Reviewed, UniProtKB/Swiss-Prot Q9S850 (SUOX_ARATH)

Names and origin

Protein names

Recommended name:
    Sulfite oxidase
    EC=1.8.3.1
Alternative name(s):
    Moco-containing protein AtMCP
      Short name=At-SO
      Short name=AtSOX

Gene names

Name:	SOX
Synonyms:	MCP
Ordered Locus Names:	At3g01910
ORF Names:	F28J7.38, F1C9.31

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably involved in sulfite oxidative detoxification.
Catalytic activity	Sulfite + O2 + H2O = sulfate + H2O2. Ref.1
Cofactor	Molybdenum (molybdopterin). Ref.1
Pathway	Energy metabolism; sulfur metabolism.
Subunit structure	Predominantly monomer; also homodimer. Ref.1 Ref.5
Subcellular location	Peroxisome. Ref.1 Ref.2
Caution	Lacks the conserved cytochrome b5 heme-binding domain present in other sulfite oxidases.
Biophysicochemical properties	Kinetic parameters: KM=33.8 µM for sulfite (at pH 8.0 and 25 degrees Celsius)

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	chlorophyll metabolic process Inferred from mutant phenotype. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to sulfur dioxide Inferred from mutant phenotype. Source: TAIR sulfur metabolic process Ref.1 Inferred from direct assay. Source: TAIR
Cellular component	mitochondrion Inferred from direct assay. Source: TAIR peroxisome Inferred from direct assay. Source: TAIR
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW sulfite oxidase activity Ref.1 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

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

Isoform 1 (identifier: Q9S850-1)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 393

393

Sulfite oxidase

PRO_0000166077

Regions

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

Sites

Metal binding

98

1

Molybdenum-pterin

Experimental info

Sequence conflict

206

1

L → S in AAF13276. Ref.1

Sequence conflict

251

1

D → H in AAF13276. Ref.1

Secondary structure

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393

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Beta strand

21 – 24

4

Turn

25 – 28

4

Beta strand

29 – 31

3

Helix

34 – 37

4

Helix

45 – 47

3

Beta strand

58 – 60

3

Beta strand

66 – 75

10

Beta strand

78 – 80

3

Helix

81 – 85

5

Beta strand

89 – 97

9

Turn

99 – 102

4

Helix

103 – 109

7

Beta strand

122 – 131

10

Helix

132 – 137

6

Turn

138 – 140

3

Beta strand

154 – 160

7

Helix

164 – 166

3

Beta strand

172 – 176

5

Helix

177 – 181

5

Helix

183 – 185

3

Beta strand

188 – 193

6

Turn

200 – 205

6

Beta strand

207 – 209

3

Helix

215 – 217

3

Beta strand

221 – 230

10

Helix

235 – 238

4

Beta strand

239 – 241

3

Turn

250 – 252

3

Helix

255 – 257

3

Beta strand

267 – 270

4

Beta strand

275 – 279

5

Beta strand

281 – 291

11

Beta strand

298 – 306

9

Beta strand

315 – 322

8

Beta strand

326 – 328

3

Beta strand

337 – 347

11

Beta strand

349 – 357

9

Helix

367 – 370

4

Beta strand

382 – 388

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 00B4AC49E92C5DD2	FASTA	393	43,329
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11598126] [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: 12147736] [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: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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: 14527393] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MOLYBDENUM-PTERIN, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF200972 mRNA. Translation: AAF13276.1.
AB071965 mRNA. Translation: BAC10904.1.
AC010797 Genomic DNA. Translation: AAF03458.1.
AC011664 Genomic DNA. Translation: AAF14844.1.
AF360247 mRNA. Translation: AAK25957.1.
AY133863 mRNA. Translation: AAM91797.1.

IPI

IPI00541541.

RefSeq

NP_186840.1.

UniGene

At.24506

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OGP	X-ray	2.60	A/B/C/D/E/F	1-393	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q9S850.

ProMEX

Q9S850.

Genome annotation databases

GeneID

820118.

GenomeReviews

Gene locus AT3G01910 in contig BA000014_GR.

NMPDR

fig|3702.1.peg.12123.

Organism-specific databases

GeneFarm

4907.

TAIR

At3g01910.

Phylogenomic databases

OMA

Q9S850. RAVIRVD.

Enzyme and pathway databases

BRENDA

1.8.3.1. 302.

Gene expression databases

ArrayExpress

Q9S850.

Family and domain databases

InterPro

IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR000572. OxRdtase_Mopterin-bd.
[Graphical view]

Gene3D

G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit.
G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.

Pfam

PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]

PRINTS

PR00407. EUMOPTERIN.

PROSITE

PS00559. MOLYBDOPTERIN_EUK. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SUOX_ARATH

Accession

Primary (citable) accession number: Q9S850
Secondary accession number(s): Q9SNW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)