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Database: UniProt/TrEMBL
Entry: A0A0K1JLF2_9MICO
LinkDB: A0A0K1JLF2_9MICO
Original site: A0A0K1JLF2_9MICO 
ID   A0A0K1JLF2_9MICO        Unreviewed;       922 AA.
AC   A0A0K1JLF2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 15.
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   ORFNames=VV02_19740 {ECO:0000313|EMBL:AKU17554.1};
OS   Luteipulveratus mongoliensis.
OC   Bacteria; Actinobacteria; Micrococcales; Dermacoccaceae;
OC   Luteipulveratus.
OX   NCBI_TaxID=571913 {ECO:0000313|EMBL:AKU17554.1, ECO:0000313|Proteomes:UP000066480};
RN   [1] {ECO:0000313|EMBL:AKU17554.1, ECO:0000313|Proteomes:UP000066480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN07-A0370 {ECO:0000313|EMBL:AKU17554.1,
RC   ECO:0000313|Proteomes:UP000066480};
RA   Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K.,
RA   Sanglier J.-J., Yeo T.;
RT   "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT   (Dermacoccaceae) from Sarawak, Malaysia.";
RL   Submitted (MAR-2015) 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; CP011112; AKU17554.1; -; Genomic_DNA.
DR   RefSeq; WP_052594292.1; NZ_CP011112.1.
DR   EnsemblBacteria; AKU17554; AKU17554; VV02_19740.
DR   KEGG; lmoi:VV02_19740; -.
DR   PATRIC; fig|571913.6.peg.3995; -.
DR   KO; K01595; -.
DR   Proteomes; UP000066480; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000066480};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AKU17554.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066480}.
FT   ACT_SITE    153    153       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    584    584       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   922 AA;  102360 MW;  DDC4235DDAD3DE0E CRC64;
     MSPHLDFDVS AEARAATEPL RDDIRLLGGL LGDVVREQEG ERVFAMVEQA RRRAFAVRRD
     EVDREGFAHL FHDLPTGDAL QVIRAFSLFA LLANLAEDLH RERRRALHIQ AGDPPLDGSL
     AASFAKLASA GLEPTEVRAA LTDATVVPVI TAHPTETRRR TVFDAQTRIK ETMRLRERMT
     LTDAEESDAL RDIKIQVITL WQTALIRLQR VKIQDEIEVG LRFFEASLFE VMPQINAQVR
     RELAELYPGT DLLSEPLLRA GSWIGGDRDG NPNVDADVVA TASSRAAQTA LTHYADELAE
     LETSLSLSVR MTRVSDALRD LAARNSEDLR DDEPYRQAVR WVRVRLTSTY NRFFDDRLAH
     AVDAPDAEAY ETPAELLADL DVIDTSLRGD GDDLIADDRL LRLREAVRTF GFHLYGLDLR
     QNSDVHEETI AELFAWAGVH DAYADLDEDA KVALLVGELG SRRPLVGRGA SFSEQTQREL
     AITAAAARAV QTYGPESVPN YVISMCTSVS DMLECAVLLK EAGLLDPVSG TCPVNIVPLF
     ETIEDLQVSA TTLRAALGVP AYRALVDSKG SLQEVMLGYS DSNKDGGYLA ANWALYRAEL
     DLVDVAREGD IRLRLFHGRG GTVGRGGGPS YEAILAQPRG AVRGSLRLTE QGEIIAAKYA
     EPRLAVRNLE ALVSATLEAS LLDTERLGEE TKAAYEHLDE LAGLAREAYA DLVHRTPGFV
     EYFKSSTPVA EIGALNIGSR PASRKPTEQI SDLRAIPWVM SWSLSRVMLP GWYGTGSALE
     QWVGGDDERL ALLRGYYERW PFFQTVMSNL AQVIAKSDLG IAERYSRLVE DEALRERVFG
     KLVDEHERTV RMFGRITGHE DLLWDNAGLK RSVFNRFPYL EPLNHLQLEL LHRYRAGDES
     EQLRRGILLT MNGLATALRN SG
//
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