ID Q0P9W6_CAMJE Unreviewed; 599 AA.
AC Q0P9W6;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=Pyruvate carboxylase B subunit {ECO:0000313|EMBL:CAL35053.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:CAL35053.1};
GN Name=pycB {ECO:0000313|EMBL:CAL35053.1};
GN OrderedLocusNames=Cj0933c {ECO:0000313|EMBL:CAL35053.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL35053.1, ECO:0000313|Proteomes:UP000000799};
RN [1] {ECO:0000313|EMBL:CAL35053.1, ECO:0000313|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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DR EMBL; AL111168; CAL35053.1; -; Genomic_DNA.
DR PIR; D81367; D81367.
DR RefSeq; WP_002858311.1; NZ_SZUC01000001.1.
DR RefSeq; YP_002344331.1; NC_002163.1.
DR AlphaFoldDB; Q0P9W6; -.
DR IntAct; Q0P9W6; 1.
DR STRING; 192222.Cj0933c; -.
DR PaxDb; 192222-Cj0933c; -.
DR EnsemblBacteria; CAL35053; CAL35053; Cj0933c.
DR GeneID; 905229; -.
DR KEGG; cje:Cj0933c; -.
DR PATRIC; fig|192222.6.peg.917; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_3_7; -.
DR OMA; GYHALEM; -.
DR OrthoDB; 9769961at2; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000313|EMBL:CAL35053.1};
KW Pyruvate {ECO:0000313|EMBL:CAL35053.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000799}.
FT DOMAIN 6..277
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 523..598
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 599 AA; 65834 MW; E5C075E114E40444 CRC64;
MAKKFIDVMD TSFRDGFQSV YGARVLMDDF FPAVEAAKEA GITHFEFGGG ARFQSLYFYL
NEDAFTMMDR FRAIVGKDAN LQTLARGVNT VTLDTGSSEL IDLHAKLFAK HGTTTIRNFD
ALNDINNLKF SGECIAKHGL KHEIAITLMD LPPNCKGAHD VPFYEKILKE ILAAEIPFHS
ICFKDASGTS NPNKIYETIK MARKILPQDM HIRLHTHETA GVSIACYLAA LEAGVDGIDL
AAAPVSGGTS QPDILTMMHA LKGKDYDLGG LEEEKILKYE EVLKDCLKEY FLPPEATMVN
PLIPFSPMPG GALTANTQMM RDNNILDKFP QVIHAMREVV EKGGFGTSVT PVSQFYFQQA
FNNVMFGSWK KIAEGYGKMV LGYFGKTPVA PDANIIELAS KQLNLEPTTE LAINIADKDE
SKSIAYTKTL LEKEGIETSE ENIFVAAACK EKGIAFLKGE AKVNIRKLAS MPKPMSADEN
KFTVAVNGNK YHVEVSYGFD KDVNVKSVKK VEENKNIISS NSTSSVDAEN EVLAGISGNV
FKIYVNEGEE VKSGQAIMVL EAMKMEIEVN APKDGIILEL CIKIGDTVNE GEVLAIYKN
//