ID B6SXW4_MAIZE Unreviewed; 481 AA. AC B6SXW4; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 03-MAY-2023, entry version 70. DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG29697.1}; RN [1] {ECO:0000313|EMBL:ACG29697.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4; RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V., RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.; RT "Insights into corn genes derived from large-scale cDNA sequencing."; RL Plant Mol. Biol. 69:179-194(2009). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492, 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; EU957579; ACG29697.1; -; mRNA. DR RefSeq; NP_001148092.1; NM_001154620.1. DR AlphaFoldDB; B6SXW4; -. DR OrthoDB; 1205055at2759; -. DR ExpressionAtlas; B6SXW4; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro. 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; IPR012394; Aldehyde_DH_NAD(P). DR PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Membrane {ECO:0000256|SAM:Phobius}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492, KW ECO:0000256|RuleBase:RU003345}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 457..476 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 6..432 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 211 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1, FT ECO:0000256|PROSITE-ProRule:PRU10007" FT ACT_SITE 246 FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1" SQ SEQUENCE 481 AA; 52443 MW; 4C59AB36203F6E77 CRC64; MAGMAEETVR ELRASFAAGR TRPAEWRAAQ LKGLIRMIDE KEAEISAALH EDLAKPHMES FLHEISLTKS SCKFALKGLK NWMKPEKVPA AITTFPSSAQ IVPEPLGVVL IISAWNYPFI LSIDPVIGAI AAGNAVVLKP SEIAPATSSL LAKLLPEYVD NSCIKVVEGS VPETTALLEQ RWDKIFYTGN GTVGRIVMAA AAKHLTPVAL ELGGKSPVIV DSNVDLHVAA KRIVVGKWGC NNGQACIAPD YIITTKSFAP ELVASFKRVL ERFYGEDPLQ SADLSRIVNS KQFKRLTNLI EEKRVADKIV YGGKADEKQL KISPTLLLDV PEDSEIMTGE IFGPLLPIVT VEKIEESFDL INAKPKPLAA YLFTKNRKLQ EEFVASVPAG GMLVNDIALH LTNPYMPFGG VGDSGMGCYH GKFGFDCFSH KKGVLIRGFG GEANARYPPY TTEKQKILRG LINGSFIALI LALLGFPREK R //