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Database: UniProt/TrEMBL
Entry: H8L338_FRAAD
LinkDB: H8L338_FRAAD
Original site: H8L338_FRAAD 
ID   H8L338_FRAAD            Unreviewed;       902 AA.
AC   H8L338;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   20-DEC-2017, entry version 38.
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   OrderedLocusNames=Fraau_0346 {ECO:0000313|EMBL:AFC84836.1};
OS   Frateuria aurantia (strain ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB
OS   13370) (Acetobacter aurantius).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC84836.1, ECO:0000313|Proteomes:UP000005234};
RN   [1] {ECO:0000313|Proteomes:UP000005234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33424 / DSM 6220 / NBRC 3245 / NCIMB 13370
RC   {ECO:0000313|Proteomes:UP000005234};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G.,
RA   Teshima H., Kyrpides N., Mavromatis K., Ivanova N., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Frateuria aurantia DSM 6220.";
RL   Submitted (FEB-2012) 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; CP003350; AFC84836.1; -; Genomic_DNA.
DR   RefSeq; WP_014401842.1; NC_017033.1.
DR   EnsemblBacteria; AFC84836; AFC84836; Fraau_0346.
DR   KEGG; fau:Fraau_0346; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000005234; 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:UP000005234};
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:AFC84836.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005234}.
FT   COILED      286    306       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    149    149       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    569    569       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   902 AA;  100598 MW;  13E4619746039E4C CRC64;
     MDVNRNPEFL AHDGPLREDV HRLGALVGQV LSEQAGESFY EEVEAIRKAS IDRRKQGRPM
     DQLSARLGGW AADDAQALAR AFSMYFQAVN MAEMVHRIRR RRDYQRADER PQPESLLDVF
     ARLKQNGVGF EELMGWIEKT RIEPVFTAHP TEAMRRSLLD KQKVIVNALI HGFDAGRTPQ
     ERRADRSAML TALSAAWQTA ESAATGPSVQ DEHYHVSYYL SHPLYRVVPS LYAQLAEALE
     QVYGQSPELP RLLSFATWVG GDMDGNPNVG AETMEASLSA QRSQVLEAYQ ADLQQLESLL
     SQTSDRVAVS PAIEQRLHDY AALLPDVDRR IRPRHRNMPY RCLLTYIDAR IEATRDDGAG
     AYAGPEPFCD DLALIEASLR GHRGEHAGAR QVRRLRRRAL AFGFHLARLD VRQDSRVHDD
     ALAVLLQRPE WVELPASERA QVLGEYAGGT RALPRDAQDA TVQRMQAVFA QLHAMRARYG
     VEAAGLYIIS MARSAADVLA VLALARRGGL VQDDGQVPLD IAPLFEIVED LRAAADTLRA
     LLADPVYRGH LQARGNRQWV MLGYSDSGKD SGTLAARWAV QRAQVELLEA AREGGIEIAF
     FHGRGGSASR GGGRITQALE SSPRGSVAGM LRVTEQGEVI NRKYGIRALA LRNLEQSLGA
     VLSASLRPRQ PDVRAPQWRE QMGALANWSR EHYRELVDHP DFVGYFRTAT PIDVIEQMTL
     GSRPSRRRSM RGVQDLRAIP WVFAWTQCRS ILTGWYGLGF ALQKGEQVFG LAALQEMARD
     WPFFANMLED IEMVLAKCDL DIAEAFSKLS GELHPVFFGR ISEEFERSRD LILRIKGSDR
     LLQAQPRLAV SIGLRNPYVD PISLLQVDLL RRWRGEGSQP GPLLEALLAC VNGVSQGLQN
     TG
//
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