Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Benzaldehyde dehydrogenase (NAD(+))

Gene

AAO4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the accumulation of benzoic acid (BA) in siliques.1 Publication

Catalytic activityi

Benzaldehyde + NAD+ + H2O = benzoate + NADH.1 Publication
(Indol-3-yl)acetaldehyde + H2O + O2 = (indol-3-yl)acetate + H2O2.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Enzyme regulationi

Inhibited by Cu2+.1 Publication

Kineticsi

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).

  1. KM=23 µM for benzoic acid (BA) (at pH7, in the presence of NAD+)1 Publication
  2. KM=58.1 µM for NAD+ (at pH7, in the presence of benzoic acid (BA))1 Publication
  3. KM=2.07 µM for indole-3-acetaldehyde (at pH7)1 Publication
  4. KM=103.9 µM for cinnamylaldehyde (at pH7)1 Publication
  1. Vmax=1.2 nmol/sec/mg enzyme with benzoic acid (BA) as substrate (at pH7, in the presence of NAD+)1 Publication
  2. Vmax=3.2 nmol/sec/mg enzyme with NAD+ as substrate (at pH7, in the presence of benzoic acid (BA))1 Publication
  3. Vmax=1.5 nmol/sec/mg enzyme with indole-3-acetaldehyde as substrate (at pH7)1 Publication
  4. Vmax=5.5 nmol/sec/mg enzyme with cinnamylaldehyde as substrate (at pH7)1 Publication

pH dependencei

Optimum pH is 7.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi48 – 481Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi51 – 511Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • abscisic acid biosynthetic process Source: UniProtKB-KW
  • auxin biosynthetic process Source: UniProtKB-KW
  • glucosinolate metabolic process Source: TAIR
  • xanthine catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Abscisic acid biosynthesis, Auxin biosynthesis

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BRENDAi1.2.3.1. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Benzaldehyde dehydrogenase (NAD(+)) (EC:1.2.1.28)
Alternative name(s):
Aldehyde oxidase 4
Short name:
AO-4
Short name:
AtAO-4
Short name:
AtAO2
Indole-3-acetaldehyde oxidase (EC:1.2.3.7)
Short name:
IAA oxidase
Gene namesi
Name:AAO4
Synonyms:AO2
Ordered Locus Names:At1g04580
ORF Names:T1G11.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G04580.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13371337Benzaldehyde dehydrogenase (NAD(+))PRO_0000166112Add
BLAST

Proteomic databases

PaxDbiQ7G191.
PRIDEiQ7G191.

PTM databases

iPTMnetiQ7G191.

Expressioni

Tissue specificityi

Transcripts expressed at high levels in developing siliques and at low levels in dry seeds.2 Publications

Inductioni

Induced by dehydration, in rosette but not in roots.1 Publication

Gene expression databases

GenevisibleiQ7G191. AT.

Interactioni

Subunit structurei

Aldehyde oxidases (AO) are homodimers and heterodimers of AO subunits.By similarity

Protein-protein interaction databases

STRINGi3702.AT1G04580.1.

