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Protein

Sulfite oxidase

Gene

SOX

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably involved in sulfite oxidative detoxification.

Catalytic activityi

Sulfite + O2 + H2O = sulfate + H2O2.1 Publication

Cofactori

Mo-molybdopterin2 PublicationsNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.2 Publications

Kineticsi

  1. KM=33.8 µM for sulfite (at pH 8.0 and 25 degrees Celsius)

    Pathwayi: sulfur metabolism

    This protein is involved in the pathway sulfur metabolism, which is part of Energy metabolism.
    View all proteins of this organism that are known to be involved in the pathway sulfur metabolism and in Energy metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi98 – 981Molybdenum
    Binding sitei202 – 2021Molybdopterin
    Binding sitei207 – 2071Molybdopterin

    GO - Molecular functioni

    • molybdenum ion binding Source: InterPro
    • sulfite oxidase activity Source: TAIR

    GO - Biological processi

    • chlorophyll metabolic process Source: TAIR
    • nitrate assimilation Source: InterPro
    • response to sulfur dioxide Source: TAIR
    • sulfur compound metabolic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, Molybdenum

    Enzyme and pathway databases

    BioCyciARA:GQT-2438-MONOMER.
    ARA:GQT-301-MONOMER.
    BRENDAi1.8.3.1. 399.
    ReactomeiR-ATH-1614517. Sulfide oxidation to sulfate.
    UniPathwayiUPA00096.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfite oxidase (EC:1.8.3.1)
    Alternative name(s):
    Moco-containing protein AtMCP
    Short name:
    At-SO
    Short name:
    AtSOX
    Gene namesi
    Name:SOX
    Synonyms:MCP
    Ordered Locus Names:At3g01910
    ORF Names:F1C9.31, F28J7.38
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G01910.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrion Source: TAIR
    • peroxisome Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Sulfite oxidasePRO_0000166077Add
    BLAST

    Proteomic databases

    PaxDbiQ9S850.
    PRIDEiQ9S850.

    Expressioni

    Gene expression databases

    ExpressionAtlasiQ9S850. baseline and differential.
    GenevisibleiQ9S850. AT.

    Interactioni

    Subunit structurei

    Predominantly monomer; also homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi5452. 2 interactions.
    IntActiQ9S850. 1 interaction.
    STRINGi3702.AT3G01910.1.

    Structurei

    Secondary structure

    1
    393
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103Combined sources
    Beta strandi21 – 244Combined sources
    Turni25 – 284Combined sources
    Beta strandi29 – 313Combined sources
    Helixi34 – 374Combined sources
    Helixi45 – 473Combined sources
    Beta strandi58 – 603Combined sources
    Beta strandi66 – 7510Combined sources
    Beta strandi78 – 803Combined sources
    Helixi81 – 855Combined sources
    Beta strandi89 – 979Combined sources
    Turni99 – 1024Combined sources
    Helixi103 – 1097Combined sources
    Beta strandi122 – 13110Combined sources
    Helixi132 – 1376Combined sources
    Turni138 – 1403Combined sources
    Beta strandi154 – 1607Combined sources
    Helixi164 – 1663Combined sources
    Beta strandi172 – 1765Combined sources
    Helixi177 – 1815Combined sources
    Helixi183 – 1853Combined sources
    Beta strandi188 – 1936Combined sources
    Turni200 – 2056Combined sources
    Beta strandi207 – 2093Combined sources
    Helixi215 – 2173Combined sources
    Beta strandi221 – 23010Combined sources
    Helixi235 – 2384Combined sources
    Beta strandi239 – 2413Combined sources
    Turni250 – 2523Combined sources
    Helixi255 – 2573Combined sources
    Beta strandi267 – 2704Combined sources
    Beta strandi275 – 2795Combined sources
    Beta strandi281 – 29111Combined sources
    Beta strandi298 – 3069Combined sources
    Beta strandi315 – 3228Combined sources
    Beta strandi326 – 3283Combined sources
    Beta strandi337 – 34711Combined sources
    Beta strandi349 – 3579Combined sources
    Helixi367 – 3704Combined sources
    Beta strandi382 – 3887Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OGPX-ray2.60A/B/C/D/E/F1-393[»]
    ProteinModelPortaliQ9S850.
    SMRiQ9S850. Positions 2-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9S850.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 242233Moco domainAdd
    BLAST
    Regioni49 – 535Molybdopterin-binding
    Regioni159 – 1613Molybdopterin-binding
    Regioni218 – 2203Molybdopterin-binding
    Regioni243 – 393151HomodimerizationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi391 – 3933Microbody targeting signalSequence analysis

    Phylogenomic databases

    eggNOGiKOG0535. Eukaryota.
    COG2041. LUCA.
    HOGENOMiHOG000252609.
    InParanoidiQ9S850.
    OMAiPVDLFYK.
    PhylomeDBiQ9S850.

