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UniProtKB/Swiss-Prot entry Q7XH05

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDO1_ORYSJ
Primary accession number Q7XH05
Secondary accession numbers Q0IZ18 Q8W2P4
Integrated into Swiss-Prot on July 25, 2006
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 37)
Name and origin of the protein
Protein name Probable aldehyde oxidase 1
Synonyms AO-1
EC 1.2.3.1
Gene name
OrderedLocusNames: Os10g0138100, LOC_Os10g04860
ORFNames: OSJNAa0087H07.7
From
Oryza sativa subsp. japonica (Rice) [TaxID: 39947] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Ehrhartoideae; Oryzeae; Oryza.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
DOI=10.1126/science.1083523; PubMed=12791992 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"In-depth view of structure, activity, and evolution of rice chromosome 10.";
Science 300:1566-1569(2003).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Nipponbare;
DOI=10.1126/science.1081288; PubMed=12869764 [NCBI, ExPASy, EBI, Israel, Japan]
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice.";
Science 301:376-379(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AC099733; AAL70116.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP008216; BAF26047.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DP000086; AAP52052.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK121557; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
RefSeq NP_001064133.1; -.
UniGene Os.8217
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase Q7XH05.
Organism-specific databases
Gramene Q7XH05; -.
Ontologies
GO
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004031; Molecular function: aldehyde oxidase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030151; Molecular function: molybdenum ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009688; Biological process: abscisic acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009851; Biological process: auxin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
G3DSA:3.10.20.30; Ferredoxin_fold; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000127; Xanthine_DH; 1.
ProDom PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q7XH05.
ProtoNet Q7XH05.
Genome annotation databases
GeneID 4348072; -.
KEGG osa:4348072; -.
NMPDR fig|39947.1.peg.11312; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1358  1358     Probable aldehyde oxidase 1. PRO_0000247645
DOMAIN   4     91  88     2Fe-2S ferredoxin-type. 
DOMAIN   236    418  183     FAD-binding PCMH-type. 
METAL   43     43        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   48     48        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   51     51        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   73     73        Iron-sulfur (2Fe-2S) (By similarity). 
CONFLICT   221    221        F -> L (in Ref. 2; AK121557). 
CONFLICT   610    610        D -> V (in Ref. 2; AK121557). 
CONFLICT   660    660        E -> G (in Ref. 2; AK121557). 
CONFLICT   1296   1296        H -> R (in Ref. 2; AK121557). 
Sequence information
Length: 1358 AA [This is the length of the unprocessed precursor] Molecular weight: 145453 Da [This is the MW of the unprocessed precursor] CRC64: 75B3A692C75D537D [This is a checksum on the sequence] 
        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
Q7XH05 in FASTA format

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