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Database: UniProt/TrEMBL
Entry: A0A0D5Y502_9PSED
LinkDB: A0A0D5Y502_9PSED
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ID   A0A0D5Y502_9PSED        Unreviewed;       876 AA.
AC   A0A0D5Y502;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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=PCL1606_49560 {ECO:0000313|EMBL:AKA26403.1};
OS   Pseudomonas chlororaphis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=587753 {ECO:0000313|EMBL:AKA26403.1, ECO:0000313|Proteomes:UP000032748};
RN   [1] {ECO:0000313|EMBL:AKA26403.1, ECO:0000313|Proteomes:UP000032748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCL1606 {ECO:0000313|EMBL:AKA26403.1,
RC   ECO:0000313|Proteomes:UP000032748};
RX   PubMed=25679537; DOI=10.1094/MPMI-10-14-0326-FI;
RA   Calderon C.E., Ramos C., de Vicente A., Cazorla F.M.;
RT   "Comparative Genomic Analysis of Pseudomonas chlororaphis PCL1606
RT   Reveals New Insight into Antifungal Compounds Involved in
RT   Biocontrol.";
RL   Mol. Plant Microbe Interact. 28:249-260(2015).
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; CP011110; AKA26403.1; -; Genomic_DNA.
DR   RefSeq; WP_044461425.1; NZ_CP011110.1.
DR   EnsemblBacteria; AKA26403; AKA26403; PCL1606_49560.
DR   KEGG; pcz:PCL1606_49560; -.
DR   PATRIC; fig|587753.10.peg.4950; -.
DR   KO; K01595; -.
DR   Proteomes; UP000032748; 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:UP000032748};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AKA26403.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AKA26403.1}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    543    543       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   876 AA;  96913 MW;  AD3AB2DD3DBCE549 CRC64;
     MTDIDARLRE DVHLLGELLG NTIREQYGEG FLDKIEQIRK GAKADRRGSL DAELSASLNQ
     LSEDELLPVA RAFNQFLNLA NIAEQYQLIH RREESQAAPF EARVLPELLA RLRAEGHGAE
     ALARQLGRLE IELVLTAHPT EVARRTLIQK YDAIAAQLAA QDHRDLTSAE RGQIQARLQR
     LIAEAWHTEE IRRTRPTPVD EAKWGFAVIE HSLWQAIPNY LRKADQALQA ATGMRLPLEA
     APIRFASWMG GDRDGNPNVT AAVTREVLLL ARWMAADLYL RDVDQLAADL SMQQANAALR
     ALAGDSAEPY RAVLKQLRER LRATRNWAQA SLSGAAPAPA QVLQNNRELL DPLELCYQSL
     HECGMGVIAD GPLLDCLRRA VTFGLFLVRL DVRQDSSRHT AAMTEITDYL GLGRYGDWNE
     EERIAFLMRE LGSRRPLLPG YFKPSADTAE VLATCREIAA APAASLGSYV ISMAGAASDV
     LAVQLLLKES GVLRPMRVVP LFETLADLDN AGPVIEQLLL LPGYRARLQG PQEVMIGYSD
     SAKDAGTTAA AWAQYRAQER LVDICREQQV ELLLFHGRGG TVGRGGGPAH AAILSQPPGS
     VAGRFRTTEQ GEMIRFKFGL PDIAEQNLNL YLAAVLEATL LPPPLPQPAW RDLMDELAAD
     GVQAYRAVVR ENPQFVEYFR QSTPEQELGR LPLGSRPAKR RAGGIESLRA IPWIFGWTQT
     RLMLPAWLGW ETALSKALER GEGELLGQMR EQWPFFRTRI DMLEMVLAKA DADIARSYDE
     RLVEPALLPL GAHLRDLLSQ ACSVVLGLTG QSQLLAHSPD TLEFIRLRNT YLDPLHLLQA
     ELLARSRRQD GTQDSPVEQA LLVSVAGIAA GLRNTG
//
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