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Database: UniProt
Entry: Q7G191
LinkDB: Q7G191
Original site: Q7G191 
ID   ALDO4_ARATH             Reviewed;        1337 AA.
AC   Q7G191; O23027; O49157; Q7GB29;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   19-FEB-2014, entry version 87.
DE   RecName: Full=Benzaldehyde dehydrogenase (NAD(+));
DE            EC=1.2.1.28;
DE   AltName: Full=Aldehyde oxidase 4;
DE            Short=AO-4;
DE            Short=AtAO-4;
DE            Short=AtAO2;
DE   AltName: Full=Indole-3-acetaldehyde oxidase;
DE            Short=IAA oxidase;
DE            EC=1.2.3.7;
GN   Name=AAO4; Synonyms=AO2; OrderedLocusNames=At1g04580;
GN   ORFNames=T1G11.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RA   Seo M., Koshiba T.;
RT   "Arabidopsis aldehyde oxidase cDNA.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1337.
RC   STRAIN=cv. Wassilewskija; TISSUE=Root;
RX   PubMed=9655945; DOI=10.1016/S0167-4781(98)00085-2;
RA   Hoff T., Frandsen G.I., Rocher A., Mundy J.;
RT   "Biochemical and genetic characterization of three molybdenum cofactor
RT   hydroxylases in Arabidopsis thaliana.";
RL   Biochim. Biophys. Acta 1398:397-402(1998).
RN   [5]
RP   INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10972874; DOI=10.1046/j.1365-313x.2000.00812.x;
RA   Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y.,
RA   Koshiba T.;
RT   "Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
RL   Plant J. 23:481-488(2000).
RN   [6]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15574845; DOI=10.1093/pcp/pch198;
RA   Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T.;
RT   "Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene
RT   family revealed a major role of AAO3 in ABA biosynthesis in seeds.";
RL   Plant Cell Physiol. 45:1694-1703(2004).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=19297586; DOI=10.1104/pp.109.135848;
RA   Ibdah M., Chen Y.-T., Wilkerson C.G., Pichersky E.;
RT   "An aldehyde oxidase in developing seeds of Arabidopsis converts
RT   benzaldehyde to benzoic Acid.";
RL   Plant Physiol. 150:416-423(2009).
CC   -!- FUNCTION: Involved in the accumulation of benzoic acid (BA) in
CC       siliques.
CC   -!- CATALYTIC ACTIVITY: Benzaldehyde + NAD(+) + H(2)O = benzoate +
CC       NADH.
CC   -!- CATALYTIC ACTIVITY: (Indol-3-yl)acetaldehyde + H(2)O + O(2) =
CC       (indol-3-yl)acetate + H(2)O(2).
CC   -!- COFACTOR: Binds 2 2Fe-2S clusters (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- COFACTOR: Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per
CC       subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by Cu(2+).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=23 uM for benzoic acid (BA) (at pH7, in the presence of
CC         NAD(+));
CC         KM=58.1 uM for NAD(+) (at pH7, in the presence of benzoic acid
CC         (BA));
CC         KM=2.07 uM for indole-3-acetaldehyde (at pH7);
CC         KM=103.9 uM for cinnamylaldehyde (at pH7);
CC         Vmax=1.2 nmol/sec/mg enzyme with benzoic acid (BA) as substrate
CC         (at pH7, in the presence of NAD(+));
CC         Vmax=3.2 nmol/sec/mg enzyme with NAD(+) as substrate (at pH7, in
CC         the presence of benzoic acid (BA));
CC         Vmax=1.5 nmol/sec/mg enzyme with indole-3-acetaldehyde as
CC         substrate (at pH7);
CC         Vmax=5.5 nmol/sec/mg enzyme with cinnamylaldehyde as substrate
CC         (at pH7);
CC         Note=Kcat is 95.2 sec(-1) with benzoic acid (BA) as substrate,
CC         253.9 sec(-1) with NAD(+) as substrate, 1.904 sec(-1) with
CC         indole-3-acetaldehyde as substrate, and 436.5 sec(-1) with
CC         cinnamylaldehyde as substrate (at pH 7, PubMed:19297586);
CC       pH dependence:
CC         Optimum pH is 7;
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius;
CC   -!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of
CC       AO subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Transcripts expressed at high levels in
CC       developing siliques and at low levels in dry seeds.
CC   -!- INDUCTION: Induced by dehydration, in rosette but not in roots.
CC   -!- DISRUPTION PHENOTYPE: Plants have normal abscisic acid (ABA)
CC       levels, normal germination and are not affected in abscisic
CC       aldehyde oxidase activity in siliques, dry seeds and leaves.
CC       Reduced levels of benzoic acid (BA), 3-
CC       benzoyloxypropylglucosinolate and 4-benzoyloxybutylglucosinolate
CC       in seeds.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB80640.1; Type=Erroneous gene model prediction;
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DR   EMBL; AB037271; BAA90299.1; -; mRNA.
DR   EMBL; AC002376; AAB80640.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27717.1; -; Genomic_DNA.
DR   EMBL; AF039897; AAC39511.1; -; mRNA.
DR   PIR; D86178; D86178.
DR   PIR; T52051; T52051.
DR   RefSeq; NP_563711.1; NM_100337.2.
DR   UniGene; At.465; -.
DR   ProteinModelPortal; Q7G191; -.
DR   SMR; Q7G191; 3-171, 200-405, 567-1322.
DR   PaxDb; Q7G191; -.
DR   PRIDE; Q7G191; -.
DR   EnsemblPlants; AT1G04580.1; AT1G04580.1; AT1G04580.
DR   GeneID; 839488; -.
DR   KEGG; ath:AT1G04580; -.
DR   GeneFarm; 4895; 470.
DR   TAIR; AT1G04580; -.
DR   eggNOG; COG4630; -.
DR   HOGENOM; HOG000191197; -.
DR   InParanoid; Q7G191; -.
DR   OMA; EENTSAY; -.
DR   PhylomeDB; Q7G191; -.
DR   ProtClustDB; PLN00192; -.
DR   Genevestigator; Q7G191; -.
DR   GO; GO:0005829; C:cytosol; TAS:TAIR.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018488; F:aryl-aldehyde oxidase activity; IDA:TAIR.
DR   GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IDA:TAIR.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR   Gene3D; 1.10.150.120; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.365.10; -; 6.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.90.1170.50; -; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR   InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR   InterPro; IPR012675; Beta-grasp_dom.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   PIRSF; PIRSF000127; Xanthine_DH; 1.
DR   SMART; SM01008; Ald_Xan_dh_C; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF47741; SSF47741; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF54665; SSF54665; 1.
DR   SUPFAM; SSF55447; SSF55447; 1.
DR   SUPFAM; SSF56003; SSF56003; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1   1337       Benzaldehyde dehydrogenase (NAD(+)).
FT                                /FTId=PRO_0000166112.
FT   DOMAIN        4     91       2Fe-2S ferredoxin-type.
FT   DOMAIN      225    409       FAD-binding PCMH-type.
FT   METAL        43     43       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        48     48       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        51     51       Iron-sulfur (2Fe-2S) (By similarity).
FT   CONFLICT   1257   1257       V -> I (in Ref. 4; AAC39511).
SQ   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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