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Benzaldehyde dehydrogenase (NAD( )) (EC 1.2.1.28) (Aldehyde oxidase 4) (AO-4) (AtAO-4) (AtAO2) (Indole-3-acetaldehyde oxidase) (IAA oxidase) (EC 1.2.3.7)

 ALDO4_ARATH             Reviewed;        1337 AA.
Q7G191; O23027; O49157; Q7GB29;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
10-OCT-2018, entry version 116.
RecName: Full=Benzaldehyde dehydrogenase (NAD(+));
EC=1.2.1.28;
AltName: Full=Aldehyde oxidase 4;
Short=AO-4;
Short=AtAO-4;
Short=AtAO2;
AltName: Full=Indole-3-acetaldehyde oxidase;
Short=IAA oxidase;
EC=1.2.3.7;
Name=AAO4; Synonyms=AO2; OrderedLocusNames=At1g04580;
ORFNames=T1G11.17;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Rosette leaf;
Seo M., Koshiba T.;
"Arabidopsis aldehyde oxidase cDNA.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1337.
STRAIN=cv. Wassilewskija; TISSUE=Root;
PubMed=9655945; DOI=10.1016/S0167-4781(98)00085-2;
Hoff T., Frandsen G.I., Rocher A., Mundy J.;
"Biochemical and genetic characterization of three molybdenum cofactor
hydroxylases in Arabidopsis thaliana.";
Biochim. Biophys. Acta 1398:397-402(1998).
[5]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=10972874; DOI=10.1046/j.1365-313x.2000.00812.x;
Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y.,
Koshiba T.;
"Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
Plant J. 23:481-488(2000).
[6]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15574845; DOI=10.1093/pcp/pch198;
Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T.;
"Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene
family revealed a major role of AAO3 in ABA biosynthesis in seeds.";
Plant Cell Physiol. 45:1694-1703(2004).
[7]
FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
STRAIN=cv. Columbia;
PubMed=19297586; DOI=10.1104/pp.109.135848;
Ibdah M., Chen Y.-T., Wilkerson C.G., Pichersky E.;
"An aldehyde oxidase in developing seeds of Arabidopsis converts
benzaldehyde to benzoic Acid.";
Plant Physiol. 150:416-423(2009).
-!- FUNCTION: Involved in the accumulation of benzoic acid (BA) in
siliques. {ECO:0000269|PubMed:19297586}.
-!- CATALYTIC ACTIVITY: Benzaldehyde + NAD(+) + H(2)O = benzoate +
NADH. {ECO:0000269|PubMed:19297586}.
-!- CATALYTIC ACTIVITY: (Indol-3-yl)acetaldehyde + H(2)O + O(2) =
(indol-3-yl)acetate + H(2)O(2). {ECO:0000269|PubMed:19297586}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000250};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000250};
-!- ACTIVITY REGULATION: Inhibited by Cu(2+).
{ECO:0000269|PubMed:19297586}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=23 uM for benzoic acid (BA) (at pH7, in the presence of
NAD(+)) {ECO:0000269|PubMed:19297586};
KM=58.1 uM for NAD(+) (at pH7, in the presence of benzoic acid
(BA)) {ECO:0000269|PubMed:19297586};
KM=2.07 uM for indole-3-acetaldehyde (at pH7)
{ECO:0000269|PubMed:19297586};
KM=103.9 uM for cinnamylaldehyde (at pH7)
{ECO:0000269|PubMed:19297586};
Vmax=1.2 nmol/sec/mg enzyme with benzoic acid (BA) as substrate
(at pH7, in the presence of NAD(+))
{ECO:0000269|PubMed:19297586};
Vmax=3.2 nmol/sec/mg enzyme with NAD(+) as substrate (at pH7, in
the presence of benzoic acid (BA))
{ECO:0000269|PubMed:19297586};
Vmax=1.5 nmol/sec/mg enzyme with indole-3-acetaldehyde as
substrate (at pH7) {ECO:0000269|PubMed:19297586};
Vmax=5.5 nmol/sec/mg enzyme with cinnamylaldehyde as substrate
(at pH7) {ECO:0000269|PubMed:19297586};
Note=Kcat is 95.2 sec(-1) with benzoic acid (BA) as substrate,
253.9 sec(-1) with NAD(+) as substrate, 1.904 sec(-1) with
indole-3-acetaldehyde as substrate, and 436.5 sec(-1) with
cinnamylaldehyde as substrate (at pH 7, PubMed:19297586).;
pH dependence:
Optimum pH is 7. {ECO:0000269|PubMed:19297586};
Temperature dependence:
Optimum temperature is 30 degrees Celsius.
{ECO:0000269|PubMed:19297586};
-!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of
AO subunits. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19297586}.
-!- TISSUE SPECIFICITY: Transcripts expressed at high levels in
developing siliques and at low levels in dry seeds.
{ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:15574845}.
-!- INDUCTION: Induced by dehydration, in rosette but not in roots.
{ECO:0000269|PubMed:10972874}.
-!- DISRUPTION PHENOTYPE: Plants have normal abscisic acid (ABA)
levels, normal germination and are not affected in abscisic
aldehyde oxidase activity in siliques, dry seeds and leaves.
Reduced levels of benzoic acid (BA), 3-
benzoyloxypropylglucosinolate and 4-benzoyloxybutylglucosinolate
in seeds. {ECO:0000269|PubMed:15574845,
ECO:0000269|PubMed:19297586}.
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB80640.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB037271; BAA90299.1; -; mRNA.
EMBL; AC002376; AAB80640.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE27717.1; -; Genomic_DNA.
EMBL; AF039897; AAC39511.1; -; mRNA.
PIR; D86178; D86178.
PIR; T52051; T52051.
