SUOX_ARATH
ID SUOX_ARATH Reviewed; 393 AA.
AC Q9S850; Q9SNW2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Sulfite oxidase;
DE EC=1.8.3.1;
DE AltName: Full=Moco-containing protein AtMCP;
DE Short=At-SO;
DE Short=AtSOX;
GN Name=SOX; Synonyms=MCP; OrderedLocusNames=At3g01910;
GN ORFNames=F1C9.31, F28J7.38;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11598126; DOI=10.1074/jbc.m108078200;
RA Eilers T., Schwarz G., Brinkmann H., Witt C., Richter T., Nieder J.,
RA Koch B., Hille R., Haensch R., Mendel R.R.;
RT "Identification and biochemical characterization of Arabidopsis thaliana
RT sulfite oxidase. A new player in plant sulfur metabolism.";
RL J. Biol. Chem. 276:46989-46994(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=12147736; DOI=10.1093/jxb/erf042;
RA Nakamura T., Meyer C., Sano H.;
RT "Molecular cloning and characterization of plant genes encoding novel
RT peroxisomal molybdoenzymes of the sulphite oxidase family.";
RL J. Exp. Bot. 53:1833-1836(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MO-MOLYBDOPTERIN,
RP COFACTOR, DOMAIN, AND SUBUNIT.
RX PubMed=14527393; DOI=10.1016/j.str.2003.09.001;
RA Schrader N., Fischer K., Theis K., Mendel R.R., Schwarz G., Kisker C.;
RT "The crystal structure of plant sulfite oxidase provides insights into
RT sulfite oxidation in plants and animals.";
RL Structure 11:1251-1263(2003).
CC -!- FUNCTION: Probably involved in sulfite oxidative detoxification.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sulfite = H2O2 + sulfate; Xref=Rhea:RHEA:24600,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17359; EC=1.8.3.1;
CC Evidence={ECO:0000269|PubMed:11598126};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000269|PubMed:11598126, ECO:0000269|PubMed:14527393};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000269|PubMed:11598126, ECO:0000269|PubMed:14527393};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.8 uM for sulfite (at pH 8.0 and 25 degrees Celsius);
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC -!- SUBUNIT: Predominantly monomer; also homodimer.
CC {ECO:0000269|PubMed:11598126, ECO:0000269|PubMed:14527393}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11598126,
CC ECO:0000269|PubMed:12147736}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9S850-1; Sequence=Displayed;
CC -!- CAUTION: Lacks the conserved cytochrome b5 heme-binding domain present
CC in other sulfite oxidases. {ECO:0000305}.
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DR EMBL; AF200972; AAF13276.1; -; mRNA.
DR EMBL; AB071965; BAC10904.1; -; mRNA.
DR EMBL; AC010797; AAF03458.1; -; Genomic_DNA.
DR EMBL; AC011664; AAF14844.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73732.1; -; Genomic_DNA.
DR EMBL; AF360247; AAK25957.1; -; mRNA.
DR EMBL; AY133863; AAM91797.1; -; mRNA.
DR RefSeq; NP_186840.1; NM_111057.4. [Q9S850-1]
DR PDB; 1OGP; X-ray; 2.60 A; A/B/C/D/E/F=1-393.
DR PDBsum; 1OGP; -.
DR AlphaFoldDB; Q9S850; -.
DR SMR; Q9S850; -.
DR BioGRID; 5452; 3.
DR IntAct; Q9S850; 1.
DR STRING; 3702.AT3G01910.1; -.
DR PaxDb; Q9S850; -.
DR PRIDE; Q9S850; -.
DR ProteomicsDB; 226766; -. [Q9S850-1]
DR EnsemblPlants; AT3G01910.1; AT3G01910.1; AT3G01910. [Q9S850-1]
DR GeneID; 820118; -.
DR Gramene; AT3G01910.1; AT3G01910.1; AT3G01910. [Q9S850-1]
DR KEGG; ath:AT3G01910; -.
DR Araport; AT3G01910; -.
DR TAIR; locus:2078683; AT3G01910.
DR eggNOG; KOG0535; Eukaryota.
DR InParanoid; Q9S850; -.
DR OMA; WARHVQF; -.
DR PhylomeDB; Q9S850; -.
DR BioCyc; MetaCyc:AT3G01910-MON; -.
DR BRENDA; 1.8.3.1; 399.
DR UniPathway; UPA00096; -.
DR EvolutionaryTrace; Q9S850; -.
DR PRO; PR:Q9S850; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S850; baseline and differential.
DR Genevisible; Q9S850; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IBA:GO_Central.
DR GO; GO:0008482; F:sulfite oxidase activity; IDA:TAIR.
DR GO; GO:0015994; P:chlorophyll metabolic process; IMP:TAIR.
DR GO; GO:0010477; P:response to sulfur dioxide; IMP:TAIR.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:TAIR.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PRINTS; PR00407; EUMOPTERIN.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Molybdenum;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT CHAIN 1..393
FT /note="Sulfite oxidase"
FT /id="PRO_0000166077"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 10..242
FT /note="Moco domain"
FT REGION 243..393
FT /note="Homodimerization"
FT MOTIF 391..393
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 49..53
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT BINDING 98
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT BINDING 159..161
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT BINDING 202
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT BINDING 207
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT BINDING 218..220
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT CONFLICT 206
FT /note="L -> S (in Ref. 1; AAF13276)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="D -> H (in Ref. 1; AAF13276)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1OGP"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:1OGP"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:1OGP"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1OGP"
FT TURN 200..205
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:1OGP"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 281..291
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 337..347
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:1OGP"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:1OGP"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:1OGP"
SQ SEQUENCE 393 AA; 43329 MW; 00B4AC49E92C5DD2 CRC64;
MPGIRGPSEY SQEPPRHPSL KVNAKEPFNA EPPRSALVSS YVTPVDLFYK RNHGPIPIVD
HLQSYSVTLT GLIQNPRKLF IKDIRSLPKY NVTATLQCAG NRRTAMSKVR NVRGVGWDVS
AIGNAVWGGA KLADVLELVG IPKLTASTNL GARHVEFVSV DRCKEENGGP YKASITLSQA
TNPEADVLLA YEMNGETLNR DHGFPLRVVV PGVIGARSVK WLDSINVIAE ESQGFFMQKD
YKMFPPSVNW DNINWSSRRP QMDFPVQSAI CSVEDVQMVK PGKVSIKGYA VSGGGRGIER
VDISLDGGKN WVEASRTQEP GKQYISEHSS SDKWAWVLFE ATIDVSQTTE VIAKAVDSAA
NVQPENVESV WNLRGVLNTS WHRVLLRLGH SNL
