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Database: UniProt/TrEMBL
Entry: A0A160U5F8_BRASZ
LinkDB: A0A160U5F8_BRASZ
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ID   A0A160U5F8_BRASZ        Unreviewed;       929 AA.
AC   A0A160U5F8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-MAR-2018, 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=BF49_1737 {ECO:0000313|EMBL:CUT10657.1};
OS   Bradyrhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=376 {ECO:0000313|EMBL:CUT10657.1, ECO:0000313|Proteomes:UP000077107};
RN   [1] {ECO:0000313|EMBL:CUT10657.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BF49_genome1 {ECO:0000313|EMBL:CUT10657.1};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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; LN901633; CUT10657.1; -; Genomic_DNA.
DR   RefSeq; WP_063993146.1; NZ_LN901633.1.
DR   EnsemblBacteria; CUT10657; CUT10657; BF49_1737.
DR   GeneID; 32221948; -.
DR   KEGG; brad:BF49_1737; -.
DR   PATRIC; fig|376.36.peg.1774; -.
DR   KO; K01595; -.
DR   Proteomes; UP000077107; Chromosome i.
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:UP000077107};
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:CUT10657.1}.
FT   ACT_SITE    161    161       {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   929 AA;  103786 MW;  2F28F2C551436E7F CRC64;
     MSLQTISSDT ADQRPNRPED VQALEADVRL RDDIRLLGRI LGDTVRDQEG ADVFDLVERI
     RQTSIRFHRD EDRLARRELE QILDSMSTSE TVRIVRAFSY FSHLANIAED QNNIRQMRAN
     KGGGSGVLAE TLAHARAAGI GADALRNFFK SALVSPVLTA HPTEVRRKST MDREMEVASL
     LDRRERVALT AEEAAASDEQ LRREVLTLWQ TNLLRRTKLT VLDEVANGLS FYDYTFLREV
     PRLVNALEDR LEEGGDQAAG ELASFLRMGS WIGGDRDGNP FVTADVMRGT LRLQSSRVMQ
     FYLNELHVLG SELSIAAHLA DVSEELRTLA ERSPDTSPHR SGEPYRLAVS GIYARLTATA
     EMLQVEITRR PVGKGAPYDS VGELKADLDV LHRSLISNNA GVIARGRLRL LRRAVDCFGL
     HLARLDIRQN SAVHERTIAE LMDAANPGMS YLALGEDARI SLLTNELRST RSLVSPFVKY
     SDETMGELNV FHAAAEAHAK FGSDAIPQCI ISMCKGMSDM LEVAVLLKEV GLVHPSGRSA
     INIVPLFETI EDLQASSAIM DRMLSLHDYR RLVDSRGSVQ EVMLGYSDSN KDGGFVTSGW
     ELYKAEIGLV DVFERHGVRL RLFHGRGGSV GRGGGPSYDA IIAQPGGAVN GQIRITEQGE
     IISSKYSNAE VGRNNLEILA AATLEASLLH PRQSAPRREY LTAMDELSNL AFKAYRGLVY
     ETDGFVDYFW ASTVINEIAT LNIGSRPASR KKTRAIEDLR AIPWVFSWAQ CRLMLPGWYG
     FGSAVEQWIA EHPDKGMPFL KELYREWPFF RMLLSNMDMV LAKSSIAIAS RYAELVPDEA
     LREKIFGRIR REWHSCIETL LDIMGQDRLL QGNPLLERSV RHRFPYLDPL NHVQVELLKE
     HRAQNPDEQV LRGIQLTING ISAGLRNTG
//
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