ID BADH1_ORYSJ Reviewed; 505 AA. AC O24174; Q0JCK7; Q7F9Q3; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=Betaine aldehyde dehydrogenase 1; DE Short=OsBADH1; DE EC=1.2.1.8; GN Name=BADH1; OrderedLocusNames=Os04g0464200, LOC_Os04g39020; GN ORFNames=OSJNBa0060P14.8; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=9193078; DOI=10.1046/j.1365-313x.1997.11051115.x; RA Nakamura T., Yokota S., Muramoto Y., Tsutsui K., Oguri Y., Fukui K., RA Takabe T.; RT "Expression of a betaine aldehyde dehydrogenase gene in rice, a RT glycinebetaine nonaccumulator, and possible localization of its protein in RT peroxisomes."; RL Plant J. 11:1115-1120(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12447439; DOI=10.1038/nature01183; RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., RA Li J., Hong G., Xue Y., Han B.; RT "Sequence and analysis of rice chromosome 4."; RL Nature 420:316-320(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). RN [7] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY. RX PubMed=18704694; DOI=10.1007/s11103-008-9381-x; RA Bradbury L.M., Gillies S.A., Brushett D.J., Waters D.L., Henry R.J.; RT "Inactivation of an aminoaldehyde dehydrogenase is responsible for RT fragrance in rice."; RL Plant Mol. Biol. 68:439-449(2008). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY SUBMERGENCE, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=cv. Nipponbare; RX PubMed=19850038; DOI=10.1016/j.febslet.2009.10.039; RA Mitsuya S., Yokota Y., Fujiwara T., Mori N., Takabe T.; RT "OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant RT peroxisomes."; RL FEBS Lett. 583:3625-3629(2009). RN [9] RP FUNCTION, MUTAGENESIS OF ASN-164 AND TRP-172, BINDING OF BETAINE ALDEHYDE RP AND GAMMA-4-AMINOBUTYRALDEHYDE, INTERACTION WITH NAD, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22534193; DOI=10.1016/j.biochi.2012.04.009; RA Jiamsomboon K., Treesuwan W., Boonyalai N.; RT "Dissecting substrate specificity of two rice BADH isoforms: Enzyme RT kinetics, docking and molecular dynamics simulation studies."; RL Biochimie 94:1773-1783(2012). CC -!- FUNCTION: Dehydrogenase that can use N-acetyl-gamma-aminobutyraldehyde CC (NAGABald), gamma-guanidinobutyraldehyde (GGBald), betaine aldehyde CC (Bet-ald), gamma-aminobutyraldehyde (GAB-ald), acetaldehyde, 4- CC aminobutylaldehyde (AB-ald), 3-aminopropionaldehyde (AP-ald), 4-N- CC trimethylaminobutyraldehyde (TMAB-ald) and 3-N- CC trimethylaminopropionaldehyde (TMAP-ald) as substrates. Catalyzes the CC oxidation of GAB-ald more efficiently than Bet-ald. May convert CC acetaldehyde into acetate, thus facilitating the production of acetyl- CC CoA in peroxisomes under anaerobic conditions. CC {ECO:0000269|PubMed:18704694, ECO:0000269|PubMed:19850038, CC ECO:0000269|PubMed:22534193}. CC -!- CATALYTIC ACTIVITY: CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.8; CC Evidence={ECO:0000269|PubMed:18704694}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=420 uM for N-acetyl-gamma-aminobutyraldehyde (NAGABald) CC {ECO:0000269|PubMed:18704694}; CC KM=545 uM for gamma-guanidinobutyraldehyde (GGBald) CC {ECO:0000269|PubMed:18704694}; CC KM=3 mM for betaine aldehyde {ECO:0000269|PubMed:18704694}; CC KM=497 uM for gamma-aminobutyraldehyde {ECO:0000269|PubMed:18704694}; CC KM=1.29 mM for betaine aldehyde (at 30 degrees Celsius) CC {ECO:0000269|PubMed:22534193}; CC KM=432 uM for gamma-aminobutyraldehyde (at 30 degrees Celsius) CC {ECO:0000269|PubMed:22534193}; CC KM=99 uM for acetaldehyde (at 30 degrees Celsius) CC {ECO:0000269|PubMed:22534193}; CC KM=2.6 mM for betaine aldehyde {ECO:0000269|PubMed:19850038}; CC KM=4.5 uM for 4-aminobutyraldehyde (AB-ald) CC {ECO:0000269|PubMed:19850038}; CC KM=17 uM for 3-aminopropionaldehyde (AP-ald) CC {ECO:0000269|PubMed:19850038}; CC KM=7.8 uM for 4-N-trimethylaminobutyraldehyde (TMAB-ald) CC {ECO:0000269|PubMed:19850038}; CC KM=35 uM for 3-N-trimethylaminopropionaldehyde (TMAP-ald) CC {ECO:0000269|PubMed:19850038}; CC KM=130 uM for acetaldehyde {ECO:0000269|PubMed:19850038}; CC Vmax=0.71 umol/min/mg enzyme with acetaldehyde as substrate CC {ECO:0000269|PubMed:19850038}; CC pH dependence: CC Optimum pH is 9.5. {ECO:0000269|PubMed:18704694, CC ECO:0000269|PubMed:19850038, ECO:0000269|PubMed:22534193}; CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via CC choline pathway; betaine from betaine aldehyde: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19850038}. CC -!