ID Q5FP50_GLUOX Unreviewed; 512 AA. AC Q5FP50; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226}; DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226}; GN OrderedLocusNames=GOX2110 {ECO:0000313|EMBL:AAW61846.1}; OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61846.1, ECO:0000313|Proteomes:UP000006375}; RN [1] {ECO:0000313|EMBL:AAW61846.1, ECO:0000313|Proteomes:UP000006375} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=621H {ECO:0000313|EMBL:AAW61846.1, RC ECO:0000313|Proteomes:UP000006375}; RX PubMed=15665824; DOI=10.1038/nbt1062; RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., RA Ehrenreich A., Gottschalk G., Deppenmeier U.; RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). 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; CP000009; AAW61846.1; -; Genomic_DNA. DR RefSeq; WP_011253623.1; NZ_LT900338.1. DR AlphaFoldDB; Q5FP50; -. DR SMR; Q5FP50; -. DR STRING; 290633.GOX2110; -. DR KEGG; gox:GOX2110; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_2_5; -. DR Proteomes; UP000006375; 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; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000006375}. FT DOMAIN 27..486 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 260 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 512 AA; 54226 MW; A83956BBC1A93939 CRC64; MTASLRCEVA ALLDSLGVSP DLYTGGSLAV KSPLTGEVIA EVSEVSAEQA KETIASSLDA FKAWRRVPAP RRGELVRLLG EELRASKEAL GRLVTLEVGK VPSEGLGEVQ EMIDICDFAV GLSRQLYGLT IQSERPDHRL TEQWHPAGPV GIISAFNFPV AVWSWNAALA LVCGDSVIWK PSEKTPLTAL ATQALFLKAA ARFGSDAPVA LSTLLVGGRE IGELMVKDRR VPVISATGST RMGRDVGERV ARRFGRSILE LGGNNASIVT PSADLDLTLR AVAFGAMGTA GQRCTTLRRL FVHSSVYDTL VPKLVNVYKT ISVGNPVEGD ALVGPLIDVA SFKMMQDSLK AAADAGGTVH GGTRVDVNGE ASFYVRPAMV EMPSQTGPVL EETFAPILYV MKYDTLDEAI ALQNDVVQGL SSSIFATDIR EVEQFLSAQG SDCGIANVNM GPSGAEIGGA FGGEKETGGG RESGSDAWKA YMRRQTNAIN YGRTLPLAQG VKFDVYGGSA DA //