ID   Q3BX65_XANC5            Unreviewed;       489 AA.
AC   Q3BX65;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
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; Pseudomonadota; 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., Schneicker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   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   RefSeq; WP_011346489.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BX65; -.
DR   STRING; 456327.BJD11_18200; -.
DR   KEGG; xcv:XCV0917; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_0_6; -.
DR   Proteomes; UP000007069; 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   CDD; cd07139; ALDH_AldA-Rv0768; 1.
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   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          25..485
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
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
//