Reviewed, UniProtKB/Swiss-Prot Q9VWP4 (SUOX_DROME)

Names and origin

Protein names

Recommended name:
    Probable sulfite oxidase, mitochondrial
    EC=1.8.3.1

Gene names

ORF Names:

CG7280

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	573 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	Sulfite + O2 + H2O = sulfate + H2O2.
Cofactor	Binds 1 protoheme group By similarity. Molybdenum (molybdopterin) By similarity.
Pathway	Energy metabolism; sulfur metabolism.
Subcellular location	Mitochondrion intermembrane space By similarity.
Sequence similarities	Contains 1 cytochrome b5 heme-binding domain.
Caution	It is not obvious if the molybdenum-pterin domain is functional; the conserved cysteine (position 339) is replaced by an isoleucine.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Heme Iron Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein catabolic process Non-traceable author statement. Source: UniProtKB
Cellular component	mitochondrial intermembrane space Non-traceable author statement. Source: UniProtKB
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW sulfite oxidase activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 573		Probable sulfite oxidase, mitochondrial		PRO_0000006485
Regions
	Domain	108 – 186	79	Cytochrome b5 heme-binding
	Region	187 – 206	20	Hinge By similarity
	Region	207 – 573	367	Molybdenum-pterin domain By similarity
	Region	240 – 244	5	Molybdenum-pterin-binding By similarity
	Region	342 – 344	3	Molybdenum-pterin-binding By similarity
	Region	388 – 401	14	Molybdenum-pterin-binding By similarity
Sites
	Metal binding	144	1	Iron (heme axial ligand) By similarity
	Metal binding	168	1	Iron (heme axial ligand) By similarity
	Metal binding	287	1	Molybdenum-pterin By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9VWP4-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 71AB1D2B3465D811	FASTA	573	64,346
	10 20 30 40 50 60 MRLLRPSWAG LLRGRHHQHQ RHHRRLLLTT SRGSNGEREE QQHSQWSSPG SRSEQLFYAA 70 80 90 100 110 120 FWAGGLTLGY HWLTDKKNHV LLEGQKVASE EELEATARLW HVTNRRELPT YRAEEVEQHN 130 140 150 160 170 180 SVEKRIWVTY GLGVYDVTDF VENHPGGDKI LMAAGSAIDP FWGIYQQHNT LEVLELLEGF 190 200 210 220 230 240 RIGNLEGLVV TNVDDELGSP WSQEPQRHAL LKPASKRPFN AEPPIGLLAE QFYTPNELFY 250 260 270 280 290 300 VRNHLPVPVI NPEDYELEIE GGAKDKTLTL DGIKALPKHS VTAAIMCGGN RRSEMTKVKA 310 320 330 340 350 360 VKGLSWGAGA VGNAKWSGAR LCDILREQGV QPDETKHVIF EGADLDPTSH PYGASIPLAK 370 380 390 400 410 420 ALDPRGDVIL AYEMNDEPLS RDHGFPIRVI VPGTVGARNV KWLTRIVVAD KESDSHWQQN 430 440 450 460 470 480 DYKGFSPSTD WDTVDFSKSD AIQAMPVTSA ICTPQPGARV KVDDDEGHIT VRGYAWSGGG 490 500 510 520 530 540 RKIVRVDLTN DEGVSWHVAE LEQEEMPDGR HYGWSLWTAR LPVSEAQRRA GDVEIWAKAV 550 560 570 DSAYNVQPEK FEHIWNLRGV LANAYHKVKV KII

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014298 Genomic DNA. Translation: AAF48894.1. AY069352 mRNA. Translation: AAL39497.1.
RefSeq	NP_573331.1.
UniGene	Dm.213
3D structure databases
HSSP	HSSP built from PDB template 1SOX based on UniProtKB P07850.
ModBase	Search...
Proteomic databases
PRIDE	Q9VWP4.
Genome annotation databases
Ensembl	FBgn0030966. Drosophila melanogaster. [Contig view]
GeneID	32878.
KEGG	dme:Dmel_CG7280.
NMPDR	fig|7227.3.peg.18553.
Organism-specific databases
FlyBase	FBgn0030966. CG7280.
Phylogenomic databases
HOGENOM	Q9VWP4.
OMA	Q9VWP4. RINAKEP.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-002532-MON.
BRENDA	1.8.3.1. 48.
Gene expression databases
ArrayExpress	Q9VWP4.
GermOnline	CG7280. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001199. Cyt_B5. IPR018506. Cyt_B5_heme-BS. IPR005066. MoCF_OxRdtse_dimer. IPR008335. Mopterin_OxRdtase_euk. IPR000572. OxRdtase_Mopterin-bd. [Graphical view]
Gene3D	G3DSA:3.10.120.10. Cyt_B5. 1 hit. G3DSA:2.60.40.650. MoCF_oxrdtse_dimer. 1 hit. G3DSA:3.90.420.10. Oxred_molyb_bd. 1 hit.
Pfam	PF00173. Cyt-b5. 1 hit. PF03404. Mo-co_dimer. 1 hit. PF00174. Oxidored_molyb. 1 hit. [Graphical view]
PRINTS	PR00407. EUMOPTERIN.
ProDom	PD000612. Cyt_B5. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. PS00559. MOLYBDOPTERIN_EUK. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	780842.

Entry information

Entry name

SUOX_DROME

Accession

Primary (citable) accession number: Q9VWP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project