Q7G191 (ALDO4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aldehyde oxidase 4
Short name=AO-4
Short name=AtAO-4
Short name=AtAO2
EC=1.2.3.1

Gene names

Name:	AAO4
Synonyms:	AO2
Ordered Locus Names:	At1g04580
ORF Names:	T1G11.17

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1337 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	An aldehyde + H2O + O2 = a carboxylic acid + H2O2.
Cofactor	Binds 2 2Fe-2S clusters By similarity. FAD By similarity. Molybdopterin By similarity.
Subunit structure	Aldehyde oxidases (AO) are homo- and heterodimers of AO subunits By similarity.
Tissue specificity	Transcripts expressed at high levels in developing siliques and at low levels in dry seeds. Ref.5 Ref.6
Induction	Induced by dehydration, in rosette but not in roots. Ref.5
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. Ref.6
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.
Sequence caution	The sequence AAB80640.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glucosinolate metabolic process Inferred from mutant phenotype. Source: TAIR
Cellular component	cytosol Traceable author statement. Source: TAIR
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aryl-aldehyde oxidase activity Inferred from direct assay. Source: TAIR benzaldehyde dehydrogenase (NAD+) activity Inferred from direct assay. Source: TAIR electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on CH-OH group of donors Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1337	1337	Aldehyde oxidase 4		PRO_0000166112
Regions
	Domain	4 – 91	88	2Fe-2S ferredoxin-type
	Domain	225 – 409	185	FAD-binding PCMH-type
Sites
	Metal binding	43	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	51	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Sequence conflict	1257	1	V → I in AAC39511. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q7G191 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: 8DCF487FA3F7D6B8	FASTA	1,337	147,304
	10 20 30 40 50 60 MAGDDLVFAV NGEKFEVLSV NPSTTLLEFL RSNTCFKSVK LSCGEGGCGA CIVILSKYDP 70 80 90 100 110 120 VLDQVEEYSI NSCLTLLCSL NGCSITTSDG LGNTEKGFHP IHKRFAGFHA SQCGFCTPGM 130 140 150 160 170 180 CISLYSALSK AHNSQSSPDY LTALAAEKSI AGNLCRCTGY RPIADACKSF ASDVDIEDLG 190 200 210 220 230 240 FNSFWRKGES REEMLKKLPP YNPEKDLITF PDFLKEKIKC QHNVLDQTRY HWSTPGSVAE 250 260 270 280 290 300 LQEILATTNP GKDRGLIKLV VGNTGTGYYK EEKQYGRYID ISHIPEMSMI KKDDREIEIG 310 320 330 340 350 360 AVVTISKVID ALMEENTSAY VFKKIGVHME KVANHFIRNS GSIGGNLVMA QSKSFPSDIT 370 380 390 400 410 420 TLLLAADASV HMINAGRHEK LRMGEYLVSP PILDTKTVLL KVHIPRWIAS STTGLLFETY 430 440 450 460 470 480 RAALRPIGSA LPYINAAFLA VVSHDASSSG IIVDKCRLAF GSYGGYHSIR AREVEDFLTG 490 500 510 520 530 540 KILSHSVLYE AVRLLKGIIV PSIDTSYSEY KKSLAVGFLF DFLYPLIESG SWDSEGKHID 550 560 570 580 590 600 GHIDPTICLP LLSSAQQVFE SKEYHPVGEA IIKFGAEMQA SGEAVYVDDI PSLPHCLHGA 610 620 630 640 650 660 FIYSTKPLAW IKSVGFSGNV TPIGVLAVIT FKDIPEVGQN IGYITMFGTG LLFADEVTIS 670 680 690 700 710 720 AGQIIALVVA DTQKHADMAA HLAVVEYDSR NIGTPVLSVE DAVKRSSLFE VPPEYQPEPV 730 740 750 760 770 780 GDISKGMAEA DRKIRSVELR LGSQYFFYME TQTALALPDE DNCLVVYSST QAPEFTQTVI 790 800 810 820 830 840 ATCLGIPEHN VRVITRRVGG GFGGKAIKSM PVATACALAA KKMQRPVRIY VNRKTDMIMA 850 860 870 880 890 900 GGRHPLKITY SVGFRSDGKL TALDLNLFID AGSDVDVSLV MPQNIMNSLR KYDWGALSFD 910 920 930 940 950 960 IKVCKTNLPS RTSLRAPGEV QGSYIAESII ENVASSLKMD VDVVRRINLH TYESLRKFYK 970 980 990 1000 1010 1020 QAAGEPDEYT LPLLWDKLEV SADFRRRAES VKEFNRCNIW RKRGISRVPI IHLVIHRPTP 