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Database: UniProt/TrEMBL
Entry: D2BD79_STRRD
LinkDB: D2BD79_STRRD
Original site: D2BD79_STRRD 
ID   D2BD79_STRRD            Unreviewed;       879 AA.
AC   D2BD79;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   07-JUN-2017, entry version 57.
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=Sros_1323 {ECO:0000313|EMBL:ACZ84320.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 /
OS   NI 9100).
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ84320.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ84320.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A.,
RA   Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Sims D., Meincke L., Brettin T., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(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; CP001814; ACZ84320.1; -; Genomic_DNA.
DR   RefSeq; WP_012888065.1; NC_013595.1.
DR   STRING; 479432.Sros_1323; -.
DR   EnsemblBacteria; ACZ84320; ACZ84320; Sros_1323.
DR   KEGG; sro:Sros_1323; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000002029; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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:UP000002029};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ACZ84320.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ACZ84320.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029}.
FT   ACT_SITE    149    149       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    540    540       {ECO:0000256|HAMAP-Rule:MF_00595}.
SQ   SEQUENCE   879 AA;  96316 MW;  08480FFA0C40E082 CRC64;
     MSAIAHHQAE RSSAVTEMPD ELRADVRLLG ELLGQVIAEY GGDDLLADVE RLRKAVIAAR
     RGKVSVDEIT AMVAEWPVER AVQIARAFTC YFHLANLAEE HFRIRTLRVR DTGEEPLPES
     LAQAVQELGG ERVTELVEGL RLHPVLTAHP TEARRRAVVT AIQRISGQLA AYNSPERGAA
     ERAETRRRLL EEIDLLWRTS QLRSTKLDPL DEVRTAMAAF DETLFRVVPL VYRSLDAALG
     EGTGTREPLA RPFIRYGSWI GGDRDGNPNV TAKVTRDAVL IQAEHVLIAL ENATHRIART
     LTLTAGYTPA SPRLRAALTA AENDHPELVS EMATRSPQEP HRQWLLFVAA RIVATRQRGL
     DLAYRSPEEL LGDLRTAQES LVAAGAERQA YGELQHLIWQ VETFGFHLAE LEVRQHSQVH
     AAALAELAAG RTSERTDEVL ATIRTIGWIQ ERYGVTACSR YVVSFTRSAD DIAAVYALAG
     HALGDKAPQL DVVPLFESGA DLANAPGVLS GMLEIPGIQQ RLAANGRRLE VMLGYSDSAK
     ELGPAAATLK LYEAQEALAA WAAEHDVRLT LFHGRGGALG RGGGPANRAV LAQAPGSVGG
     RFKVTEQGEV IFARYGHAAI ARRHMEQVTS AVLLASTPSI EARTAEAAGR FRGMAEQVAS
     ASEKAYRSLT EAPGFPEWFS LVSPLEEIGS LRLGSRPARR GLGAPRSLDD LRAIPWVFAW
     AQTRVNLPGW YGLGSGLQAV ISESGLDELR AAYREWPLFA SLLDNVEMSL AKTDRDIAAR
     YLALGGRDDF VEQVLREYDL TRRLVLEITG HSRLLENRRV LSRAVQLRDP YVDALSHLQL
     RALSRLRADD GLSEEERERL STLLLLSVNG VAAGLQNTG
//
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