ID   D2Q6J8_BIFDB            Unreviewed;       918 AA.
AC   D2Q6J8;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   OrderedLocusNames=BDP_0023 {ECO:0000313|EMBL:ADB08720.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB08720.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB08720.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA   Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA   Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA   Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
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; CP001750; ADB08720.1; -; Genomic_DNA.
DR   RefSeq; WP_003838081.1; NC_013714.1.
DR   AlphaFoldDB; D2Q6J8; -.
DR   SMR; D2Q6J8; -.
DR   STRING; 401473.BDP_0023; -.
DR   GeneID; 69535624; -.
DR   KEGG; bde:BDP_0023; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000008693; 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:ADB08720.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:ADB08720.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT   REGION          1..31
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        181
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        580
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   918 AA;  102758 MW;  4697F0908EB45C35 CRC64;
     MTTNDQQITP ADAAIVSSGT GTKGPEERDL PASLKEEMDL CLQILREVLG EFDEQLLASF
     DEVRGYALNA SAERFAGILT DTNPDQDDLQ NVVNTVDKLD MHDAQLLARA FATYFHLANL
     CEENYRVSVL HKRETAVDEN QAVDPVNEMT GAYHQLINEL GPAKARDLLD KLEFHPVFTA
     HPTEARRKAV EGKIRRISRL LEAHKLLGGS DKKENSRRLF NEIDALFRTS PIALKKPTPV
     EEADTILDIF DNTLFYTIPQ VYRRFDDWVL GDKAGLVPPM CPAFFHPGSW IGSDRDGNPN
     VTAKVSRQVA RKFSDHVLGA LEIETRTVGK NLTMEAGTTP PSDELKSLWN HQKEMSERLT
     DKAALISTKE MHRAVMLVMA DRLHYTIERD ADLMYHSCDE FLEDLKIVQR SLAAANAKRS
     AYGPVQDLIW QTETFGFHMV EMEFRQHSVV HSRALEDIRE HGLHGERGPL QPMTHEVLDT
     FRALGAIQKR NGIKAARRYI ISFTKSAQNI KDVYELNRLA FSHPEDVPTI DVIPLFEQLE
     DLQNSVDVLE DMIKIPEVQA RLKATGGKLE VMLGYSDSSK DAGPTSATLA LHSAQERIAK
     WAESHDIDLT LFHGRGGAVG RGGGPANRAV LAQPVGSVKC RFKLTEQGEV IFARYGNPAL
     AIRHVESVAA ATLLQSAPSV EKRNTDMTEK YADMANKLDE AAHNRFLDLL NTPDFAPWFS
     TVTPLTEIGL LPIGSRPAKR GLGAKSLDDL RTIPWIFSWA QARINLAAWY GLGTACEQFG
     DLKTLRQAYE EWPLFSTFID NIEMSLAKTD ERIAKMYLAL GDREDLNKKV LDEMELTREW
     VLKIVGDEWP LQHRHVLGQA IRIRSPYVDA LSVTQVLALG SLRKQVDKEE LTHGQQENYT
     YLILCTVSGV AAGLQNTG
//