Reviewed, UniProtKB/Swiss-Prot Q852M1 (ALDO2_ORYSJ)

Names and origin

Protein names

Recommended name:
    Probable aldehyde oxidase 2
      Short name=AO-2
    EC=1.2.3.1

Gene names

Ordered Locus Names:	Os03g0790900, LOC_Os03g57690
ORF Names:	OSJNBa0087O09.20

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	1355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 AK100342 differs from that shown. Reason: Frameshift at position 683.

Ontologies

Keywords
Biological process	Abscisic acid biosynthesis Auxin biosynthesis
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	abscisic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW auxin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro aldehyde oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1355	1355	Probable aldehyde oxidase 2		PRO_0000247646
Regions
	Domain	9 – 96	88	2Fe-2S ferredoxin-type
	Domain	244 – 422	179	FAD-binding PCMH-type
Sites
	Metal binding	48	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	53	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	56	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	78	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q852M1-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: ECBDA2871B95BFC7	FASTA	1,355	145,064
	10 20 30 40 50 60 MGSEAAAARP VVVTVNGERY EAVGVDPSTT LLEFLRTRTP VRGPKLGCGE GGCGACVVVV 70 80 90 100 110 120 SKYDAVADEV TEFSASSCLT LLGSLHHCAV TTSEGIGNSR DGFHAVQRRL SGFHASQCGF 130 140 150 160 170 180 CTPGMCMSIY SALAKADRCS SRPSPPPGFS KLTAAEAEKA VSGNLCRCTG YRPIVDACKS 190 200 210 220 230 240 FAADVDLEDL GLNAFWKKGA DDERADVGKL PAYSGGAAVC TFPEFLKSEI RSSMGQANGG 250 260 270 280 290 300 APAVAVTGDG WFHPKSVEEF HRLFDSNLFD ERSVKIVASN TGSGVYKDQD LHDKYINISQ 310 320 330 340 350 360 ILELSAINRS SKGVEIGAVV SISKAIEILS DGGAVFRKIA DHLSKVASSF VQNTATIGGN 370 380 390 400 410 420 IIMAQRLSFP SDIATVLLAA GSTVTIQVAA KRMCITLEEF LKQPPCDSRT LLVSISIPDW 430 440 450 460 470 480 GSDDGITFES FRAAPRPLGN AVSYVNSAFL ARSSVDGSSG SHLIEDVCLA FGAFGAEHAI 490 500 510 520 530 540 RAREVEEFLK GKLVSAPVIL EAVRLLKGVV SPAEGTTHPE YRVSLAVSYL FRFLTSLANG 550 560 570 580 590 600 LDEPENANVP NGSCTNGTAN GSANSSPEKH SNVDSSDLPI KSRQEMVFSD EYKPVGKPIE 610 620 630 640 650 660 KTGAELQASG EAVYVDDIPA PKDCLYGAFI YSTHPHAHIK DINFRSSLAS QKVITVITAK 670 680 690 700 710 720 DIPTGGENIG SCFPMLGDEA LFVHPVSEFA GQNIGVVIAE TQKYAYMAAK QAVIEYSTEN 730 740 750 760 770 780 LQPPILTIED AVQHNSYFPV PPFLAPTPIG DFNQAMSEAD HKIIDGEVKL ESQYYFYMET 790 800 810 820 830 840 QTALAIPDED NCITLYVSAQ LPEITQNTVA RCLGIPYHNV RIITRRVGGG FGGKAMKAIH 850 860 870 880 890 900 VAAACAVAAF KLRRPVRMYL DRKTDMIMAG GRHPMKVKYS VGFKSDGKIT GLHFDLGMNG 910 920 930 940 950 960 GISPDCSPVL PVAIVGALKK YNWGALSFDI KVCKTNVSSK SAMRAPGDAQ GSFIAEAIVE 970 980 990 1000 1010 1020 HIASTLSVDT NAIRRKNLHD FESLKVFYGN SAGDPSTYSL VTIFDKLASS PEYQQRAAMV 1030 1040 1050 1060 1070 1080 EHFNAGNRWK KRGISCVPIT YDVRLRPTPG KVSIMNDGSI AVEVGGVEIG QGLWTKVKQM 1090 1100 1110 1120 1130 1140 TAFALGQLCD DGGEGLIDKV RVIQADTLSM IQGGFTGGST TSETSCEAVR KSCAALVERL 1150 1160 1170 1180 1190 1200 KPIKEKAGTP PWKSLIAQAS MASVKLTEHA YWTPDPTFTS YLNYGAAISE VEVDVLTGET 1210 1220 1230 1240 1250 1260 TILRSDLVYD CGQSLNPAVD LGQVEGAFVQ GIGFFTNEEY TTNSDGLVIN DGTWTYKIPT 1270 1280 1290 1300 1310 1320 VDTIPKQFNV ELINSARDHK RVLSSKASGE PPLLLASSVH CAMREAIRAA RKEFAGAGGS 1330 1340 1350 PLTFQMDVPA TMPIVKELCG LDVVERYLES FAAKA

References

[1]

"Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species." The rice chromosome 3 sequencing consortium Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S. , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S. Genome Res. 15:1284-1291(2005) [PubMed: 16109971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.

[2]

"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed: 12869764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC087096 Genomic DNA. Translation: AAO24920.1. AK100342 mRNA. No translation available.
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Organism-specific databases
Gramene	Q852M1.
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. 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:3.30.365.10. Ald_xan_DH_mo_bd. 2 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.
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.
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALDO2_ORYSJ

Accession

Primary (citable) accession number: Q852M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	June 1, 2003
Last modified:	July 7, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)