BADH1_ORYSJ
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 03-AUG-2022, entry version 133.
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}.
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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; 4530.OS04T0464200-01; -.
DR PaxDb; O24174; -.
DR PRIDE; 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; AFTASMH; -.
DR OrthoDB; 153834at2759; -.
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 Genevisible; O24174; OS.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
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 (GAB-
FT ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in
FT 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 (GAB-
FT ald) and betaine aldehyde (Bet-ald) and 2-fold increase in
FT 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
