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Database: UniProt/TrEMBL
Entry: A6SX34_JANMA
LinkDB: A6SX34_JANMA
Original site: A6SX34_JANMA 
ID   A6SX34_JANMA            Unreviewed;       959 AA.
AC   A6SX34;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-SEP-2017, entry version 69.
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   ECO:0000313|EMBL:ABR88524.1};
GN   OrderedLocusNames=mma_1141 {ECO:0000313|EMBL:ABR88524.1};
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88524.1, ECO:0000313|Proteomes:UP000006388};
RN   [1] {ECO:0000313|EMBL:ABR88524.1, ECO:0000313|Proteomes:UP000006388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille {ECO:0000313|EMBL:ABR88524.1,
RC   ECO:0000313|Proteomes:UP000006388};
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M.,
RA   Raoult D., Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the
RT   convergent evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
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; CP000269; ABR88524.1; -; Genomic_DNA.
DR   RefSeq; WP_012078998.1; NC_009659.1.
DR   STRING; 375286.mma_1141; -.
DR   EnsemblBacteria; ABR88524; ABR88524; mma_1141.
DR   KEGG; mms:mma_1141; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000006388; 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:UP000006388};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABR88524.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABR88524.1}.
FT   ACT_SITE    169    169       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    611    611       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   959 AA;  107073 MW;  D3A8A41BE2695D62 CRC64;
     MAKQPTTPPR VSSPSAKKAV NKAANPATNK DAPLKEDIRL LGRILGDVLR DQEGDAVFEV
     VETIRQTAVR FRREADVQAG ADLNKLLKKL TREQTISVVR AFSYFSHLAN IAEDQHHNRR
     RRAHLLAGSA PQEGSVAFAL EKLANAGVNG ATVRKFFKDA LISPVLTAHP TEVQRKSILD
     AEHDIARLLA ARDLPMTARE RAANTELLRS LVTTLWQTRL LRYSKLSVED EINNALSYYR
     ITFLRELPAL YEDIESEIAE QFPQRASSAN ANRDQHSYVQ MGSWIGGDRD GNPNVNGDTM
     QLALARQSTT ILEFYLEEVH ALGAELPVST FLAGVSPEVQ ALADKSPDTS EHRADEQYRR
     ALIGIYARLA ATARAHGATN ILRKEVGPGA PYESAVEFSA DLQLLVDSLK ERHGAVLIKP
     RLAPLLRAAE IFGFHLATLD MRQSSDVHER VLSELFKRAE VETSYADLPE QKKVELLLTE
     LDKPRLLYSP YIDYSDETNS ELNILRAAHH IRQRYGSRAI RNYIISHTET VSDLLEVLLL
     QRETGLLRPD TDVASVGEVE LMVIPLFETI PDLRLAASIM EQVMAIPKVR RLIAKQGHLQ
     EVMLGYSDSN KDGGFLTSNW ELYKAETELV NVFNRAGVKL RLFHGRGGTV GRGGGPSYEA
     ILAQPPGTVN GQIRLTEQGE IIASKFSNPE IGRRNLALLV AATLEASLTP PPADRKAAKK
     LAEFESVMAE LSELAYKGYR NLVYETPGFT DYFFSATPIA EIAELNIGSR PASRKATRRI
     EDLRAIPWGF SWGQCRLLLP GWYGFGSAIE QWLEQGENKA KRVATLRAMF KEWPFFVTLL
     SNMDMVLSKT DLAVASRYSE MVVDRKLRNS IFKRIVAEHE RTSSCLTLIT GKKERLANNP
     LLARSIKNRF AYLDPLNHLQ VELIKRHRAA MRDGKIDDRV RRGIHLSING IAAGLRNTG
//
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