ID C5CY69_VARPS Unreviewed; 512 AA. AC C5CY69; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226}; DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226}; GN OrderedLocusNames=Vapar_0310 {ECO:0000313|EMBL:ACS16973.1}; OS Variovorax paradoxus (strain S110). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS16973.1}; RN [1] {ECO:0000313|EMBL:ACS16973.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S110 {ECO:0000313|EMBL:ACS16973.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P., RA Leadbetter J.R., Spain J.C., Han J.I.; RT "Complete sequence of chromosome 1 of Variovorax paradoxus S110."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, 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; CP001635; ACS16973.1; -; Genomic_DNA. DR AlphaFoldDB; C5CY69; -. DR STRING; 543728.Vapar_0310; -. DR KEGG; vap:Vapar_0310; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_2_4; -. DR OrthoDB; 6187633at2; -. 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; cd07130; ALDH_F7_AASADH; 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 InterPro; IPR044638; ALDH7A1-like. DR PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 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 31..489 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 264 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 512 AA; 54017 MW; 558660CEC8F96F2B CRC64; MPEAQAFLSV ATEIAQLLQR LGVPGAAHTG GELTVRSPVT GEVVAQVRQT TAAEAAAAIG QAHEAFKAWR SVPAPRRGEL VRLLGEELRA AKADLGRLVT LEAGKIPSEG AGEVQEMIDI CDFAVGLSRQ LYGLTLATER AEHRMMETWH PLGVCGVISA FNFPVAVWSW NAALALVCGD SVVWKPSEKT PLTALAVHAI AQRALARFGD APEGLLGLLL GQRDIGEVLV DDHRVPILSA TGSTAMGRQV GPKLAARFAR AILELGGNNA AIVTPSADLD LTLRAIAFSA MGTAGQRCTT LRRLFVHDSV YDALVPKLAK VYGNVQVGDP REAGTLVGPL IDRAAFDGMQ KALGESREIG ATVHGGQRVE GIGTKDAFYV RPALVELKSH DGPVLRETFA PILYVVRYSA LDDAIEWHNA VGAGLSSSIF TLNVREAERF LSSAGSDCGI ANVNIGPSGA EIGGAFGGEK ETGGGREAGS DSWKAYMRRA TNTINYSTAL PLAQGVTFEI ND //