    Family and domain databases

    Gene3Di2.60.40.650. 1 hit.
    3.90.420.10. 1 hit.
    InterProiIPR014756. Ig_E-set.
    IPR005066. MoCF_OxRdtse_dimer.
    IPR008335. Mopterin_OxRdtase_euk.
    IPR000572. OxRdtase_Mopterin-bd_dom.
    [Graphical view]
    PfamiPF03404. Mo-co_dimer. 1 hit.
    PF00174. Oxidored_molyb. 1 hit.
    [Graphical view]
    PRINTSiPR00407. EUMOPTERIN.
    SUPFAMiSSF56524. SSF56524. 1 hit.
    SSF81296. SSF81296. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q9S850-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MPGIRGPSEY SQEPPRHPSL KVNAKEPFNA EPPRSALVSS YVTPVDLFYK
    60 70 80 90 100
    RNHGPIPIVD HLQSYSVTLT GLIQNPRKLF IKDIRSLPKY NVTATLQCAG
    110 120 130 140 150
    NRRTAMSKVR NVRGVGWDVS AIGNAVWGGA KLADVLELVG IPKLTASTNL
    160 170 180 190 200
    GARHVEFVSV DRCKEENGGP YKASITLSQA TNPEADVLLA YEMNGETLNR
    210 220 230 240 250
    DHGFPLRVVV PGVIGARSVK WLDSINVIAE ESQGFFMQKD YKMFPPSVNW
    260 270 280 290 300
    DNINWSSRRP QMDFPVQSAI CSVEDVQMVK PGKVSIKGYA VSGGGRGIER
    310 320 330 340 350
    VDISLDGGKN WVEASRTQEP GKQYISEHSS SDKWAWVLFE ATIDVSQTTE
    360 370 380 390
    VIAKAVDSAA NVQPENVESV WNLRGVLNTS WHRVLLRLGH SNL
    Length:393
    Mass (Da):43,329
    Last modified:May 1, 2000 - v1
    Checksum:i00B4AC49E92C5DD2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061L → S in AAF13276 (PubMed:11598126).Curated
    Sequence conflicti251 – 2511D → H in AAF13276 (PubMed:11598126).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200972 mRNA. Translation: AAF13276.1.
    AB071965 mRNA. Translation: BAC10904.1.
    AC010797 Genomic DNA. Translation: AAF03458.1.
    AC011664 Genomic DNA. Translation: AAF14844.1.
    CP002686 Genomic DNA. Translation: AEE73732.1.
    AF360247 mRNA. Translation: AAK25957.1.
    AY133863 mRNA. Translation: AAM91797.1.
    RefSeqiNP_186840.1. NM_111057.3. [Q9S850-1]
    UniGeneiAt.24506.
    At.48610.

    Genome annotation databases

    EnsemblPlantsiAT3G01910.1; AT3G01910.1; AT3G01910. [Q9S850-1]
    GeneIDi820118.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200972 mRNA. Translation: AAF13276.1.
    AB071965 mRNA. Translation: BAC10904.1.
    AC010797 Genomic DNA. Translation: AAF03458.1.
    AC011664 Genomic DNA. Translation: AAF14844.1.
    CP002686 Genomic DNA. Translation: AEE73732.1.
    AF360247 mRNA. Translation: AAK25957.1.
    AY133863 mRNA. Translation: AAM91797.1.
    RefSeqiNP_186840.1. NM_111057.3. [Q9S850-1]
    UniGeneiAt.24506.
    At.48610.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OGPX-ray2.60A/B/C/D/E/F1-393[»]
    ProteinModelPortaliQ9S850.
    SMRiQ9S850. Positions 2-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi5452. 2 interactions.
    IntActiQ9S850. 1 interaction.
    STRINGi3702.AT3G01910.1.

    Proteomic databases

    PaxDbiQ9S850.
    PRIDEiQ9S850.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G01910.1; AT3G01910.1; AT3G01910. [Q9S850-1]
    GeneIDi820118.

    Organism-specific databases

    TAIRiAT3G01910.

    Phylogenomic databases

    eggNOGiKOG0535. Eukaryota.
    COG2041. LUCA.
    HOGENOMiHOG000252609.
    InParanoidiQ9S850.
    OMAiPVDLFYK.
    PhylomeDBiQ9S850.

    Enzyme and pathway databases

    UniPathwayiUPA00096.
    BioCyciARA:GQT-2438-MONOMER.
    ARA:GQT-301-MONOMER.
    BRENDAi1.8.3.1. 399.
    ReactomeiR-ATH-1614517. Sulfide oxidation to sulfate.

    Miscellaneous databases

    EvolutionaryTraceiQ9S850.
    PROiQ9S850.

    Gene expression databases

    ExpressionAtlasiQ9S850. baseline and differential.
    GenevisibleiQ9S850. AT.

    Family and domain databases

    Gene3Di2.60.40.650. 1 hit.
    3.90.420.10. 1 hit.
    InterProiIPR014756. Ig_E-set.
    IPR005066. MoCF_OxRdtse_dimer.
    IPR008335. Mopterin_OxRdtase_euk.
    IPR000572. OxRdtase_Mopterin-bd_dom.
    [Graphical view]
    PfamiPF03404. Mo-co_dimer. 1 hit.
    PF00174. Oxidored_molyb. 1 hit.
    [Graphical view]
    PRINTSiPR00407. EUMOPTERIN.
    SUPFAMiSSF56524. SSF56524. 1 hit.
    SSF81296. SSF81296. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. A new player in plant sulfur metabolism."
      Eilers T., Schwarz G., Brinkmann H., Witt C., Richter T., Nieder J., Koch B., Hille R., Haensch R., Mendel R.R.
      J. Biol. Chem. 276:46989-46994(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, SUBCELLULAR LOCATION.
      Strain: cv. Columbia.
    2. "Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulphite oxidase family."
      Nakamura T., Meyer C., Sano H.
      J. Exp. Bot. 53:1833-1836(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      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.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      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.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "The crystal structure of plant sulfite oxidase provides insights into sulfite oxidation in plants and animals."
      Schrader N., Fischer K., Theis K., Mendel R.R., Schwarz G., Kisker C.
      Structure 11:1251-1263(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MO-MOLYBDOPTERIN, COFACTOR, DOMAIN, SUBUNIT.

    Entry informationi

    Entry nameiSUOX_ARATH
    AccessioniPrimary (citable) accession number: Q9S850
    Secondary accession number(s): Q9SNW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: May 1, 2000
    Last modified: February 17, 2016
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Caution

    Lacks the conserved cytochrome b5 heme-binding domain present in other sulfite oxidases.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.