ID   D4BLI9_BIFBR            Unreviewed;       917 AA.
AC   D4BLI9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   Name=ppc {ECO:0000313|EMBL:EFE90177.1};
GN   ORFNames=BIFBRE_02924 {ECO:0000313|EMBL:EFE90177.1};
OS   Bifidobacterium breve DSM 20213 = JCM 1192.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE90177.1, ECO:0000313|Proteomes:UP000003191};
RN   [1] {ECO:0000313|EMBL:EFE90177.1, ECO:0000313|Proteomes:UP000003191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE90177.1,
RC   ECO:0000313|Proteomes:UP000003191};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) 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:EFE90177.1}.
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DR   EMBL; ACCG02000002; EFE90177.1; -; Genomic_DNA.
DR   RefSeq; WP_003827906.1; NZ_JDUD01000007.1.
DR   AlphaFoldDB; D4BLI9; -.
DR   STRING; 1685.RY69_2000; -.
DR   KEGG; bbrd:BBBR_0034; -.
DR   PATRIC; fig|518634.20.peg.36; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000003191; 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:EFE90177.1}; Lyase {ECO:0000313|EMBL:EFE90177.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:EFE90177.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003191};
KW   Transferase {ECO:0000313|EMBL:EFE90177.1}.
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   917 AA;  102563 MW;  83B8D1E280C576A2 CRC64;
     MATPEEQITP ADAAIVTTGT GRKGPEEHDL PQSLKDDMDL CLKILRDVLG EYNPELLSTF
     DTVRNYSVEA SAEHFAELED PNPAQDGLKE AVNVIDNMTL HDAQLLARAF ATYFHLANLS
     EENYRVSVLH ERENNVSGEQ AVDPINELTV AYHQLINEMG PAKAKELLDQ LEFHPVFTAH
     PTEARRKAVE GKIRRISELL GEYKILGGSD KKECLRRLYN EIDALFRTSP IALKKPTPVE
     EADTILDIFD NTLFHTIPKV YRRFDDWILG DQAGLVEPAC PAFFHPGSWI GSDRDGNPNV
     TAKVSRAVAR KFSDHVIAAL EEATRTVGRN LTMEAETTPP SAELKNLWSH QKEMSERLTD
     KAALISTKEM HRAVMLVMAD RLHYTIERDA DLMYHSCDDF LNDLKVVQRS LAEAGAKRSA
     YGPLQDLIWQ TETFGFHMVE MEFRQHSVVH ARALADIREH GLHGERGDLQ PMTHEVLDTF
     RALGAIQKRN GLKAARRYII SFTKSAQNIK DVYELNRLAF SHPEDVPTID VIPLFEQLED
     LQNSVDVLEE MIKIPEVQAR LKATGNKLEV MLGYSDSSKD AGPTSATLAL HSAQERIAKW
     AESHDIDLTL FHGRGGAVGR GGGPANRAVL AQPVGSVKCR FKLTEQGEVI FARYGNPVLA
     IRHVESVAAA TLLQSAPSVE KRNTDMTKKY ADMAAQLDEA AHNRFLDLLN TDGFAPWFSI
     VTPLTEIGLL PIGSRPAKRG LGAKSLDDLR TIPWIFSWAQ ARINLAAWYG LGTACEKFGD
     LETMRQAYEE WPLFSTFIDN IEMSIAKTDE RIAKMYLALG DREDLNKKVL EEMELTRKWV
     LDIVGDKWPL QHRHVLGQAI RIRSPYVDAL SVTQVLALKS LRKKVDKEEL SQSQQAGFIY
     LILCTVSGVA AGLQNTG
//