BALDH_ANTMA
ID BALDH_ANTMA Reviewed; 534 AA.
AC C7A2A0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Benzaldehyde dehydrogenase, mitochondrial {ECO:0000303|PubMed:19292760};
DE EC=1.2.1.28 {ECO:0000269|PubMed:19292760};
DE AltName: Full=2-phenylacetaldehyde dehydrogenase {ECO:0000305};
DE EC=1.2.1.39 {ECO:0000269|PubMed:19292760};
DE AltName: Full=Acetaldehyde dehydrogenase {ECO:0000305};
DE EC=1.2.1.3 {ECO:0000269|PubMed:19292760};
DE Flags: Precursor;
GN Name=BALDH {ECO:0000303|PubMed:19292760};
OS Antirrhinum majus (Garden snapdragon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=4151;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=cv. Maryland True Pink; TISSUE=Petal;
RX PubMed=19292760; DOI=10.1111/j.1365-313x.2009.03864.x;
RA Long M.C., Nagegowda D.A., Kaminaga Y., Ho K.K., Kish C.M., Schnepp J.,
RA Sherman D., Weiner H., Rhodes D., Dudareva N.;
RT "Involvement of snapdragon benzaldehyde dehydrogenase in benzoic acid
RT biosynthesis.";
RL Plant J. 59:256-265(2009).
CC -!- FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid
CC (FVBP) biosynthetic pathway (PubMed:19292760). Catalyzes the oxidation
CC of benzaldehyde to benzoic acid (BA) (PubMed:19292760). Capable of
CC oxidizing a broad spectrum of aliphatic aldehydes; increased carbon
CC chain length results in a decrease in its efficiency (PubMed:19292760).
CC {ECO:0000269|PubMed:19292760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000269|PubMed:19292760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000269|PubMed:19292760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000269|PubMed:19292760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295;
CC Evidence={ECO:0000269|PubMed:19292760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC Evidence={ECO:0000269|PubMed:19292760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841;
CC Evidence={ECO:0000269|PubMed:19292760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylacetaldehyde + H2O + NAD(+) = 2-phenylacetate + 2 H(+)
CC + NADH; Xref=Rhea:RHEA:21392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16424, ChEBI:CHEBI:18401, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.39;
CC Evidence={ECO:0000269|PubMed:19292760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21393;
CC Evidence={ECO:0000269|PubMed:19292760};
CC -!- ACTIVITY REGULATION: Inhibited by disulfiram.
CC {ECO:0000269|PubMed:19292760}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.37 uM for benzaldehyde {ECO:0000269|PubMed:19292760};
CC KM=2.01 uM for acetaldehyde {ECO:0000269|PubMed:19292760};
CC KM=5.35 uM for phenylacetaldehyde {ECO:0000269|PubMed:19292760};
CC Vmax=1.32 nmol/sec/mg enzyme with benzaldehyde as substrate
CC {ECO:0000269|PubMed:19292760};
CC Vmax=8.93 nmol/sec/mg enzyme with acetaldehyde as substrate
CC {ECO:0000269|PubMed:19292760};
CC Vmax=1.00 nmol/sec/mg enzyme with phenylacetaldehyde as substrate
CC {ECO:0000269|PubMed:19292760};
CC Note=kcat is 0.31 sec(-1) with benzaldehyde as substrate
CC (PubMed:19292760). kcat is 2.08 sec(-1) with acetaldehyde as
CC substrate (PubMed:19292760). kcat is 0.23 sec(-1) with
CC phenylacetaldehyde as substrate (PubMed:19292760).
CC {ECO:0000269|PubMed:19292760};
CC pH dependence:
CC Optimum pH is 8. Active in a broad range of pH varying from 6 to 9.
CC {ECO:0000269|PubMed:19292760};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:19292760}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P51977}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19292760}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the upper and lower
CC flower petal lobes, and, at low levels, in flower tubes, pistils,
CC stamens and sepals. {ECO:0000269|PubMed:19292760}.
CC -!- DEVELOPMENTAL STAGE: In corollas, accumulates progressively during
CC flower development, from buds to anthesis, with a peak at flower
CC opening, but fades out in senescing flowers.
CC {ECO:0000269|PubMed:19292760}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring from the
CC late afternoon hours until early morning and lowest levels during the
CC afternoon in flowers. {ECO:0000269|PubMed:19292760}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; FJ151199; ACM89738.1; -; mRNA.
DR AlphaFoldDB; C7A2A0; -.
DR SMR; C7A2A0; -.
DR PRIDE; C7A2A0; -.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IDA:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
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 Mitochondrion; NAD; Oxidoreductase; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..534
FT /note="Benzaldehyde dehydrogenase, mitochondrial"
FT /id="PRO_0000451519"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 199..202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 225..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 258..259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 278..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT BINDING 301..303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 381..385
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 432..434
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P51977"
FT SITE 202
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P51977"
SQ SEQUENCE 534 AA; 58190 MW; 69FC11EFA18DD055 CRC64;
MAAHRFSSLL SRSVPLLSRG GKQSYLGRGV YRYGTAAAAA LEEPIKPPVS VQYDKLLING
QFVDAASGKT FPTLDPRSGE VIAHVAEGDA EDINRAVAAA RKAFDEGPWP KMPAYERQKI
MLRFADLVEK HNDEVAALEA WDSGKPYEQC AQVEIPMFVR LFRYYAGWAD KIHGLTIPAD
GPHHVQTLHE PIGVAGQIIP WNFPLVMFGW KVGPALACGN SVVLKTAEQT PLSALLVSKL
FHEAGLPEGV LNIVSGFGPT AGAALCRHMD VDKLAFTGST ETGKIVLELS AKSNLKPVTL
ELGGKSPFIV CEDADVDKAV ELAHFALFFN QGQCCCAGSR TFVHEKVYDE FVEKAKARAL
KRTVGDPFKA GMEQGPQVDA DQFEKILKYI RSGAESGATL ETGGDRLGTK GYYIQPTVFS
DVKDDMLIAK DEIFGPVQTI LKFKELDEVI RRANNSSYGL AAGVFTQNLD TANTMMRALR
AGTVWINCFD TFDAAIPFGG YKMSGIGREK GEYSLKNYLQ VKAVVTALKN PAWL
