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Database: UniProt/TrEMBL
Entry: D7B6Q0_NOCDD
LinkDB: D7B6Q0_NOCDD
Original site: D7B6Q0_NOCDD 
ID   D7B6Q0_NOCDD            Unreviewed;       908 AA.
AC   D7B6Q0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-SEP-2017, entry version 58.
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=Ndas_3940 {ECO:0000313|EMBL:ADH69337.1};
OS   Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115
OS   / JCM 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU
OS   509) (Actinomadura dassonvillei).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Nocardiopsis.
OX   NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH69337.1, ECO:0000313|Proteomes:UP000002219};
RN   [1] {ECO:0000313|EMBL:ADH69337.1, ECO:0000313|Proteomes:UP000002219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC   NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC   {ECO:0000313|Proteomes:UP000002219};
RX   PubMed=21304737; DOI=10.4056/sigs.1363462;
RA   Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Pagani I.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Djao O.D., Rohde M., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Nocardiopsis dassonvillei type strain
RT   (IMRU 509).";
RL   Stand. Genomic Sci. 3:325-336(2010).
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; CP002040; ADH69337.1; -; Genomic_DNA.
DR   STRING; 446468.Ndas_3940; -.
DR   EnsemblBacteria; ADH69337; ADH69337; Ndas_3940.
DR   KEGG; nda:Ndas_3940; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000002219; Chromosome 1.
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   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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002219};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ADH69337.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ADH69337.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     33       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        34    908       Phosphoenolpyruvate carboxylase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003093123.
FT   ACT_SITE    178    178       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    572    572       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   908 AA;  99525 MW;  EF635CCD0626961F CRC64;
     MVNARAKHRK YAPAHLAAGA ISVGSVTMTA VSAERDSARQ EVPEQLRNDV KLLGEMLGTV
     LAESGGEDLL ADVEKLRRAV IGARDGSVTG EEITAIVAAW PLERAKQVAR AFTVYFHLAN
     LAEEHQRMRA LRERDDAANP PRESLAAAVR AIREGEGGEE RLDELIAGME FHPVVTAHPT
     EARRRAVSTS ILRVSAQLEA WHSSHEGSSA AAEAHRRLLE EIDLLWRTSQ LRYTRLNPLD
     EVRTALAAFD ETIFSVIPQV YRSLDAAIDP EGTGVRPPRA TPFVRYGSWI GGDRDGNPYV
     TSDITREAVL IQSEHVLRGL EASCTKVART LTAYSNLTPA SPALLDALAS AKAGQPELTA
     EIGARSPNEP HRQLLLLAAA RLRATRERDA DLAYPDADAF LADLRTVQES LAEAGAVRQA
     YGELQHLVWQ AQTFGFHLAE LEIRQHSEVH AAALAELREG GELSERTEEV LATIRVIAWI
     QERFGVEACR RYVVSFTRSA EDIAAVYELA AHALPAGRVP VLDVVPLFET GADLDASPHV
     LDGMLKLPQV NKRLDETGRR IEVMLGYSDS AKDVGPVSAT LRLYDAQARL AAWAEEHDVR
     LTLFHGRGGS LGRGGGPASR ALLAQAPGSV GGRFKVTEQG EVIFARYGQP AIARRHIEQV
     GHAVLMASTD AVQERERSAE RRYRAHADTI ARAAQEAYLE LINTEDFAVW FSRVSPLEEL
     GELRLGSRPS RRGAARGLGD LRAIPWVFAW TQTRVNLPGW FGLGTGLAAV EDLGVLQAAY
     REWPMFSSLL DNAEMSLAKT DRDIAQRYLA LGGRPELTER VLAEYDRTRD LVLKVTGHSR
     LLENRAVLSR AVDLRNPYVD ALSHLQLRAL EALRGEEADS LSEEDQQHLE RLLLLSVNGV
     AAGLQNTG
//
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