ID D2Q6J8_BIFDB Unreviewed; 918 AA.
AC D2Q6J8;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
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 OMA; PWVFGWT; -.
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
//