Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sulfite oxidase

Gene

SUOX

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Sulfite + O2 + H2O = sulfate + H2O2.

Cofactori

Protein has several cofactor binding sites:

Pathway: 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 bindingi40 – 401Iron (heme axial ligand)
Metal bindingi65 – 651Iron (heme axial ligand)
Binding sitei69 – 691Heme b1 Publication
Metal bindingi185 – 1851Molybdenum
Binding sitei244 – 2441Molybdopterin
Binding sitei283 – 2831Molybdopterin
Binding sitei288 – 2881Molybdopterin

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDAi1.8.2.1. 1306.
1.8.3.1. 1306.
UniPathwayiUPA00096.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite oxidase (EC:1.8.3.1)
Gene namesi
Name:SUOX
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Sulfite oxidasePRO_0000166076Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124Combined sources
Turni18 – 203Combined sources
Beta strandi21 – 266Combined sources
Beta strandi29 – 324Combined sources
Turni34 – 396Combined sources
Helixi44 – 474Combined sources
Helixi48 – 503Combined sources
Beta strandi53 – 553Combined sources
Helixi56 – 616Combined sources
Helixi63 – 664Combined sources
Helixi68 – 758Combined sources
Beta strandi78 – 825Combined sources
Beta strandi92 – 943Combined sources
Turni96 – 994Combined sources
Beta strandi107 – 1115Combined sources
Turni112 – 1154Combined sources
Beta strandi116 – 1183Combined sources
Helixi121 – 1244Combined sources
Beta strandi126 – 1294Combined sources
Turni132 – 1343Combined sources
Turni148 – 1503Combined sources
Beta strandi152 – 1565Combined sources
Turni158 – 1603Combined sources
Beta strandi163 – 1664Combined sources
Helixi167 – 1737Combined sources
Beta strandi177 – 1848Combined sources
Turni186 – 1894Combined sources
Helixi190 – 1945Combined sources
Beta strandi208 – 21811Combined sources
Helixi219 – 2257Combined sources
Beta strandi237 – 2459Combined sources
Beta strandi251 – 2577Combined sources
Helixi258 – 2625Combined sources
Helixi264 – 2663Combined sources
Beta strandi269 – 2746Combined sources
Helixi281 – 2833Combined sources
Turni284 – 2863Combined sources
Beta strandi288 – 2903Combined sources
Helixi296 – 2983Combined sources
Beta strandi301 – 31111Combined sources
Helixi316 – 3194Combined sources
Beta strandi320 – 3223Combined sources
Turni331 – 3333Combined sources
Helixi336 – 3383Combined sources
Beta strandi348 – 3547Combined sources
Beta strandi362 – 37211Combined sources
Beta strandi379 – 39113Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi411 – 4199Combined sources
Beta strandi424 – 43310Combined sources
Helixi444 – 4463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SOXX-ray1.90A/B1-459[»]
2A99X-ray2.20A95-459[»]
2A9AX-ray2.00A/B95-459[»]
2A9BX-ray2.50A95-459[»]
2A9CX-ray2.50A/B95-459[»]
2A9DX-ray1.70A/B95-459[»]
3HBGX-ray1.90A1-459[»]
3HBPX-ray2.40A1-459[»]
3HBQX-ray2.80A1-459[»]
3R18X-ray2.40A1-459[»]
3R19X-ray2.10A1-459[»]
ProteinModelPortaliP07850.
SMRiP07850. Positions 3-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07850.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 8380Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 9510Hinge
Regioni96 – 323228Moco domainAdd
BLAST
Regioni136 – 1405Molybdopterin-binding
Regioni299 – 3013Molybdopterin-binding
Regioni324 – 459136HomodimerizationAdd
BLAST

