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Database: UniProt/TrEMBL
Entry: Q3BX65_XANC5
LinkDB: Q3BX65_XANC5
Original site: Q3BX65_XANC5 
ID   Q3BX65_XANC5            Unreviewed;       489 AA.
AC   Q3BX65;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   28-MAR-2018, entry version 79.
DE   SubName: Full=Putative aldehyde dehydrogenase {ECO:0000313|EMBL:CAJ22548.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:CAJ22548.1};
GN   OrderedLocusNames=XCV0917 {ECO:0000313|EMBL:CAJ22548.1};
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN   [1] {ECO:0000313|EMBL:CAJ22548.1, ECO:0000313|Proteomes:UP000007069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10 {ECO:0000313|EMBL:CAJ22548.1,
RC   ECO:0000313|Proteomes:UP000007069};
RX   PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O.,
RA   Schneicker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A.,
RA   Bonas U., Bartels D., Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant
RT   pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed
RT   by the complete genome sequence.";
RL   J. Bacteriol. 187:7254-7266(2005).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AM039952; CAJ22548.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q3BX65; -.
DR   STRING; 316273.XCV0917; -.
DR   EnsemblBacteria; CAJ22548; CAJ22548; XCV0917.
DR   KEGG; xcv:XCV0917; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00128; -.
DR   OMA; DINGGPF; -.
DR   OrthoDB; POG091H019T; -.
DR   BioCyc; XCAM316273:GJF8-920-MONOMER; -.
DR   Proteomes; UP000007069; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007069};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000313|EMBL:CAJ22548.1}.
FT   DOMAIN       25    485       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   489 AA;  52429 MW;  9BF2940283983924 CRC64;
     MEALFETLRG IAARGPLGLF IDGQWRASTG DRSVDVIAPH TEERLLRYTE PSHADTEAAI
     AAARRAFDHG PWPQLSPQAR SVALKRVADH LRARMPELAE AWTGQVGATL GFSKRASQQA
     PDLFDYYADL IATHAFVEPR VRPNGGRVHV VQEPVGVVAA ITPWNAPLVL LCYKVAAALA
     AGCTVVAKPS PETPIDAYIL AECISAAGVP DGVFNLLPAG REVGEQLIRH PHVDKVSFTG
     STQAGRSIGI ACAERLARVG LELGGKSAAI VLEDADIAKV LPTLVPYSMP IAGQVCFSLT
     RVLVPAQRRE EVLQAYCAAL SAVKLGDPFA EDTGMGPLAL GRQLERVQSY IAKGKAQGAR
     LAMGGGRPAH LSRGFFVEPT VFAEVTPDMT IAREEIFGPV VSFIDYHDEA DLIAKAKASD
     YGLHGTIYSE DAERAYRIAR RVRSGSHAIN GMWVDISMPF GGFKHSGIGR EGGIEGLHAF
     LETKTLYLS
//
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