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Database: UniProt/TrEMBL
Entry: K4IYW3_BIFAP
LinkDB: K4IYW3_BIFAP
Original site: K4IYW3_BIFAP 
ID   K4IYW3_BIFAP            Unreviewed;       919 AA.
AC   K4IYW3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   OrderedLocusNames=BAST_0060 {ECO:0000313|EMBL:AFU70665.1};
OS   Bifidobacterium asteroides (strain PRL2011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU70665.1, ECO:0000313|Proteomes:UP000007006};
RN   [1] {ECO:0000313|EMBL:AFU70665.1, ECO:0000313|Proteomes:UP000007006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRL2011 {ECO:0000313|EMBL:AFU70665.1,
RC   ECO:0000313|Proteomes:UP000007006};
RX   PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA   Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA   Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA   Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA   Ventura M.;
RT   "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT   colonization of the insect gut.";
RL   PLoS ONE 7:E44229-E44229(2012).
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; CP003325; AFU70665.1; -; Genomic_DNA.
DR   RefSeq; WP_015021105.1; NC_018720.1.
DR   AlphaFoldDB; K4IYW3; -.
DR   STRING; 1147128.BAST_0060; -.
DR   GeneID; 41009354; -.
DR   KEGG; bast:BAST_0060; -.
DR   PATRIC; fig|1147128.3.peg.58; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000007006; 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:AFU70665.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:AFU70665.1}.
FT   REGION          1..31
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        182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        581
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   919 AA;  102955 MW;  BAD65B2781E2784B CRC64;
     MTDSNQQITA ADATLVTSGT GTKGPEERKL PQSLDEDMAL CLRLLRDVLG EFDQQLLKRF
     DSLREDVMTA SAEHFNRHPS DPVPDEDGLS KAVALIDDTS VKDSQLLARA LTTYFHLANL
     CEENYRVKVL HEREGKVDLK VKGTDPINEM TSAYSQLLQE MGPAKASELL EKLEFHPVFT
     AHPTEARRKA VEGKIRRIAN LLAVRRGLGG SELEENERLL HNEIDALFRT SPIAAKKPTP
     VEEANTILDI FDATLFETIP KVYRRFDDWM LGKKAGMVKP VCPAFFHPGS WIGSDRDGNP
     NVTAKVSRKV ARKFSDHMLE ALVKATTTVG RNMTMEVTTT PPSSELRSLW SHQKEMSERL
     TDRATTISHN ELHRAVVLVI ADRLQATIQR DADLMYADCD DFIADLRVVQ DSLAKAGAVR
     QAYGPLQDLI WQAQTFGFHM VEMEFRQHSL VHARALEDIR EHGLHGERGE LQPMTHEVLD
     TFRALGAIQK RNGQKAARRY IISFTKSAQN VKDVYELNRL AFEHAEDVPV IDVIPLFEQL
     EDLQNSVDVL EEIIKIPEVQ ARLKETGNKM EVMLGYSDSS KDAGPVSATL ALHSAQERIA
     KWAESHDIDL TLFHGRGGAV GRGGGPANRA VLAQPVGSVN CRFKLTEQGE VIFARYGNPV
     LAIRHIESVA AATLLQSAPS VEERNTTMTE KYADMADELD QAAHERFLDL LHTPDFAPWF
     SIVTPLNEIG LLPIGSRPAK RGLGAKSLDD LRTIPWVFSW AQARINLAAW YGLGTACEKF
     GDLETLRQAY EEWPLFSTFI DNIEMSLAKT DERIAKMYLS LGDRDDLSQK VLSEMELTRK
     WVLQIVGDEW PLQHRHVLGQ AIRIRSPYVD ALSVTQVRAL RTLRRRNDKE ELSKSQQADF
     IYLILCTVSG VAAGLQNTG
//
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