ID E3HT68_ACHXA Unreviewed; 509 AA. AC E3HT68; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 60. DE SubName: Full=Acetaldehyde dehydrogenase {ECO:0000313|EMBL:ADP13694.1}; DE EC=1.2.1.3 {ECO:0000313|EMBL:ADP13694.1}; GN Name=aldB {ECO:0000313|EMBL:ADP13694.1}; GN OrderedLocusNames=AXYL_00335 {ECO:0000313|EMBL:ADP13694.1}; OS Achromobacter xylosoxidans (strain A8). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Achromobacter. OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP13694.1, ECO:0000313|Proteomes:UP000006876}; RN [1] {ECO:0000313|EMBL:ADP13694.1, ECO:0000313|Proteomes:UP000006876} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A8 {ECO:0000313|EMBL:ADP13694.1, RC ECO:0000313|Proteomes:UP000006876}; RX PubMed=21097610; DOI=10.1128/JB.01299-10; RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.; RT "Complete genome sequence of the haloaromatic acids-degrading bacterium RT Achromobacter xylosoxidans A8."; RL J. Bacteriol. 193:791-792(2011). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|RuleBase:RU003345}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002287; ADP13694.1; -; Genomic_DNA. DR RefSeq; WP_013391092.1; NC_014640.1. DR AlphaFoldDB; E3HT68; -. DR STRING; 762376.AXYL_00335; -. DR KEGG; axy:AXYL_00335; -. DR PATRIC; fig|762376.5.peg.334; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_0_0_4; -. DR OrthoDB; 6187633at2; -. DR Proteomes; UP000006876; 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; cd07116; ALDH_ACDHII-AcoD; 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 PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1. DR PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 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 30..496 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 265 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 509 AA; 55738 MW; 8AD0BE12C3782652 CRC64; MDIATRITPD SYGTRLDLKT QYDNFIDGKW QKPADGEYFD NVTPVTGQVL TRNARSKERD IELALDAAHR AAPKWGATPA AQRAHMLMQI ADVMEANLER LATAETWDNG KPIREARAAD IPLAIDHFRY FASCIRSQEG GLSEIDSDTV AYHFNEPLGV VGQIIPWNFP ILMAAWKLAP ALAAGNCVVL KPAEQTPLGI LLLMELIGDI LPAGVINVVT GFGLEAGKPL ASNKRIAKIA FTGETTTGRL IMQYASQNII PVTLELGGKS PNIFFADVAA QDDDFLDKAV EGFVMFALNQ GEVCTCPSRA LIQESLYDKF MERALKRVAE IKQGNPLDAD TMLGAQASTE QLEKILSYLD IGKQEGADVL AGGSRAQMQG ALEGGYYVQP TVFKGHNKMR VFQEEIFGPV VAVTTFKDAD DALALANDTL YGLGAGVWSR DANTCYRMGR AIKAGRVWTN CYHAYPAHAA FGGYKQSGIG RENHKMMLNH YQQTKNLLVS YSPKKLGFF //