BADH2_ORYSI
ID BADH2_ORYSI Reviewed; 503 AA.
AC B3VMC0;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Betaine aldehyde dehydrogenase 2;
DE Short=BADH 2;
DE EC=1.2.1.8;
GN Name=BADH2; ORFNames=OsI_29289;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND ROLE IN RICE
RP FRAGRANCE.
RC STRAIN=cv. Nanjing 11;
RX PubMed=18599581; DOI=10.1105/tpc.108.058917;
RA Chen S., Yang Y., Shi W., Ji Q., He F., Zhang Z., Cheng Z., Liu X., Xu M.;
RT "Badh2, encoding betaine aldehyde dehydrogenase, inhibits the biosynthesis
RT of 2-acetyl-1-pyrroline, a major component in rice fragrance.";
RL Plant Cell 20:1850-1861(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP ROLE IN RICE FRAGRANCE.
RX PubMed=19706531; DOI=10.1073/pnas.0904077106;
RA Kovach M.J., Calingacion M.N., Fitzgerald M.A., McCouch S.R.;
RT "The origin and evolution of fragrance in rice (Oryza sativa L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14444-14449(2009).
CC -!- FUNCTION: Dehydrogenase that can use N-acetyl-c-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. Mediates the
CC conversion of GAB-ald into gamma-aminobutyric acid (GABA), and prevents
CC the formation of 2-acetyl-1-pyrroline (2AP) which gives fragrant rice
CC its aromatic properties. {ECO:0000269|PubMed:18599581}.
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 -!- 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:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present in a truncated form, mostly allele badh2.1, also
CC called 'fgr' in fragrant rice varieties (e.g. basmati and jasmine
CC rice). The loss of activity leads to accumulation of 2-acetyl-1-
CC pyrroline (2AP) that confers the flavor of fragrant rice. Haplotype
CC analysis suggests a single origin of the badh2.1 allele within the
CC Japonica varietal group and demonstrates the introgression of this
CC allele from Japonica to Indica (PubMed:18599581, PubMed:19706531).
CC {ECO:0000305|PubMed:18599581, ECO:0000305|PubMed:19706531}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; EU770319; ACF06146.1; -; Genomic_DNA.
DR EMBL; EU770322; ACF06149.1; -; mRNA.
DR EMBL; CM000133; EEC83602.1; -; Genomic_DNA.
DR AlphaFoldDB; B3VMC0; -.
DR SMR; B3VMC0; -.
DR STRING; 39946.B3VMC0; -.
DR EnsemblPlants; BGIOSGA028697-TA; BGIOSGA028697-PA; BGIOSGA028697.
DR Gramene; BGIOSGA028697-TA; BGIOSGA028697-PA; BGIOSGA028697.
DR HOGENOM; CLU_005391_0_1_1; -.
DR OMA; EGGHYSF; -.
DR BRENDA; 1.2.1.8; 4460.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000007015; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0071454; P:cellular response to anoxia; ISS: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 2: Evidence at transcript level;
KW Cytoplasm; NAD; Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..503
FT /note="Betaine aldehyde dehydrogenase 2"
FT /id="PRO_0000430058"
FT MOTIF 501..503
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 260
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /evidence="ECO:0000250"
FT BINDING 161..170
FT /ligand="betaine aldehyde"
FT /ligand_id="ChEBI:CHEBI:15710"
FT /evidence="ECO:0000250"
FT BINDING 238..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 260..261
FT /ligand="4-aminobutanal"
FT /ligand_id="ChEBI:CHEBI:58264"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="betaine aldehyde"
FT /ligand_id="ChEBI:CHEBI:15710"
FT /evidence="ECO:0000250"
FT BINDING 292..295
FT /ligand="betaine aldehyde"
FT /ligand_id="ChEBI:CHEBI:15710"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="4-aminobutanal"
FT /ligand_id="ChEBI:CHEBI:58264"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="betaine aldehyde"
FT /ligand_id="ChEBI:CHEBI:15710"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="4-aminobutanal"
FT /ligand_id="ChEBI:CHEBI:58264"
FT /evidence="ECO:0000250"
SQ SEQUENCE 503 AA; 54683 MW; 1011B305C31F4446 CRC64;
MATAIPQRQL FVAGEWRAPA LGRRLPVVNP ATESPIGEIP AGTAEDVDAA VAAAREALKR
NRGRDWARAP GAVRAKYLRA IAAKIIERKS ELARLETLDC GKPLDEAAWD MDDVAGCFEY
FADLAESLDK RQNAPVSLPM ENFKCYLRKE PIGVVGLITP WNYPLLMATW KVAPALAAGC
TAVLKPSELA SVTCLELADV CKEVGLPSGV LNIVTGLGSE AGAPLSSHPG VDKVAFTGSY
ETGKKIMASA APMVKPVSLE LGGKSPIVVF DDVDVEKAVE WTLFGCFWTN GQICSATSRL
ILHKKIAKEF QERMVAWAKN IKVSDPLEEG CRLGPVVSEG QYEKIKQFVS TAKSQGATIL
TGGVRPKHLE KGFYIEPTII TDVDTSMQIW REEVFGPVLC VKEFSTEEEA IELANDTHYG
LAGAVLSGDR ERCQRLTEEI DAGIIWVNCS QPCFCQAPWG GNKRSGFGRE LGEGGIDNYL
SVKQVTEYAS DEPWGWYKSP SKL