Structurei

3D structure databases

ProteinModelPortaliQ7G191.
SMRiQ7G191. Positions 3-171, 200-405, 567-1322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 91882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini225 – 409185FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
InParanoidiQ7G191.
OMAiFINDLAP.
OrthoDBiEOG093600DW.
PhylomeDBiQ7G191.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7G191-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGDDLVFAV NGEKFEVLSV NPSTTLLEFL RSNTCFKSVK LSCGEGGCGA
60 70 80 90 100
CIVILSKYDP VLDQVEEYSI NSCLTLLCSL NGCSITTSDG LGNTEKGFHP
110 120 130 140 150
IHKRFAGFHA SQCGFCTPGM CISLYSALSK AHNSQSSPDY LTALAAEKSI
160 170 180 190 200
AGNLCRCTGY RPIADACKSF ASDVDIEDLG FNSFWRKGES REEMLKKLPP
210 220 230 240 250
YNPEKDLITF PDFLKEKIKC QHNVLDQTRY HWSTPGSVAE LQEILATTNP
260 270 280 290 300
GKDRGLIKLV VGNTGTGYYK EEKQYGRYID ISHIPEMSMI KKDDREIEIG
310 320 330 340 350
AVVTISKVID ALMEENTSAY VFKKIGVHME KVANHFIRNS GSIGGNLVMA
360 370 380 390 400
QSKSFPSDIT TLLLAADASV HMINAGRHEK LRMGEYLVSP PILDTKTVLL
410 420 430 440 450
KVHIPRWIAS STTGLLFETY RAALRPIGSA LPYINAAFLA VVSHDASSSG
460 470 480 490 500
IIVDKCRLAF GSYGGYHSIR AREVEDFLTG KILSHSVLYE AVRLLKGIIV
510 520 530 540 550
PSIDTSYSEY KKSLAVGFLF DFLYPLIESG SWDSEGKHID GHIDPTICLP
560 570 580 590 600
LLSSAQQVFE SKEYHPVGEA IIKFGAEMQA SGEAVYVDDI PSLPHCLHGA
610 620 630 640 650
FIYSTKPLAW IKSVGFSGNV TPIGVLAVIT FKDIPEVGQN IGYITMFGTG
660 670 680 690 700
LLFADEVTIS AGQIIALVVA DTQKHADMAA HLAVVEYDSR NIGTPVLSVE
710 720 730 740 750
DAVKRSSLFE VPPEYQPEPV GDISKGMAEA DRKIRSVELR LGSQYFFYME
760 770 780 790 800
TQTALALPDE DNCLVVYSST QAPEFTQTVI ATCLGIPEHN VRVITRRVGG
810 820 830 840 850
GFGGKAIKSM PVATACALAA KKMQRPVRIY VNRKTDMIMA GGRHPLKITY
860 870 880 890 900
SVGFRSDGKL TALDLNLFID AGSDVDVSLV MPQNIMNSLR KYDWGALSFD
910 920 930 940 950
IKVCKTNLPS RTSLRAPGEV QGSYIAESII ENVASSLKMD VDVVRRINLH
960 970 980 990 1000
TYESLRKFYK QAAGEPDEYT LPLLWDKLEV SADFRRRAES VKEFNRCNIW
1010 1020 1030 1040 1050
RKRGISRVPI IHLVIHRPTP GKVSILNDGS VAVEVAGIEV GQGLWTKVQQ
1060 1070 1080 1090 1100
MVAYGLGMIK CEGSDDLLER IRLLQTDTLS MSQSSYTAGS TTSENCCEAV
1110 1120 1130 1140 1150
RLCCGILVER LRPTMNQILE NARSVTWDML IQQANAQSVD LSARTFYKPE
1160 1170 1180 1190 1200
SSSAEYLNYG VGASEVEVDL VTGRTEIIRS DIIYDCGKSL NPAVDLGQIE
1210 1220 1230 1240 1250
GAFVQGIGFF MYEEYTTNEN GLVNEEGTWD YKIPTIDTIP KQFNVQILNS
1260 1270 1280 1290 1300
GHHKNRVLSS KASGEPPLLV AASVHCATRS AIREARKQYL SWNCIDDDHR
1310 1320 1330
ERCDLGFELP VPATMPVVKQ LCGLESIEKY LEWKTYP
Length:1,337
Mass (Da):147,304
Last modified:April 26, 2005 - v2
Checksum:i8DCF487FA3F7D6B8
GO

Sequence cautioni

The sequence AAB80640 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1257 – 12571V → I in AAC39511 (PubMed:9655945).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037271 mRNA. Translation: BAA90299.1.
AC002376 Genomic DNA. Translation: AAB80640.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE27717.1.
AF039897 mRNA. Translation: AAC39511.1.
PIRiD86178.
T52051.
RefSeqiNP_563711.1. NM_100337.2.
UniGeneiAt.465.

Genome annotation databases

EnsemblPlantsiAT1G04580.1; AT1G04580.1; AT1G04580.
GeneIDi839488.
GrameneiAT1G04580.1; AT1G04580.1; AT1G04580.
KEGGiath:AT1G04580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037271 mRNA. Translation: BAA90299.1.
AC002376 Genomic DNA. Translation: AAB80640.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE27717.1.
AF039897 mRNA. Translation: AAC39511.1.
PIRiD86178.
T52051.
RefSeqiNP_563711.1. NM_100337.2.
UniGeneiAt.465.

3D structure databases

ProteinModelPortaliQ7G191.
SMRiQ7G191. Positions 3-171, 200-405, 567-1322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G04580.1.

PTM databases

iPTMnetiQ7G191.

Proteomic databases

PaxDbiQ7G191.
PRIDEiQ7G191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G04580.1; AT1G04580.1; AT1G04580.
GeneIDi839488.
GrameneiAT1G04580.1; AT1G04580.1; AT1G04580.
KEGGiath:AT1G04580.

Organism-specific databases

TAIRiAT1G04580.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
InParanoidiQ7G191.
OMAiFINDLAP.
OrthoDBiEOG093600DW.
PhylomeDBiQ7G191.

Enzyme and pathway databases

BRENDAi1.2.3.1. 399.

Miscellaneous databases

PROiQ7G191.

Gene expression databases

GenevisibleiQ7G191. AT.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALDO4_ARATH
AccessioniPrimary (citable) accession number: Q7G191
Secondary accession number(s): O23027, O49157, Q7GB29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: September 7, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.