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Database: UniProt/TrEMBL
Entry: C6D470_PAESJ
LinkDB: C6D470_PAESJ
Original site: C6D470_PAESJ 
ID   C6D470_PAESJ            Unreviewed;       936 AA.
AC   C6D470;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-SEP-2017, entry version 66.
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   OrderedLocusNames=Pjdr2_5636 {ECO:0000313|EMBL:ACT04244.1};
OS   Paenibacillus sp. (strain JDR-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=324057 {ECO:0000313|EMBL:ACT04244.1, ECO:0000313|Proteomes:UP000002510};
RN   [1] {ECO:0000313|Proteomes:UP000002510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDR-2 {ECO:0000313|Proteomes:UP000002510};
RX   PubMed=22675593; DOI=10.4056/sigs.2374349;
RA   Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA   Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S.,
RA   Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L.,
RA   Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.;
RT   "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL   Stand. Genomic Sci. 6:1-10(2012).
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; CP001656; ACT04244.1; -; Genomic_DNA.
DR   RefSeq; WP_015847182.1; NC_012914.1.
DR   STRING; 324057.Pjdr2_5636; -.
DR   EnsemblBacteria; ACT04244; ACT04244; Pjdr2_5636.
DR   KEGG; pjd:Pjdr2_5636; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000002510; 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:UP000002510};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ACT04244.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ACT04244.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002510}.
FT   ACT_SITE    157    157       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    591    591       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   936 AA;  106883 MW;  FAD21A5574F8A64E CRC64;
     MSDQVTSTLS AQHRPQANNL LRRDVRFLGN ILGEVLVHQG GRELLDIVEQ IRETSKALRA
     EFVPELFEQF KTTIASLSPE IRHQVIRAFA IYFQLVNIAE QNHRIRRKRD YERSAGESVQ
     RGSIESAISD LKERNIDIEG VQEILSNISL ELVMTAHPTE ATRRAVLDIH KRIAEDVMEL
     DNPTLTYRER EILRDKLLNE VLILWQTDEL RDRKPTVIDE VRNGLYYFDE TLFEVLPNVY
     EELERNLTKY YPGESWHVPS YLRFGSWIGG DRDGNPSVTA KVTWETLTLN RQLAIKKYEE
     KLHELVSILS FSTNLVEVSE ELINSIKKDR EHVELKCIDL WRNAKEPYRI KLGFMLEKLA
     NTRDESLKGS AMRYNSAGEL LEDLYIIDRS LRGHFADYVA DTHIGKLVRQ VELFGFHMLT
     LDIRQHSQEH ENAMAEILAK MNIVSNYGSL SEEEKIELLS NLLEDPRPLT SSHLDYSAST
     RECLDVYHTV YRAQQEFGPE CISTYLISMT QGASDMLEVM VFAKEVGLFR KEADGSVRCT
     LQSVPLFETI DDLHAAPGIM KLLFELPIYR QAVAARGDLH EIMLGYSDSN KDGGAVTANW
     ELRVALNDIT ATAGEHGVKL KFFHGRGGAL GRGGMPLNRS ILAQPPHTVG GGIKITEQGE
     VLSSRYSMQG IAYRSLEQAT WALVTAARLA KYPQAQDDAV LKEWEEISRS ISETALNKYQ
     DLIFRDPDFL TYFKESTPLP EVGELNIGSR PSKRKNSDRF EDLRAIPWVF AWTQSRYLLP
     AWYAAGTALK QYTGDDAQRL ETLKTMYEKF PFFRSLIDNL QMALAKADLT IAKEYADMIA
     DSTIRDRIFT QIENEYTLTS DMILSITGQD EILDNVPVIQ ESIRLRNPYV DPLSYMQVQL
     LTELRELRAK EEDDPELLRE VLLTINGIAA GLRNTG
//
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