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Database: UniProt/TrEMBL
Entry: D2PKN1_KRIFD
LinkDB: D2PKN1_KRIFD
Original site: D2PKN1_KRIFD 
ID   D2PKN1_KRIFD            Unreviewed;       879 AA.
AC   D2PKN1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   20-DEC-2017, entry version 60.
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=Kfla_1442 {ECO:0000313|EMBL:ADB30543.1};
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Kribbella.
OX   NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB30543.1, ECO:0000313|Proteomes:UP000007967};
RN   [1] {ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) 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; CP001736; ADB30543.1; -; Genomic_DNA.
DR   RefSeq; WP_012919099.1; NC_013729.1.
DR   STRING; 479435.Kfla_1442; -.
DR   EnsemblBacteria; ADB30543; ADB30543; Kfla_1442.
DR   KEGG; kfl:Kfla_1442; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000007967; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 2.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 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:UP000007967};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ADB30543.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ADB30543.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007967}.
FT   COILED      279    299       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    151    151       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    544    544       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   879 AA;  96507 MW;  22053730EE5A103F CRC64;
     MTETGSQASA RTRTRARFEV PEELRADVRL LGEILGRVLV EYAGQPLLDD VEKLRELTIA
     GDGEAAEQLV ASWPHERAED VARAFTCYFH LTNLSEELHR ARVLRERDRS GDAPAVSELA
     QAVERISADA GEQQARALLN GLEFRPVLTA HPTEARRRAV LATIRRISSL LEERNDPRAG
     DSELAENRRR LVEQVDILWR TSQLRTSRPT PLDEVRSAMA VFEETLFDVV GNVYRRLDDA
     LAGDAAGTRP PVVAPFVRLG SWIGGDRDGN PNVTAAITRE AMQIQADHVL RALEQATDEL
     GRALTLDAAT TPPSAPVRRI LEDARAANPA LIADIETRSP SEPHRQLLLL AARRLAATRS
     RDADFGYPRA ADFLHELKVL QDSLVSAGAP RQAYGQLQQL IWQVSSFGFH LAELEVRQHS
     SVHAKALEEV LGGGELSDQT EEVLATLRVI GQIQQRFGPE ACRRYVVSFT RSAADLAAVY
     ELADAAMDGR PIELDVVPLF ETGEDLQNSV EVLDNAIQLT RVRHRLTAND RRFEVMLGYS
     DSAKDVGPVS ATLALYDAQA RITAWAQRNA IRLTLFHGRG GALGRGGGPA NRAVLAQAPG
     SVGGRFKLTE QGEAIPARYG NAPIAQRHIE QVTAATLLAS TPAVEDRAAA AANRFAVVEK
     TLDEAARTAY HRLVKADGFA EWFGRVTPLE ELGQLPLGSR PARRGVAVSS LEDLRAIPWV
     FAWSQARVNA PGWYGLGSAL AAVGDVAVLQ DANKNWPLFQ VMLENAEMSL AKTDRRILGR
     YLELGDRPDL SQLMLDEHAL TTEWVLKVLD GDRLLAGRRV LGRAVELRNP YVDALSYLQL
     RALRDLRTDD SLDEQQIVRT RRLLLLTVSG VAAGLQNTG
//
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