ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9S850


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SUOX_ARATH
Primary accession number Q9S850
Secondary accession number Q9SNW2
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 58)
Name and origin of the protein
Protein name Sulfite oxidase
Synonyms EC 1.8.3.1
Moco-containing protein AtMCP
At-SO
AtSOX
Gene name
Name: SOX
Synonyms: MCP
OrderedLocusNames: At3g01910
ORFNames: F28J7.38, F1C9.31
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
DOI=10.1074/jbc.M108078200; PubMed=11598126 [NCBI, ExPASy, EBI, Israel, Japan]
Eilers T., Schwarz G., Brinkmann H., Witt C., Richter T., Nieder J., Koch B., Hille R., Haensch R., Mendel R.R.;
"Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. A new player in plant sulfur metabolism.";
J. Biol. Chem. 276:46989-46994(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
DOI=10.1093/jxb/erf042; PubMed=12147736 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura T., Meyer C., Sano H.;
"Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulphite oxidase family.";
J. Exp. Bot. 53:1833-1836(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MOLYBDENUM-PTERIN, AND SUBUNIT.
DOI=10.1016/j.str.2003.09.001; PubMed=14527393 [NCBI, ExPASy, EBI, Israel, Japan]
Schrader N., Fischer K., Theis K., Mendel R.R., Schwarz G., Kisker C.;
"The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals.";
Structure 11:1251-1263(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
AF200972; AAF13276.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB071965; BAC10904.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010797; AAF03458.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC011664; AAF14844.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360247; AAK25957.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY133863; AAM91797.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_186840.1; -.
UniGene At.24506
3D structure databases
PDB
1OGP; X-ray; 2.60 A; A/B/C/D/E/F=1-393.[ExPASy / RCSB / EBI]
PDBsum 1OGP; -.
ModBase Q9S850.
Organism-specific databases
GeneFarm 4907; -.
TAIR At3g01910; -.
Gene expression databases
ArrayExpress Q9S850; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.
Pfam PF03404; Mo-co_dimer; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.
PRINTS PR00407; EUMOPTERIN.
PROSITE PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
BLOCKS Q9S850.
Proteomic databases
ProMEX Q9S850; -.
Genome annotation databases
GeneID 820118; -.
GenomeReviews BA000014_GR; AT3G01910.
NMPDR fig|3702.1.peg.12123; -.
Other
ProtoNet Q9S850.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Complete proteome; Metal-binding; Molybdenum; Oxidoreductase; Peroxisome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   393  393     Sulfite oxidase. PRO_0000166077
REGION   49    53  5     Molybdenum-pterin-binding. 
REGION   159   161  3     Molybdenum-pterin-binding. 
REGION   207   220  14     Molybdenum-pterin-binding. 
MOTIF   391   393  3     Microbody targeting signal (Potential). 
METAL   98    98        Molybdenum-pterin. 
CONFLICT   206   206        L -> S (in Ref. 1; AAF13276). 
CONFLICT   251   251        D -> H (in Ref. 1; AAF13276). 
STRAND   8    10  3      
STRAND   21    24  4      
TURN   25    28  4      
STRAND   29    31  3      
HELIX   34    37  4      
HELIX   45    47  3      
STRAND   58    60  3      
STRAND   66    75  10      
STRAND   78    80  3      
HELIX   81    85  5      
STRAND   89    97  9      
TURN   99   102  4      
HELIX   103   109  7      
STRAND   122   131  10      
HELIX   132   137  6      
TURN   138   140  3      
STRAND   154   160  7      
HELIX   164   166  3      
STRAND   172   176  5      
HELIX   177   181  5      
HELIX   183   185  3      
STRAND   188   193  6      
TURN   200   205  6      
STRAND   207   209  3      
HELIX   215   217  3      
STRAND   221   230  10      
HELIX   235   238  4      
STRAND   239   241  3      
TURN   250   252  3      
HELIX   255   257  3      
STRAND   267   270  4      
STRAND   275   279  5      
STRAND   281   291  11      
STRAND   298   306  9      
STRAND   315   322  8      
STRAND   326   328  3      
STRAND   337   347  11      
STRAND   349   357  9      
HELIX   367   370  4      
STRAND   382   388  7      
Sequence information
Length: 393 AA [This is the length of the unprocessed precursor] Molecular weight: 43329 Da [This is the MW of the unprocessed precursor] CRC64: 00B4AC49E92C5DD2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPGIRGPSEY SQEPPRHPSL KVNAKEPFNA EPPRSALVSS YVTPVDLFYK RNHGPIPIVD 

        70         80         90        100        110        120 
HLQSYSVTLT GLIQNPRKLF IKDIRSLPKY NVTATLQCAG NRRTAMSKVR NVRGVGWDVS 

       130        140        150        160        170        180 
AIGNAVWGGA KLADVLELVG IPKLTASTNL GARHVEFVSV DRCKEENGGP YKASITLSQA 

       190        200        210        220        230        240 
TNPEADVLLA YEMNGETLNR DHGFPLRVVV PGVIGARSVK WLDSINVIAE ESQGFFMQKD 

       250        260        270        280        290        300 
YKMFPPSVNW DNINWSSRRP QMDFPVQSAI CSVEDVQMVK PGKVSIKGYA VSGGGRGIER 

       310        320        330        340        350        360 
VDISLDGGKN WVEASRTQEP GKQYISEHSS SDKWAWVLFE ATIDVSQTTE VIAKAVDSAA 

       370        380        390 
NVQPENVESV WNLRGVLNTS WHRVLLRLGH SNL 

Q9S850 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!