ID A7A2Y7_BIFAD Unreviewed; 918 AA.
AC A7A2Y7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN Name=ppc {ECO:0000313|EMBL:EDN83270.1};
GN ORFNames=BIFADO_00174 {ECO:0000313|EMBL:EDN83270.1};
OS Bifidobacterium adolescentis L2-32.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=411481 {ECO:0000313|EMBL:EDN83270.1, ECO:0000313|Proteomes:UP000003773};
RN [1] {ECO:0000313|EMBL:EDN83270.1, ECO:0000313|Proteomes:UP000003773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-32 {ECO:0000313|EMBL:EDN83270.1,
RC ECO:0000313|Proteomes:UP000003773};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN83270.1, ECO:0000313|Proteomes:UP000003773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L2-32 {ECO:0000313|EMBL:EDN83270.1,
RC ECO:0000313|Proteomes:UP000003773};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bifidobacterium adolescentis (L2-32).";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDN83270.1}.
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DR EMBL; AAXD02000018; EDN83270.1; -; Genomic_DNA.
DR RefSeq; WP_003807205.1; NZ_DS264454.1.
DR AlphaFoldDB; A7A2Y7; -.
DR HOGENOM; CLU_006557_2_0_11; -.
DR Proteomes; UP000003773; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:EDN83270.1}; Lyase {ECO:0000313|EMBL:EDN83270.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Pyruvate {ECO:0000313|EMBL:EDN83270.1};
KW Transferase {ECO:0000313|EMBL:EDN83270.1}.
FT REGION 1..29
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; 102910 MW; 3864CE7C92E8EEE7 CRC64;
MTTENEQITP ADAAIVSSGT GTKGPEERDL PASLKEEMDL CLQILREVLG EFDENLLAKF
DEVREHALKA SDERFSGILT DTNPDQDDLQ KVVDIVDKVD VHDAQLLARA FTTYFHLANL
CEENYRVSVL HQREAAVNED QAVDPVNEMT CAYHQLINEM GPARAKELLD QLEFHPVFTA
HPTEARRKAV EGKIRRISQL LEAHKLLGGS DKKENSRRLF NEIDALFRTS PIALKKPTPV
EEADTILDIF DNTLFYTIPQ VYRRFDDWVL GDKAGLVPPV CPAFFHPGSW IGSDRDGNPN
VTAKVSRQVA RKFSDHVLGA LEIETRRVGK NLTMEAETTP PSAELKSLWN HQKEMSERLT
DKAALISTKE LHRAVMLVMA DRLKATIDRD ADLMYHSCED YIADLKTVQR SLAEANAKRS
AYGPLQDLIW QAETFGFHMV EMEFRQHSVV HSRALEDIRE HGLHGERGEL QPMTHEVLDT
FRALGSIQKR NGIKAARRYI ISFTKSAQNI KDVYELNRLA FSHPEDVPTI DVIPLFEQLE
DLQNSVDVLE EMIKIPEVQA RLKATGGKME VMLGYSDSSK DAGPTSATLA LHSAQERIAK
WAESHDIDLT LFHGRGGAVG RGGGPANRAV LAQPVGSVKC RFKLTEQGEV IFARYGNPVL
AIRHVESVAA ATLLQSAPSV EKRNTDMTKK YADMASKLDE AAHNRFLDLL NTDGFAPWFS
TVTPLTEIGL LPIGSRPAKR GLGAKSLDDL RTIPWIFSWA QARINLAAWY GLGTACEQFG
DLNTLRQAYE EWPLFSTFID NIEMSLAKTD ERIAKMYLAL GDREDLNKKV LDEMELTRKW
VLKIVGDEWP LQHRHVLGQA IRIRSPYVDA LSVTQVLALG SLRKRVDKEE LTHGQKENYT
YLILCTVSGV AAGLQNTG
//
