1};
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY83508.1, ECO:0000313|Proteomes:UP000007477};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHEA-2;
RA   Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT   "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT   Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights
RT   into environmental adaptation.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY83508.1, ECO:0000313|Proteomes:UP000007477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY83508.1,
RC   ECO:0000313|Proteomes:UP000007477};
RX   PubMed=21441526; DOI=10.1128/JB.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(2011).
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; CP002177; ADY83508.1; -; Genomic_DNA.
DR   RefSeq; WP_014208009.1; NC_016603.1.
DR   RefSeq; YP_004997190.1; NC_016603.1.
DR   STRING; 871585.BDGL_002922; -.
DR   EnsemblBacteria; ADY83508; ADY83508; BDGL_002922.
DR   GeneID; 11637569; -.
DR   KEGG; acc:BDGL_002922; -.
DR   PATRIC; fig|871585.3.peg.2921; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000007477; 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:UP000007477};
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:ADY83508.1}.
FT   COILED      806    833       {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;  102030 MW;  338DCF7DE8D507DB CRC64;
     MVQQIDAPLR EDVRLLGNLL GETLKQHAGQ ELFNQIEQIR ALAKGARDGQ AEAEKQLEQL
     FLELPDEELL PLTRAFSHFL NFANIAEQYH VVRSRRQAEF DSDANSPNPL VHLFQKFKDK
     SISTEKLFQQ ICDLKIELVL TAHPTEVSRR TLIQKYDDIN ACLSQLDQQK LTPRERQNAL
     ANLKQQISSA WQTDEIRQHR PTPVDEAKWG FATIEQTLWN AVPKFIRELN ELVQENCQLN
     LPLNIAPVRF ASWMGGDRDG NPNVTHQITQ EVLWLSRWQA ADLYLRDIEN LRWELSIQTC
     SEEMIQAIGS QHAEPYREYL RATRERLKAT RHWLAQRLQG LEADDSNVIK SKDELLQPLL
     LCYRSLIDSN LPEIANGQLL DFIYRVNCFG IELLKLDIRQ ESGRHRQAIS AITEYLGLGN
     FESWTEQARQ NFLIQELQSK RPLLPKYINE PEGSLIGHPD VQEVFATMRT LADQPPESLG
     AYIISMAEYP SDVLAVLLLQ KEAGIQHPLR VVPLFETLKD LDGAATTMNT LFNMHWYKQH
     IQGKHEVMIG YSDSAKDAGF MSANWAQYRA QEELTAIAQT HGVQLTLFHG RGGSISRGGA
     PTQQALFSQP PGSISGAIRV TEQGEMIRFK FGLEGIAMQN LEIYTAATLE ATLLPPPEPK
     AEWRELMNRM TDHSVKVYRQ TVRENPHFVK YLRTVTPELE LQMLPLGSRP AKRKVSGGIE
     SLRAIPWVFA WTQIRLMLPA WLGTGAAINE VIADQQKATL DEMLQQWPYF QTLIDMLEMV
     LSKADANIAL YYESHLTEDE DLKVLGNQLR QRLKDAVETL LKLKDESKLL SNNEVLDQSM
     QVRKPYLLPL HLLQAELMKR RRDYLAERQA EHTPVDHALM VSIAGIAAGL RNTG
//
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