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Database: UniProt/TrEMBL
Entry: F6ACT6_PSEF1
LinkDB: F6ACT6_PSEF1
Original site: F6ACT6_PSEF1 
ID   F6ACT6_PSEF1            Unreviewed;       878 AA.
AC   F6ACT6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   20-JUN-2018, entry version 46.
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=Psefu_1165 {ECO:0000313|EMBL:AEF21142.1};
OS   Pseudomonas fulva (strain 12-X).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF21142.1, ECO:0000313|Proteomes:UP000000686};
RN   [1] {ECO:0000313|EMBL:AEF21142.1, ECO:0000313|Proteomes:UP000000686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA   Woyke T.;
RT   "Complete sequence of Pseudomonas fulva 12-X.";
RL   Submitted (APR-2011) 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; CP002727; AEF21142.1; -; Genomic_DNA.
DR   RefSeq; WP_013790273.1; NC_015556.1.
DR   STRING; 743720.Psefu_1165; -.
DR   EnsemblBacteria; AEF21142; AEF21142; Psefu_1165.
DR   GeneID; 31808966; -.
DR   KEGG; pfv:Psefu_1165; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; PFUL743720:PSEFU_RS05870-MONOMER; -.
DR   Proteomes; UP000000686; 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:UP000000686};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AEF21142.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AEF21142.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000686}.
FT   COILED      762    782       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    140    140       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    545    545       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   878 AA;  97769 MW;  7FE80C971FDE3633 CRC64;
     MTQIDARLRE DVHQLGELLG TTIRDQHGEA FLDKIERIRK GAKAARQGSA DGARQLSETL
     DGLHDDELLP VARAFNQFLN LANIAEQYHR VRRRATGEAQ PFENRVFDEL LQRLRANGHE
     PAALARQVAE LDIELVLTAH PTEVSRRTLI QKYDAISAQL AEQDHSDLSG AEREAIASRL
     QRLIAEAWHT EEIRRVRPTP VDEAKWGFAV IENSLWYALP TVMRKADQAL QRETGQRLPL
     DAAPIRFASW MGGDRDGNPN VTAKITREVL LLARWMAADL YLRDIDSLAA ELSMQRANDE
     LRARAGDSAE PYRAVLKQLR ERLRATRTWA HESLAGPVNP PAQVLHDNAE LREPLLLCYR
     SLHDCGMGVI ADGPLLDFLR RVSTFGLFLV RLDVRQDATR HASAMAEITE YLGLGRYDSW
     GEEQRLAFLQ DELSGRRPLL PADFNPSDDT AEVLATCREV AAAPAASLGS YVISMAGAAS
     DVLAVQLLLK EAGLRRPMRV VPLFETLADL DNAAVAIERL LGLPDYRAGL QGPQEVMIGY
     SDSAKDAGTT AAAWAQYRAQ ESLVRICREH DVELLLFHGR GGTVGRGGGP AHEAILSQPP
     GSVNGRFRTT EQGEMIRFKF GMPDIAEQNL NLYLAAVLEA TLLPPPVPQE AWRAQMDKLA
     ADGVATYRGV VREHPQFVEY FRQATPEQEL GRLPLGSRPA KRREGGVESL RAIPWIFAWT
     QTRLMLPAWL GWEAALRNAL ERGEGEVLRE MREQWPFFRT RIDMLEMVLA KADESIARLY
     DERLVTAELQ PLGAHLRDLL SQASEVVLGL TGQSQLLVHS PETLEFITVR NTYLDPLHLL
     QAELLARSRQ REQEPGSALE QALLVSVAGI AAGLRNTG
//
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