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Database: UniProt/TrEMBL
Entry: A0A076JHZ3_9BIFI
LinkDB: A0A076JHZ3_9BIFI
Original site: A0A076JHZ3_9BIFI 
ID   A0A076JHZ3_9BIFI        Unreviewed;       919 AA.
AC   A0A076JHZ3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   07-JUN-2017, entry version 18.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   ORFNames=BCOR_0083 {ECO:0000313|EMBL:AII74106.1};
OS   Bifidobacterium coryneforme.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1687 {ECO:0000313|EMBL:AII74106.1, ECO:0000313|Proteomes:UP000028587};
RN   [1] {ECO:0000313|EMBL:AII74106.1, ECO:0000313|Proteomes:UP000028587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG18911 {ECO:0000313|EMBL:AII74106.1};
RX   PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA   Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F.,
RA   Mangifesta M., Sanchez B., Viappiani A., Mancabelli L., Taminiau B.,
RA   Delcenserie V., Barrangou R., Margolles A., van Sinderen D.,
RA   Ventura M.;
RT   "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL   Appl. Environ. Microbiol. 80:6290-6302(2014).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00635164};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP007287; AII74106.1; -; Genomic_DNA.
DR   RefSeq; WP_033498609.1; NZ_CP007287.1.
DR   EnsemblBacteria; AII74106; AII74106; BCOR_0083.
DR   KEGG; bcor:BCOR_0083; -.
DR   KO; K01595; -.
DR   Proteomes; UP000028587; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR021135; PEP_COase.
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; 2.
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|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028587};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169, ECO:0000313|EMBL:AII74106.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AII74106.1}.
FT   ACT_SITE    182    182       {ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    581    581       {ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   919 AA;  102815 MW;  73D6E0B6589C55DE CRC64;
     MTDSNQQITA ADATLVASGT GTKGPEERDL PQSLGEDMAL CLRLLRDVLG EFDKELLNRF
     DSLREDVVAA SAEHFNRHPS DPLPDEDGLA KAVALIDDTS IQDSQLLARA LTTYFHLANL
     CEENYRVRVL HEREGKIDLG VKGTDPINEM TSAYSQLLQE MGPAKASELL EKLEFHPVFT
     AHPTEARRKA VEGKIRRIAN LLAVRRGLGG SERVENERLL HNEIDALFRT SPIATKKPTP
     VEESNTILDI FDATLFQTIP RVYRRFDDWM LGKKAGTVKP VCPAFFHPGS WIGSDRDGNP
     NVTAKVSRKV ARKFSDHVLK ALQEATSTVG RNMTMEATTT PPSSELRSLW SHQKEMSERL
     TDRAEVVSHR ELHRAVVLVI ADRLTATIKR DADLMYRSCD DFIADLKIVQ DSLAAAGAVR
     QAYGPLQDLI WQAQTFGFHM VEMEFRQHSL VHARALEDIR EHGLHGERGE LQPMTHEVLD
     TFRALGAIQK RNGQKAARRY IISFTKSAQN VKDVYELNRL AFEHAEDVPV IDVIPLFEQL
     EDLQNSVDVL EEIIKIPEVQ ARLKKTGNKM EVMLGYSDSS KDAGPVSATL ALHSAQERIA
     KWAQSHDIDV TLFHGRGGAV GRGGGPANRA VLAQPVGSVN CRFKLTEQGE VIFARYGNPV
     LAIRHIESVA AATLLQSAPS VEERNTTMTE KYSDMAAKLD DSAHRRFLDL LHTPDFAPWF
     SIVTPLNEIG LLPIGSRPAK RGLGAKSLDD LRTIPWVFSW AQARINLAAW YGLGTACEEF
     NDLDTLRQAY EEWPLFSTFI DNIEMSLAKT DERIAKMYLS LGDRDDLSQK VLSEMELTRK
     WVLQIVGDEW PLQHRHVLGQ AIRIRSPYVD ALSVTQVRAL RTLRRRNDKE ELSKSQQADF
     IYLILCTVSG VAAGLQNTG
//
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