Reviewed, UniProtKB/Swiss-Prot Q7XH05 (ALDO1_ORYSJ)

Names and origin

Protein names

Recommended name:
    Probable aldehyde oxidase 1
      Short name=AO-1
    EC=1.2.3.1

Gene names

Ordered Locus Names:	Os10g0138100, LOC_Os10g04860
ORF Names:	OSJNAa0087H07.7

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	1358 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 + H(2)O + O(2) = a carboxylic acid + H(2)O(2).
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 BAF26047.1 differs from that shown. Reason: Erroneous gene model prediction.

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: InterPro 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 – 1358	1358	Probable aldehyde oxidase 1		PRO_0000247645
Regions
	Domain	4 – 91	88	2Fe-2S ferredoxin-type
	Domain	236 – 418	183	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
	Metal binding	73	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Sequence conflict	221	1	F → L in AK121557. Ref.2
	Sequence conflict	610	1	D → V in AK121557. Ref.2
	Sequence conflict	660	1	E → G in AK121557. Ref.2
	Sequence conflict	1296	1	H → R in AK121557. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q7XH05-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 75B3A692C75D537D	FASTA	1,358	145,453
	10 20 30 40 50 60 MGEAAAVVAV NGERYEAVGV DPSMTLLEFL RTRTPFRGPK LGCGEGGCGA CAVVVSKYDA 70 80 90 100 110 120 AADEVTSFSA SSCLTLLGSL HHCAVTTSEG IGNSRDGFHP VQRRLAGFHA SQCGFCTPGM 130 140 150 160 170 180 CVSIFSALAN ADRAASAAPP PPPTPPGFSR LTAADAERAV SGNLCRCTGY RPILDACKSF 190 200 210 220 230 240 AADVDLEDLG LNSFWKKGER ADITKLPAYS CTADVATFPE FLKSEIRSSG GAPAVAVTGD 250 260 270 280 290 300 GCWFHPRSIE EFHRLFECNL FDEMSVKIVA SNTGSGVYKD QDLHDKYINI SQIPELSAIN 310 320 330 340 350 360 RSSNGIEIGA AVSISKAIEI LRSDGGDAVV FRKIAYHLGK VASPFVRNTA TIGGNIIMAQ 370 380 390 400 410 420 RMSFPSDIAT VLLAAGSTVT IQQVASKRMC LTLEEFLKQP PCDSRTLLIS ISIPDWCSYD 430 440 450 460 470 480 GITFETFRAA PRPFGNAVSY VNSAFLARSS LDAASGSHLI EDVRLAFGAF GSEHAIRASK 490 500 510 520 530 540 VEEFLKGKLV SASVILEAVR LLKGVVSPAE GTTHPEYRVS LAVSYLFRFL SSLANGLDDK 550 560 570 580 590 600 PENANNVPNG SCTTNGTTNG SAESTVDSFD LPIKSRQEMV FSDEYKPVGK PIKKVGAELQ 610 620 630 640 650 660 ASGEAVYVDD IPAPKDCLYG AFIYSTHPHA HIKGVNFRSS LASQKVITVI TAKDIPTGGE 670 680 690 700 710 720 NVGSCFPMLG DEALFADPVA EFAGQNIGVV IAETQKYAYM AARQAVIEYN TENLQPPILT 730 740 750 760 770 780 VEDAVQHNSY FQVPPFLQPK PIGDFNQAMS EADHKIIDGE VKLGSQYYFY METQTALAFP 790 800 810 820 830 840 DEDNCITVYC SAQMPEVTQD IVARCLGVPF HNVRIITRRV GGGFGGKAMK ATHVATACAV 850 860 870 880 890 900 AAFKLRRPVR MYLDRKTDMI MAGGRHPMKA KYSVGFKSDG KITALHLDLK INAGISPEFS 910 920 930 940 950 960 PAIPYAIVGA LKKYSWGALA FDIKVCKTNV SSKSAMRAPG DAQGSFIAEA IVEHVASTLS 970 980 990 1000 1010 1020 VATNTIRRKN LHDLESLKVF FGDSAAGEAS TSSYSLVIIF DRLASTPEYQ RRAAMVEQFN 1030 1040 1050 1060 1070 1080 GSSRWKKRGI SCVPITYSVT LRPSPGKVSI LNDGSIAVEV GGVEIGQGLW TKVKQMTAFA 1090 1100 1110 1120 1130 1140 LGQLCDDGGE GLLDNVRVIQ ADTLSMIQGG WTAGSTTSET SCEAVRKSCA ALVERLKPIK 1150 1160 1170 1180 1190 1200 EKAGTLPWKS FIAQASMASV KLTEHAYWTP DPTFTSYMNY GAATSEVEVD VLTGATTILR 1210 1220 1230 1240 1250 1260 SDLVYDCGQS LNPAVDLGQV EGAFVQGVGF FTNEEYATNA DGLVIHDGTW TYKIPTVDTI 1270 1280 1290 1300 1310 1320 PKQFNVELIN TARHHSRVLS SKASGEPPLL LASSVHCAMR EAIRAARREF AAVGGGTGGS 1330 1340 1350 DQVTSFQMDV PATMPAVKEL CGLDVVERYL ESFSATTA

References

[1]

"In-depth view of structure, activity, and evolution of rice chromosome 10." Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A. Science 300:1566-1569(2003) [PubMed: 12791992] [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	AC099733 Genomic DNA. Translation: AAL70116.1. AP008216 Genomic DNA. Translation: BAF26047.1. Sequence problems. DP000086 Genomic DNA. Translation: AAP52052.1. AK121557 mRNA. No translation available.
RefSeq	NP_001064133.1.
UniGene	Os.8217
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Genome annotation databases
GeneID	4348072.
KEGG	osa:4348072.
NMPDR	fig|39947.1.peg.11312.
Organism-specific databases
Gramene	Q7XH05.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DHase_a/b. IPR016208. Ald_Oxase/xanthine_DHase. IPR008274. AldOxase/xan_DHase_Mopterin-bd. IPR012675. b-grasp_ferredoxin-like. IPR005107. CO_DHase_flav_C. IPR016169. CO_DHase_flavot_FAD-bd_sub2. IPR001041. Ferredoxin. IPR002346. Mopterin_DHase_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. 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.
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

ALDO1_ORYSJ

Accession

Primary (citable) accession number: Q7XH05
Secondary accession number(s): Q0IZ18, Q8W2P4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)