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UniProtKB/Swiss-Prot entry P07850

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SUOX_CHICK
Primary accession number P07850
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on February 22, 2003 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 89)
Name and origin of the protein
Protein name Sulfite oxidase
Synonym EC 1.8.3.1
Gene name
Name: SUOX
From
Gallus gallus (Chicken) [TaxID: 9031] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
Protein existence 1: Evidence at protein level;
References
[1]
 PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=2687265 [NCBI, ExPASy, EBI, Israel, Japan]
Neame P.J., Barber M.J.;
"Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase.";
J. Biol. Chem. 264:20894-20901(1989).
[2]
 PROTEIN SEQUENCE OF 1-97.
TISSUE=Liver;
PubMed=510290 [NCBI, ExPASy, EBI, Israel, Japan]
Guiard B., Lederer F.;
"Amino acid sequence of the 'b5-like' heme-binding domain from chicken sulfite oxidase.";
Eur. J. Biochem. 100:441-453(1979).
[3]
 NUCLEOTIDE SEQUENCE [MRNA] OF 16-96.
STRAIN=White leghorn;
TISSUE=Liver;
Binder C.M., Irminger J.C., Jaussi R.;
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
[4]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SEQUENCE REVISION TO 152.
TISSUE=Liver;
DOI=10.1016/S0092-8674(00)80488-2; PubMed=9428520 [NCBI, ExPASy, EBI, Israel, Japan]
Kisker C., Schindelin H., Pacheco A., Wehbi W.A., Garrett R.M., Rajagopalan K.V., Enemark J.H., Rees D.C.;
"Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase.";
Cell 91:973-983(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X52559; CAA36793.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34180; A34180.
UniGene Gga.741
3D structure databases
PDB
1SOX; X-ray; 1.90 A; A/B=1-459.[ExPASy / RCSB / EBI]
2A99; X-ray; 2.20 A; A=95-459.[ExPASy / RCSB / EBI]
2A9A; X-ray; 2.00 A; A/B=95-459.[ExPASy / RCSB / EBI]
2A9B; X-ray; 2.50 A; A=95-459.[ExPASy / RCSB / EBI]
2A9C; X-ray; 2.50 A; A/B=95-459.[ExPASy / RCSB / EBI]
2A9D; X-ray; 1.70 A; A/B=95-459.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1SOX; -.
2A99; -.
2A9A; -.
2A9B; -.
2A9C; -.
2A9D; -.
ModBase P07850.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008482; Molecular function: sulfite oxidase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001199; Cyt_B5.
IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.10.120.10; Cyt_B5; 1.
G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.
Pfam PF00173; Cyt-b5; 1.
PF03404; Mo-co_dimer; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.
PRINTS PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.
ProDom PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07850.
ProtoNet P07850.
Phylogenomic databases
HOVERGEN P07850; -.
Other
LinkHub P07850; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   459  459     Sulfite oxidase. PRO_0000166076
DOMAIN   4    83  80     Cytochrome b5 heme-binding. 
REGION   86   102  17     Hinge. 
REGION   103   459  357     Molybdenum-pterin domain. 
REGION   136   140  5     Molybdenum-pterin-binding (By similarity). 
REGION   242   244  3     Molybdenum-pterin-binding (By similarity). 
REGION   288   301  14     Molybdenum-pterin-binding (By similarity). 
METAL   40    40        Iron (heme axial ligand) (By similarity). 
METAL   65    65        Iron (heme axial ligand) (By similarity). 
METAL   185   185        Molybdenum-pterin. 
METAL   239   239        Molybdenum-pterin (By similarity). 
CONFLICT   152   152        R -> RR (in Ref. 1; AA sequence). 
HELIX   9    12  4      
TURN   18    20  3      
STRAND   21    26  6      
STRAND   29    32  4      
TURN   34    39  6      
HELIX   44    47  4      
HELIX   48    50  3      
STRAND   53    55  3      
HELIX   56    61  6      
HELIX   63    66  4      
HELIX   68    75  8      
STRAND   78    82  5      
STRAND   92    94  3      
TURN   96    99  4      
STRAND   107   111  5      
TURN   112   115  4      
STRAND   116   118  3      
HELIX   121   123  3      
STRAND   126   129  4      
HELIX   132   134  3      
HELIX   148   150  3      
STRAND   152   156  5      
STRAND   163   166  4      
HELIX   167   173  7      
STRAND   176   184  9      
TURN   186   189  4      
HELIX   190   194  5      
STRAND   208   218  11      
HELIX   219   225  7      
STRAND   237   245  9      
STRAND   251   257  7      
HELIX   258   262  5      
TURN   264   266  3      
STRAND   269   274  6      
HELIX   281   283  3      
TURN   284   286  3      
STRAND   288   290  3      
HELIX   296   298  3      
STRAND   301   311  11      
HELIX   316   319  4      
STRAND   320   322  3      
TURN   331   333  3      
HELIX   336   338  3      
STRAND   348   354  7      
STRAND   362   372  11      
STRAND   379   387  9      
STRAND   411   419  9      
STRAND   424   433  10      
HELIX   444   446  3      
Sequence information
Length: 459 AA [This is the length of the unprocessed precursor] Molecular weight: 50205 Da [This is the MW of the unprocessed precursor] CRC64: 7AA222AD7E4E77F1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
APSYPRYTRE EVGRHRSPEE RVWVTHGTDV FDVTDFVELH PGGPDKILLA AGGALEPFWA 

        70         80         90        100        110        120 
LYAVHGEPHV LELLQQYKVG ELSPDEAPAA PDAQDPFAGD PPRHPGLRVN SQKPFNAEPP 

       130        140        150        160        170        180 
AELLAERFLT PNELFFTRNH LPVPAVEPSS YRLRVDGPGG RTLSLSLAEL RSRFPKHEVT 

       190        200        210        220        230        240 
ATLQCAGNRR SEMSRVRPVK GLPWDIGAIS TARWGGASLR DVLLHAGFPE ELQGGEHVCF 

       250        260        270        280        290        300 
EGLDADPGGA PYGASIPYGR ALSPAADVLL AYEMNGTELP RDHRFPVRVV VPGVVGARSV 

       310        320        330        340        350        360 
KWLRRVAVSP DESPSRWQQN DYKGFSPCVD WDTVDYRTAP AIQELPVQSA VTQPRPGAAV 

       370        380        390        400        410        420 
PPGELTVKGY AWSGGGREVV RVDVSLDGGR TWKVARLMGD KAPPGRAWAW ALWELTVPVE 

       430        440        450 
AGTELEIVCK AVDSSYNVQP DSVAPIWNLR GVLSTAWHR
P07850 in FASTA format

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