- INDUCTION: Following submergence treatment, transient decreased levels CC that recovers after re-aeration. {ECO:0000269|PubMed:19850038}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. 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; AB001348; BAA21098.1; -; Genomic_DNA. DR EMBL; AL663017; CAD41035.1; -; Genomic_DNA. DR EMBL; AP008210; BAF14930.1; -; Genomic_DNA. DR EMBL; AP014960; BAS89584.1; -; Genomic_DNA. DR EMBL; AK103582; BAG96152.1; -; mRNA. DR PIR; T03394; T03394. DR RefSeq; XP_015637091.1; XM_015781605.1. DR AlphaFoldDB; O24174; -. DR SMR; O24174; -. DR STRING; 39947.O24174; -. DR PaxDb; 39947-O24174; -. DR EnsemblPlants; Os04t0464200-01; Os04t0464200-01; Os04g0464200. DR GeneID; 4336081; -. DR Gramene; Os04t0464200-01; Os04t0464200-01; Os04g0464200. DR KEGG; osa:4336081; -. DR eggNOG; KOG2450; Eukaryota. DR HOGENOM; CLU_005391_0_1_1; -. DR InParanoid; O24174; -. DR OMA; GDHTSYV; -. DR OrthoDB; 3078548at2759; -. DR BRENDA; 1.2.1.8; 4460. DR PlantReactome; R-OSA-1119579; Glycine betaine biosynthesis III. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000000763; Chromosome 4. DR Proteomes; UP000059680; Chromosome 4. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0071454; P:cellular response to anoxia; IDA:UniProtKB. DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway. DR CDD; cd07110; ALDH_F10_BADH; 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; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1. DR PANTHER; PTHR43860:SF7; BETAINE ALDEHYDE DEHYDROGENASE 1; 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. DR Genevisible; O24174; OS. PE 1: Evidence at protein level; KW NAD; Oxidoreductase; Peroxisome; Reference proteome. FT CHAIN 1..505 FT /note="Betaine aldehyde dehydrogenase 1" FT /id="PRO_0000056530" FT MOTIF 503..505 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT ACT_SITE 262 FT /evidence="ECO:0000250" FT ACT_SITE 296 FT /evidence="ECO:0000250" FT BINDING 163..172 FT /ligand="betaine aldehyde" FT /ligand_id="ChEBI:CHEBI:15710" FT /evidence="ECO:0000305" FT BINDING 240..245 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 262..263 FT /ligand="4-aminobutanal" FT /ligand_id="ChEBI:CHEBI:58264" FT /evidence="ECO:0000305" FT BINDING 262 FT /ligand="betaine aldehyde" FT /ligand_id="ChEBI:CHEBI:15710" FT /evidence="ECO:0000305" FT BINDING 294..297 FT /ligand="betaine aldehyde" FT /ligand_id="ChEBI:CHEBI:15710" FT /evidence="ECO:0000305" FT BINDING 296 FT /ligand="4-aminobutanal" FT /ligand_id="ChEBI:CHEBI:58264" FT /evidence="ECO:0000305" FT BINDING 455 FT /ligand="betaine aldehyde" FT /ligand_id="ChEBI:CHEBI:15710" FT /evidence="ECO:0000305" FT BINDING 461 FT /ligand="4-aminobutanal" FT /ligand_id="ChEBI:CHEBI:58264" FT /evidence="ECO:0000305" FT MUTAGEN 164 FT /note="N->A: Slightly reduced affinity for NAD, 6-fold FT enhanced affinity for both gamma-4-aminobutyraldehyde FT (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold FT decrease in catalytic efficiency." FT /evidence="ECO:0000269|PubMed:22534193" FT MUTAGEN 172 FT /note="W->A: Slightly reduced affinity for NAD, enhanced FT affinity for both betaine aldehyde (Bet-ald) (10-fold) and FT gamma-4-aminobutyraldehyde (GAB-ald) (2-fold)." FT /evidence="ECO:0000269|PubMed:22534193" FT MUTAGEN 172 FT /note="W->F: Slightly reduced affinity for NAD, but 6-fold FT enhanced affinity for both gamma-4-aminobutyraldehyde FT (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold FT increase in catalytic efficiency towards GAB-ald." FT /evidence="ECO:0000269|PubMed:22534193" SQ SEQUENCE 505 AA; 54648 MW; 85EFA42B059A8081 CRC64; MAAPSAIPRR GLFIGGGWRE PSLGRRLPVV NPATEATIGD IPAATAEDVE LAVSAARDAF GRDGGRHWSR APGAVRAKYL KAIAAKIKDK KSYLALLETL DSGKPLDEAA GDMEDVAACF EYYADLAEAL DGKQRAPISL PMENFESYVL KEPIGVVGLI TPWNYPLLMA TWKVAPALAA GCTAVLKPSE LASLTCLELG GICAEIGLPP GVLNIITGLG TEAGAPLASH PHVDKIAFTG STETGKRIMI TASQMVKPVS LELGGKSPLI VFDDVDIDKA VEWAMFGCFA NAGQVCSATS RLLLHEKIAK RFLDRLVAWA KSIKISDPLE EGCRLGSVVS EGQYQKIMKF ISTARCEGAT ILYGGARPQH LKRGFFIEPT IITNVSTSMQ IWREEVFGPV ICVKEFRTER EAVELANDTH YGLAGAVISN DLERCERISK AIQSGIVWIN CSQPCFVQAP WGGNKRSGFG RELGQWGLDN YLSVKQVTKY CSDEPYGWYR PPSKL //