1030 1040 1050 1060 1070 1080 GKVSILNDGS VAVEVAGIEV GQGLWTKVQQ MVAYGLGMIK CEGSDDLLER IRLLQTDTLS 1090 1100 1110 1120 1130 1140 MSQSSYTAGS TTSENCCEAV RLCCGILVER LRPTMNQILE NARSVTWDML IQQANAQSVD 1150 1160 1170 1180 1190 1200 LSARTFYKPE SSSAEYLNYG VGASEVEVDL VTGRTEIIRS DIIYDCGKSL NPAVDLGQIE 1210 1220 1230 1240 1250 1260 GAFVQGIGFF MYEEYTTNEN GLVNEEGTWD YKIPTIDTIP KQFNVQILNS GHHKNRVLSS 1270 1280 1290 1300 1310 1320 KASGEPPLLV AASVHCATRS AIREARKQYL SWNCIDDDHR ERCDLGFELP VPATMPVVKQ 1330 LCGLESIEKY LEWKTYP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis aldehyde oxidase cDNA." Seo M., Koshiba T. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. Tissue: Rosette leaf.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Biochemical and genetic characterization of three molybdenum cofactor hydroxylases in Arabidopsis thaliana." Hoff T., Frandsen G.I., Rocher A., Mundy J. Biochim. Biophys. Acta 1398:397-402(1998) [PubMed: 9655945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1337. Strain: cv. Wassilewskija. Tissue: Root.
[5]	"Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana." Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y., Koshiba T. Plant J. 23:481-488(2000) [PubMed: 10972874] [Abstract] Cited for: INDUCTION, TISSUE SPECIFICITY.
[6]	"Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds." Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T. Plant Cell Physiol. 45:1694-1703(2004) [PubMed: 15574845] [Abstract] Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB037271 mRNA. Translation: BAA90299.1. AC002376 Genomic DNA. Translation: AAB80640.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE27717.1. AF039897 mRNA. Translation: AAC39511.1.
IPI	IPI00531258.
PIR	D86178. T52051.
RefSeq	NP_563711.1. NM_100337.2.
UniGene	At.465.
3D structure databases
ProteinModelPortal	Q7G191.
SMR	Q7G191. Positions 3-172, 562-984.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7G191.
Proteomic databases
PRIDE	Q7G191.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G04580.1; AT1G04580.1; AT1G04580.
GeneID	839488.
GenomeReviews	Gene locus AT1G04580 in contig CT485782_GR.
KEGG	ath:AT1G04580.
NMPDR	fig|3702.1.peg.605.
Organism-specific databases
GeneFarm	4895. 470.
TAIR	At1g04580.
Phylogenomic databases
eggNOG	KOG0430.
GeneTree	EPGT00050000011134.
HOGENOM	HBG746468.
InParanoid	Q7G191.
OMA	PNAICTG.
PhylomeDB	Q7G191.
ProtClustDB	PLN00192.
Gene expression databases
Genevestigator	Q7G191.
GermOnline	AT1G04580. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002888. 2Fe-2S-bd. 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_ferredoxin-type. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR001041. Ferredoxin. IPR002346. Mopterin_DH_FAD-bd. [Graphical view]
Gene3D	G3DSA:1.10.150.120. 2Fe-2S-bd. 1 hit. G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 4 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF01315. 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]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
SMART	SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF47741. 2Fe-2S_bind. 1 hit. SSF56003. Ald_xan_DH_mo_bd. 1 hit. SSF54665. Aldxan_dh_hamm. 1 hit. SSF55447. CO_deh_flav_C. 1 hit. SSF56176. FAD-binding_2. 1 hit. SSF54292. Ferredoxin. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALDO4_ARATH

Accession

Primary (citable) accession number: Q7G191
Secondary accession number(s): O23027, O49157, Q7GB29

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program