(data stored in ACNUC1104 zone)

SWISSPROT: Q7WA24_BORPA

ID   Q7WA24_BORPA            Unreviewed;       498 AA.
AC   Q7WA24;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   SubName: Full=Probable aldehyde dehydrogenase {ECO:0000313|EMBL:CAE36871.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:CAE36871.1};
GN   Name=aldH {ECO:0000313|EMBL:CAE36871.1};
GN   OrderedLocusNames=BPP1569 {ECO:0000313|EMBL:CAE36871.1};
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 aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; BX640427; CAE36871.1; -; Genomic_DNA.
DR   RefSeq; WP_010928094.1; NC_002928.3.
DR   EnsemblBacteria; CAE36871; CAE36871; BPP1569.
DR   KEGG; bpa:BPP1569; -.
DR   HOGENOM; HOG000271505; -.
DR   KO; K09472; -.
DR   OMA; MAPALCC; -.
DR   BioCyc; BPAR257311:G1GSY-1609-MONOMER; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WA24.
DR   SWISS-2DPAGE; Q7WA24.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000313|EMBL:CAE36871.1}.
FT   DOMAIN       33    492       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    267    267       {ECO:0000256|PROSITE-ProRule:PRU10007}.
FT   ACT_SITE    302    302       {ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   498 AA;  52943 MW;  6D48AD6B122D001F CRC64;
     MTLHDSAYWR AQAAALAPEG RAYIDGAYCD AADGATFAAH SPIDGRKLAD IAACGAADVD
     RAVAAARRAF EAGVWSGLAP RERKHRLLRL AALITEHQEE LALLETLDMG KPIRDALAFD
     LPETARCYAW YGEAIDKRYD EIAPTGADAL ATITREPLGV VAAVVPWNYP LMMAAWKVAP
     ALAVGNSVIL KPAEQASLSA LRLAALAEQA GIPPGVFSVV PGLGAQAGQA LGLHPDVDCI
     AFTGSTATGK RFMTYSGQSN LKRVWLECGG KSPHIVFADC PDLDRAAQVA ALAIFSNQGE
     VCIAGSRLYV QHGIYDAFME KVAAFAATLR PGNPLDPDSA LGAMVDERQT QAVMARIAAG
     AQEGARLRLG GRQVLTDSGG YYIEPTIFDC PGQDNSLVRE EIFGPVLAAQ GFADEDEAVA
     LANDSIYGLG AGLWTADLGR AHRLSRRLRA GLVWVNCYAD GDITVPFGGV KQSGFGRDKS
     LHAMDKYSDL KTTWISLR
//

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