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Database: UniProt/TrEMBL
Entry: A0A0H3EA47_BIFBP
LinkDB: A0A0H3EA47_BIFBP
Original site: A0A0H3EA47_BIFBP 
ID   A0A0H3EA47_BIFBP        Unreviewed;       918 AA.
AC   A0A0H3EA47;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   Name=ppc {ECO:0000313|EMBL:ADP35183.1};
GN   OrderedLocusNames=BBPR_0042 {ECO:0000313|EMBL:ADP35183.1};
OS   Bifidobacterium bifidum (strain PRL2010).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=702459 {ECO:0000313|EMBL:ADP35183.1, ECO:0000313|Proteomes:UP000002312};
RN   [1] {ECO:0000313|EMBL:ADP35183.1, ECO:0000313|Proteomes:UP000002312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRL2010 {ECO:0000313|EMBL:ADP35183.1,
RC   ECO:0000313|Proteomes:UP000002312};
RX   PubMed=20974960; DOI=10.1073/pnas.1011100107;
RA   Turroni F., Bottacini F., Foroni E., Mulder I., Kim J.H., Zomer A.,
RA   Sanchez B., Bidossi A., Ferrarini A., Giubellini V., Delledonne M.,
RA   Henrissat B., Coutinho P., Oggioni M., Fitzgerald G.F., Mills D.,
RA   Margolles A., Kelly D., van Sinderen D., Ventura M.;
RT   "Genome analysis of Bifidobacterium bifidum PRL2010 reveals metabolic
RT   pathways for host-derived glycan foraging.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:19514-19519(2010).
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; CP001840; ADP35183.1; -; Genomic_DNA.
DR   RefSeq; WP_013362858.1; NC_014638.1.
DR   RefSeq; YP_003970220.1; NC_014638.1.
DR   AlphaFoldDB; A0A0H3EA47; -.
DR   KEGG; bbp:BBPR_0042; -.
DR   PATRIC; fig|702459.3.peg.43; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002312; 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:ADP35183.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:ADP35183.1}.
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
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;  102479 MW;  553A77428639173A CRC64;
     MTDTDQQITP ADATIVSTGT GTKGPEEREL PESLSNDMSL CLRILRDVLG EYDPQLLATF
     DTVRNYAVKA SAEHFAGATA DPHPDEDGLA KAVATIDAMN LHDAQLLARA FATYFHLANL
     SEENYRVSVL HQRENQVEDD EAVDPVNELT TAYHQLLTEM GPAKAKALLE KLEFHPVFTA
     HPTEARRKAV EGKIRRIAEL LEENKRLGGS DKKENVRRLY NEIDALFRTS PIALKKPTPV
     EEADTILDIF DNTLFTTIPK VYHRFNDWLL GDKAGLEQPQ CPAFFHPGSW IGSDRDGNPN
     VTAKVSRQVA RKFSDHVISA LEEATRTVGR NLTMESETTP ASAELKSLWS HQKEMSERLT
     DKAALISTKE LHRAVMLVMA DRLRYTIERD ADLMYHSCDD FIADLQVVQR SLAEAGAKRS
     AYGPLQDLIW QAQTFGFHMV EMEFRQHSVV HARALEDIRE HGLHGERGEL QPMTHEVLDT
     FRALGAIQKR NGIKAARRYI ISFTKSAQNV RDVYELNRLA FSHPEDVPVI DVIPLFEQLE
     DLQNCVNVLE EIVKIPEVQA RLKATGNKME VMLGYSDSSK DAGPTTATLA LHSAESRIVA
     WAAKHDIDLT LFHGRGGAVG RGGGPANRAV LAQPKGSVNC RFKLTEQGEV IFARYGNPVL
     AIRHLESVAA ATLLQSAPSV EKTNTEMTEK YAHMTEVLDN ASHERFLDLL NTPDFAPWFS
     IVTPLTEVGL LPIGSRPAKR GLGAKSLDDL RTIPWVFSWA QARINLAAWY GLGSACEKFG
     DLDTLREAYE EWPLFSTFID NIEMSLAKTD ERIAKMYLAL GDDENLSKKV LDEMKLTTKW
     VLKIVNDEWP LQHRHVLGQA IRIRSPYVDA LSVTQVLALR SLRKKVDKEE LSKSQQAGFI
     YLILCTVSGV AAGLQNTG
//
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