Reviewed, UniProtKB/Swiss-Prot P07850 (SUOX_CHICK)

Names and origin

Protein names

Recommended name:
    Sulfite oxidase
    EC=1.8.3.1

Gene names

Name:

SUOX

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Sulfite + O2 + H2O = sulfate + H2O2.
Cofactor	Binds 1 protoheme group. Molybdenum (molybdopterin).
Pathway	Energy metabolism; sulfur metabolism.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion intermembrane space.
Sequence similarities	Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	Heme Iron Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell
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 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 459

459

Sulfite oxidase

PRO_0000166076

Regions

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

Sites

Metal binding

40

1

Iron (heme axial ligand) By similarity

Metal binding

65

1

Iron (heme axial ligand) By similarity

Metal binding

185

1

Molybdenum-pterin Ref.4

Metal binding

239

1

Molybdenum-pterin By similarity

Experimental info

Sequence conflict

152

1

R → RR AA sequence Ref.1

Secondary structure

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459

Helix Strand Turn

Details...

Helix

9 – 12

4

Turn

18 – 20

3

Beta strand

21 – 26

6

Beta strand

29 – 32

4

Turn

34 – 39

6

Helix

44 – 47

4

Helix

48 – 50

3

Beta strand

53 – 55

3

Helix

56 – 61

6

Helix

63 – 66

4

Helix

68 – 75

8

Beta strand

78 – 82

5

Beta strand

92 – 94

3

Turn

96 – 99

4

Beta strand

107 – 111

5

Turn

112 – 115

4

Beta strand

116 – 118

3

Helix

121 – 123

3

Beta strand

126 – 129

4

Helix

132 – 134

3

Helix

148 – 150

3

Beta strand

152 – 156

5

Beta strand

163 – 166

4

Helix

167 – 173

7

Beta strand

176 – 184

9

Turn

186 – 189

4

Helix

190 – 194

5

Beta strand

208 – 218

11

Helix

219 – 225

7

Beta strand

237 – 245

9

Beta strand

251 – 257

7

Helix

258 – 262

5

Turn

264 – 266

3

Beta strand

269 – 274

6

Helix

281 – 283

3

Turn

284 – 286

3

Beta strand

288 – 290

3

Helix

296 – 298

3

Beta strand

301 – 311

11

Helix

316 – 319

4

Beta strand

320 – 322

3

Turn

331 – 333

3

Helix

336 – 338

3

Beta strand

348 – 354

7

Beta strand

362 – 372

11

Beta strand

379 – 387

9

Beta strand

411 – 419

9

Beta strand

424 – 433

10

Helix

444 – 446

3

Sequences

	Sequence		Length	Mass (Da)
	P07850-1 [UniParc]. Last modified February 22, 2003. Version 3. Checksum: 7AA222AD7E4E77F1	FASTA	459	50,205
	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

References

[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: 2687265] [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: 510290] [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: 9428520] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SEQUENCE REVISION TO 152. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X52559 mRNA. Translation: CAA36793.1.

IPI

IPI00572263.

PIR

A34180.

UniGene

Gga.741

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SOX	X-ray	1.90	A/B	1-459	[»]
2A99	X-ray	2.20	A	95-459	[»]
2A9A	X-ray	2.00	A/B	95-459	[»]
2A9B	X-ray	2.50	A	95-459	[»]
2A9C	X-ray	2.50	A/B	95-459	[»]
2A9D	X-ray	1.70	A/B	95-459	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

P07850.

Enzyme and pathway databases

BRENDA

1.8.3.1. 4.

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

PR00363. CYTOCHROMEB5.
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. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SUOX_CHICK

Accession

Primary (citable) accession number: P07850

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	February 22, 2003
Last modified:	June 16, 2009
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)