ID   B3DNY4_BIFLD            Unreviewed;       917 AA.
AC   B3DNY4;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   Name=ppc {ECO:0000313|EMBL:ACD98843.1};
GN   OrderedLocusNames=BLD_1398 {ECO:0000313|EMBL:ACD98843.1};
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD98843.1, ECO:0000313|Proteomes:UP000002419};
RN   [1] {ECO:0000313|EMBL:ACD98843.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD98843.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA   Lee J.H., O'Sullivan D.J.;
RT   "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT   DJO10A and construction of a shuttle cloning vector.";
RL   Appl. Environ. Microbiol. 72:527-535(2006).
RN   [2] {ECO:0000313|EMBL:ACD98843.1, ECO:0000313|Proteomes:UP000002419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A {ECO:0000313|EMBL:ACD98843.1,
RC   ECO:0000313|Proteomes:UP000002419};
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
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; CP000605; ACD98843.1; -; Genomic_DNA.
DR   RefSeq; WP_007051728.1; NZ_AABM02000019.1.
DR   AlphaFoldDB; B3DNY4; -.
DR   KEGG; blj:BLD_1398; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000002419; 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   Magnesium {ECO:0000256|ARBA:ARBA00022842}.
FT   REGION          1..30
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;  102604 MW;  FE266BC9E7CC069C CRC64;
     MATPEEQITP ADAAIVTTGT GRKGPEEHDL PESLKYDMDL CLEILRNVLG EYNPELLSTF
     DTVRHYAVEA SAEHFAELKD PNPDQDGLKE AVNVIDNMTL HDAQLLARAF ATYFHLANLS
     EENYRVSVLH ERENNVPVDQ AVDPINELTV AYHQLINETG PAKAKELLNQ LEFHPVFTAH
     PTEARRKAVE GKIRRVSELL EEYKRLGGSD KKECLRRLYN EIDALFRTSP IALKKPTPVE
     EADTILDIFD NTLFNTIPKV YRRFDDWVLG DKAGLVEPAC PAFFHPGSWI GSDRDGNPNV
     TAKVSRAVAR KFSDHVIAAL EEATRTVGRN LTMEAETTPP SAELKSLWSH QKEMSERLTD
     KAALISTKEM HRAVMLVMAD RLHYTIERDA DLMYHSCDDF LADLKVVQRS LAAAGAKRSA
     YGPLQDLIWQ TETFGFHMVE MEFRQHSVVH ARALADIREH GLHGERGELQ PMTHEVLDTF
     RALGAIQKRN GLKAARRYII SFTKSAQNIK DVYELNRLAF SHPEDVPTID VIPLFEQLED
     LQNSVDVLEE MIKIPEVQAR LKATGNKLEV MLGYSDSSKD AGPTSATLAL HSAQERIAKW
     AESHDIDLTL FHGRGGAVGR GGGPANRAVL AQPVGSVKCR FKLTEQGEVI FARYGNPVLA
     IRHVESVAAA TLLQSAPSVE KRNTEMTEKY ADMAAQLDEA AHNRFLDLLN TDGFAPWFSI
     VTPLTEIGLL PIGSRPAKRG LGAKSLDDLR TIPWIFSWAQ ARINLAAWYG LGTACEKFGD
     LETMRQAYEE WPLFSTFIDN IEMSIAKTDE RIARMYLALG DREDLNEKVL NEMELTRKWV
     LAIVGDKWPL QHRHVLGQAI RIRSPYVDAL SVTQVLALKS LRKKVDKEEL SQSQQAGFIY
     LILCTVSGVA AGLQNTG
//