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Database: UniProt
Entry: A0A087VSJ0_9BIFI
LinkDB: A0A087VSJ0_9BIFI
Original site: A0A087VSJ0_9BIFI 
ID   A0A087VSJ0_9BIFI        Unreviewed;       919 AA.
AC   A0A087VSJ0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   ORFNames=BINDI_0030 {ECO:0000313|EMBL:AIC91316.1};
OS   Bifidobacterium indicum LMG 11587 = DSM 20214.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1341694 {ECO:0000313|EMBL:AIC91316.1, ECO:0000313|Proteomes:UP000028569};
RN   [1] {ECO:0000313|EMBL:AIC91316.1, ECO:0000313|Proteomes:UP000028569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11587 {ECO:0000313|EMBL:AIC91316.1,
RC   ECO:0000313|Proteomes:UP000028569};
RX   PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA   Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA   Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA   Barrangou R., Margolles A., van Sinderen D., 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 source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071};
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DR   EMBL; CP006018; AIC91316.1; -; Genomic_DNA.
DR   RefSeq; WP_033491489.1; NZ_JDUE01000006.1.
DR   AlphaFoldDB; A0A087VSJ0; -.
DR   KEGG; bii:BINDI_0030; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000028569; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:AIC91316.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:AIC91316.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028569}.
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        581
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   919 AA;  102802 MW;  F0E797DDEE4FA530 CRC64;
     MTDSNQQITA ADATLVASGT GTKGPEERDL PQSLGEDMAL CLRLLRDVLG EFDKELLNRF
     DSLREDVVAA SADHFNRHPS 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
     KWAESHDIDV 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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