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG017865.
InParanoidiP07850.
PhylomeDBiP07850.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSiPR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07850-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
APSYPRYTRE EVGRHRSPEE RVWVTHGTDV FDVTDFVELH PGGPDKILLA
60 70 80 90 100
AGGALEPFWA LYAVHGEPHV LELLQQYKVG ELSPDEAPAA PDAQDPFAGD
110 120 130 140 150
PPRHPGLRVN SQKPFNAEPP AELLAERFLT PNELFFTRNH LPVPAVEPSS
160 170 180 190 200
YRLRVDGPGG RTLSLSLAEL RSRFPKHEVT ATLQCAGNRR SEMSRVRPVK
210 220 230 240 250
GLPWDIGAIS TARWGGASLR DVLLHAGFPE ELQGGEHVCF EGLDADPGGA
260 270 280 290 300
PYGASIPYGR ALSPAADVLL AYEMNGTELP RDHRFPVRVV VPGVVGARSV
310 320 330 340 350
KWLRRVAVSP DESPSRWQQN DYKGFSPCVD WDTVDYRTAP AIQELPVQSA
360 370 380 390 400
VTQPRPGAAV PPGELTVKGY AWSGGGREVV RVDVSLDGGR TWKVARLMGD
410 420 430 440 450
KAPPGRAWAW ALWELTVPVE AGTELEIVCK AVDSSYNVQP DSVAPIWNLR

GVLSTAWHR
Length:459
Mass (Da):50,205
Last modified:February 22, 2003 - v3
Checksum:i7AA222AD7E4E77F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521R → RR AA sequence (PubMed:2687265).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52559 mRNA. Translation: CAA36793.1.
PIRiA34180.
UniGeneiGga.741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52559 mRNA. Translation: CAA36793.1.
PIRiA34180.
UniGeneiGga.741.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SOXX-ray1.90A/B1-459[»]
2A99X-ray2.20A95-459[»]
2A9AX-ray2.00A/B95-459[»]
2A9BX-ray2.50A95-459[»]
2A9CX-ray2.50A/B95-459[»]
2A9DX-ray1.70A/B95-459[»]
3HBGX-ray1.90A1-459[»]
3HBPX-ray2.40A1-459[»]
3HBQX-ray2.80A1-459[»]
3R18X-ray2.40A1-459[»]
3R19X-ray2.10A1-459[»]
ProteinModelPortaliP07850.
SMRiP07850. Positions 3-459.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG017865.
InParanoidiP07850.
PhylomeDBiP07850.

Enzyme and pathway databases

UniPathwayiUPA00096.
BRENDAi1.8.2.1. 1306.
1.8.3.1. 1306.

Miscellaneous databases

EvolutionaryTraceiP07850.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. Cyt_B5-like_heme/steroid-bd.
IPR018506. Cyt_B5_heme-BS.
IPR014756. Ig_E-set.
IPR005066. MoCF_OxRdtse_dimer.
IPR008335. Mopterin_OxRdtase_euk.
IPR000572. OxRdtase_Mopterin-bd_dom.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view]
PfamiPF00173. Cyt-b5. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSiPR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase."
    Neame P.J., Barber M.J.
    J. Biol. Chem. 264:20894-20901(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Amino acid sequence of the 'b5-like' heme-binding domain from chicken sulfite oxidase."
    Guiard B., Lederer F.
    Eur. J. Biochem. 100:441-453(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-97.
    Tissue: Liver.
  3. Binder C.M., Irminger J.C., Jaussi R.
    Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-96.
    Strain: White leghorn.
    Tissue: Liver.
  4. "Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase."
    Kisker C., Schindelin H., Pacheco A., Wehbi W.A., Garrett R.M., Rajagopalan K.V., Enemark J.H., Rees D.C.
    Cell 91:973-983(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 152, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME AND MO-MOLYBDOPTERIN, COFACTOR.
    Tissue: Liver.

Entry informationi

Entry nameiSUOX_CHICK
AccessioniPrimary (citable) accession number: P07850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 22, 2003
Last modified: June 24, 2015
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.