(data stored in ACNUC1104 zone)

SWISSPROT: Q7WA21_BORPA

ID   Q7WA21_BORPA            Unreviewed;       313 AA.
AC   Q7WA21;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   SubName: Full=Citrate lyase beta chain {ECO:0000313|EMBL:CAE36874.1};
DE            EC=4.1.3.6 {ECO:0000313|EMBL:CAE36874.1};
GN   Name=citE {ECO:0000313|EMBL:CAE36874.1};
GN   OrderedLocusNames=BPP1572 {ECO:0000313|EMBL:CAE36874.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|SAAS:SAAS00571010}.
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DR   EMBL; BX640427; CAE36874.1; -; Genomic_DNA.
DR   RefSeq; WP_010928096.1; NC_002928.3.
DR   EnsemblBacteria; CAE36874; CAE36874; BPP1572.
DR   KEGG; bpa:BPP1572; -.
DR   HOGENOM; HOG000242281; -.
DR   KO; K01644; -.
DR   OMA; RHTIVKF; -.
DR   BioCyc; BPAR257311:G1GSY-1612-MONOMER; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WA21.
DR   SWISS-2DPAGE; Q7WA21.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Lyase {ECO:0000313|EMBL:CAE36874.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2,
KW   ECO:0000256|SAAS:SAAS00460587}.
FT   DOMAIN       18    208       HpcH_HpaI. {ECO:0000259|Pfam:PF03328}.
FT   METAL       141    141       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   METAL       168    168       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   BINDING      79     79       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
FT   BINDING     141    141       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
SQ   SEQUENCE   313 AA;  32996 MW;  DCC06571C102483F CRC64;
     MTPISNPGGQ RRPASLRRSW MFVPGLLEQA QAAGLASGAD ALVADLEEFT APADRPAARR
     RIVALLAQCR AAGVIGAVRI NKLEEDGLDD LRGIMAGAPD AIFLPHAESA AQIAALDRAI
     SACEAEAGLA PGSTEIVPTL ESALGVTRAC EILTASPRVS ACLLAAEDLT ASLGGAERGP
     DGIELHALRA RFLVDCVAAG CLPIDCPFNY RDPAAQQADL LWARRIGLKS KCAVFAEQVP
     AIHAAFTPDA DRVAAARDLA ARFEAQRDGR DAGGARVDPP DYNTARRLLA RHAEFEQWAA
     RAARPRESQG EQS
//

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