ID Q5KYI5_GEOKA Unreviewed; 488 AA. AC Q5KYI5; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 97. DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:BAD76251.1}; GN OrderedLocusNames=GK1966 {ECO:0000313|EMBL:BAD76251.1}; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD76251.1, ECO:0000313|Proteomes:UP000001172}; RN [1] {ECO:0000313|EMBL:BAD76251.1, ECO:0000313|Proteomes:UP000001172} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD76251.1, RC ECO:0000313|Proteomes:UP000001172}; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of thermophilic RT Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(2004). 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; BA000043; BAD76251.1; -; Genomic_DNA. DR RefSeq; WP_011231452.1; NC_006510.1. DR AlphaFoldDB; Q5KYI5; -. DR STRING; 235909.GK1966; -. DR KEGG; gka:GK1966; -. DR PATRIC; fig|235909.7.peg.2106; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_0_9; -. DR Proteomes; UP000001172; Chromosome. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR CDD; cd07097; ALDH_KGSADH-YcbD; 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; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1. DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-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}; KW Reference proteome {ECO:0000313|Proteomes:UP000001172}. FT DOMAIN 18..484 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 255 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 488 AA; 52747 MW; ABEE0A290A5AD9C3 CRC64; MAVQTEIKTY LNYIDGSWVG SVSKNVEPSI NPANRNDIVG YVPRSTLEDL NAAVAAAKQA QKSWWKRSGI ERGEYLYKAA LLLEQRLEDI AETMTREMGK TLAEAKAETM RGVHILRYYA GEGARKIGDV IPSSDSGGLM FTTRVPLGVV GVISPWNFPV AIPIWKMAPA LVYGNTVVLK PASETAVTAA KVIECFHEAG FPKGVVNMVC GSGSVIGQGI ANHPDVDGVT FTGSNTVGKQ VGRAAFERGA KYQLEMGGKN PVIVAKDADL DLAVEGTISG GLRSTGQKCT ATSRVFIERE VYEPFKEKLL ERVKQLKIGN GMDAETWMGP CASESQLNTV LSYIEKGKAE GAKLIYGGNR CTEGELANGF YVEPTIFEEV DLQMTIAREE IFGPVLVLIP VDSIEEAIEL ANDTEYGLSA SIYTKNIGNI LDFIKDIEAG LVKVNAETAG VEYQAPFGGM KQSSSHSREQ GQAAIEFFTT IKTVFVKA //