RefSeq; NP_563711.1; NM_100337.3.
UniGene; At.465; -.
ProteinModelPortal; Q7G191; -.
SMR; Q7G191; -.
STRING; 3702.AT1G04580.1; -.
iPTMnet; Q7G191; -.
PaxDb; Q7G191; -.
PRIDE; Q7G191; -.
EnsemblPlants; AT1G04580.1; AT1G04580.1; AT1G04580.
GeneID; 839488; -.
Gramene; AT1G04580.1; AT1G04580.1; AT1G04580.
KEGG; ath:AT1G04580; -.
Araport; AT1G04580; -.
TAIR; locus:2197798; AT1G04580.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
InParanoid; Q7G191; -.
KO; K22417; -.
OMA; PYINAAF; -.
OrthoDB; EOG093600DW; -.
PhylomeDB; Q7G191; -.
BRENDA; 1.2.3.1; 399.
Reactome; R-ATH-964975; Vitamins B6 activation to pyridoxal phosphate.
PRO; PR:Q7G191; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q7G191; baseline and differential.
Genevisible; Q7G191; AT.
GO; GO:0005829; C:cytosol; TAS:TAIR.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0018488; F:aryl-aldehyde oxidase activity; IDA:TAIR.
GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:TAIR.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
CDD; cd00207; fer2; 1.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016166; FAD-bd_PCMH.
InterPro; IPR036318; FAD-bd_PCMH-like_sf.
InterPro; IPR002346; Mopterin_DH_FAD-bd.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
Pfam; PF03450; CO_deh_flav_C; 1.
Pfam; PF00941; FAD_binding_5; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF01799; Fer2_2; 1.
PIRSF; PIRSF000127; Xanthine_DH; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SMART; SM01092; CO_deh_flav_C; 1.
SUPFAM; SSF47741; SSF47741; 1.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF55447; SSF55447; 1.
SUPFAM; SSF56003; SSF56003; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51387; FAD_PCMH; 1.
1: Evidence at protein level;
2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis;
Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur;
Metal-binding; Molybdenum; NAD; Oxidoreductase; Reference proteome.
CHAIN 1 1337 Benzaldehyde dehydrogenase (NAD(+)).
/FTId=PRO_0000166112.
DOMAIN 4 91 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 225 409 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
METAL 43 43 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 48 48 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 51 51 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
CONFLICT 1257 1257 V -> I (in Ref. 4; AAC39511).
{ECO:0000305}.
SEQUENCE 1337 AA; 147304 MW; 8DCF487FA3F7D6B8 CRC64;
MAGDDLVFAV NGEKFEVLSV NPSTTLLEFL RSNTCFKSVK LSCGEGGCGA CIVILSKYDP
VLDQVEEYSI NSCLTLLCSL NGCSITTSDG LGNTEKGFHP IHKRFAGFHA SQCGFCTPGM
CISLYSALSK AHNSQSSPDY LTALAAEKSI AGNLCRCTGY RPIADACKSF ASDVDIEDLG
FNSFWRKGES REEMLKKLPP YNPEKDLITF PDFLKEKIKC QHNVLDQTRY HWSTPGSVAE
LQEILATTNP GKDRGLIKLV VGNTGTGYYK EEKQYGRYID ISHIPEMSMI KKDDREIEIG
AVVTISKVID ALMEENTSAY VFKKIGVHME KVANHFIRNS GSIGGNLVMA QSKSFPSDIT
TLLLAADASV HMINAGRHEK LRMGEYLVSP PILDTKTVLL KVHIPRWIAS STTGLLFETY
RAALRPIGSA LPYINAAFLA VVSHDASSSG IIVDKCRLAF GSYGGYHSIR AREVEDFLTG
KILSHSVLYE AVRLLKGIIV PSIDTSYSEY KKSLAVGFLF DFLYPLIESG SWDSEGKHID
GHIDPTICLP LLSSAQQVFE SKEYHPVGEA IIKFGAEMQA SGEAVYVDDI PSLPHCLHGA
FIYSTKPLAW IKSVGFSGNV TPIGVLAVIT FKDIPEVGQN IGYITMFGTG LLFADEVTIS
AGQIIALVVA DTQKHADMAA HLAVVEYDSR NIGTPVLSVE DAVKRSSLFE VPPEYQPEPV
GDISKGMAEA DRKIRSVELR LGSQYFFYME TQTALALPDE DNCLVVYSST QAPEFTQTVI
ATCLGIPEHN VRVITRRVGG GFGGKAIKSM PVATACALAA KKMQRPVRIY VNRKTDMIMA
GGRHPLKITY SVGFRSDGKL TALDLNLFID AGSDVDVSLV MPQNIMNSLR KYDWGALSFD
IKVCKTNLPS RTSLRAPGEV QGSYIAESII ENVASSLKMD VDVVRRINLH TYESLRKFYK
QAAGEPDEYT LPLLWDKLEV SADFRRRAES VKEFNRCNIW RKRGISRVPI IHLVIHRPTP
GKVSILNDGS VAVEVAGIEV GQGLWTKVQQ MVAYGLGMIK CEGSDDLLER IRLLQTDTLS
MSQSSYTAGS TTSENCCEAV RLCCGILVER LRPTMNQILE NARSVTWDML IQQANAQSVD
LSARTFYKPE SSSAEYLNYG VGASEVEVDL VTGRTEIIRS DIIYDCGKSL NPAVDLGQIE
GAFVQGIGFF MYEEYTTNEN GLVNEEGTWD YKIPTIDTIP KQFNVQILNS GHHKNRVLSS
KASGEPPLLV AASVHCATRS AIREARKQYL SWNCIDDDHR ERCDLGFELP VPATMPVVKQ
LCGLESIEKY LEWKTYP


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