(data stored in SCRATCH zone)

SWISSPROT: Q7WAP9_BORPA

ID   Q7WAP9_BORPA            Unreviewed;       530 AA.
AC   Q7WAP9;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:CAE36625.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:CAE36625.1};
GN   Name=acoD {ECO:0000313|EMBL:CAE36625.1};
GN   OrderedLocusNames=BPP1323 {ECO:0000313|EMBL:CAE36625.1};
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; CAE36625.1; -; Genomic_DNA.
DR   EnsemblBacteria; CAE36625; CAE36625; BPP1323.
DR   KEGG; bpa:BPP1323; -.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00138; -.
DR   OMA; TFVQEDV; -.
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; Q7WAP9.
DR   SWISS-2DPAGE; Q7WAP9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000313|EMBL:CAE36625.1}.
FT   DOMAIN       50    516       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    285    285       {ECO:0000256|PROSITE-ProRule:PRU10007}.
FT   ACT_SITE    324    324       {ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   530 AA;  57612 MW;  F0576442031B783C CRC64;
     MRPPRDGKQS SRRHNDIRRQ TMDLSDLKKL GLDVAYPFKE QYENYIGGQW VPPVGAEYFD
     NLSPITGQPF CRVPRSGAAD IELALDAAHR ARAAWARTSP AERANILLRI ADRIEGQLPM
     LAVAESIDNG KPLRETTAAD LPLAIDHFRY FAGCIRAQEG AISEIDANTV AYHFHEPIGV
     VGQIIPWNFP LLMAAWKLAP ALAAGCVVVL KPAEQTPASI LVLAELIGDL LPPGVLNVVN
     GYGKEAGQAL ATSKRIAKIA FTGSTPVGKH ILHAAADNLI PATVELGGKN PNIFFDDVMD
     HDDEFLDKAL EGLAMFALNQ GEVCTCPSRI LIQESIYERF IEKAIARVQS IKTGHPLDAG
     TMVGAQVSQV QMDKILSYID IGRQEGAQCL TGGARNDMLP GGLDQGFYVQ PTMLLGKNSM
     RIFQEEIFGP VAAVATFKDE EEAIAMANDT FYGLGAGVWS RDGARAYRVG RGIEAGRVWT
     NCYHLYPAHA AFGGYKQSGI GRETHKAALS NYQQTKCLLV SYSAKALGFF
//

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