Reviewed, UniProtKB/Swiss-Prot P51687 (SUOX_HUMAN)

Names and origin

Protein names

Recommended name:
    Sulfite oxidase, mitochondrial
    EC=1.8.3.1

Gene names

Name:

SUOX

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	545 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Sulfite + O(2) + H(2)O = sulfate + H(2)O(2).
Cofactor	Binds 1 protoheme group. Molybdenum (molybdopterin).
Pathway	Energy metabolism; sulfur metabolism.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion intermembrane space.
Involvement in disease	Defects in SUOX are the cause of isolated sulfite oxidase deficiency (ISOD) [MIM:272300]; also known as sulfocysteinuria. ISOD is characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.
Sequence similarities	Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Disease	Disease mutation
Domain	Transit peptide
Ligand	Heme Iron Metal-binding Molybdenum
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure
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 iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: InterPro sulfite oxidase activity Ref.5 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 79

79

Mitochondrion By similarity

Chain

80 – 545

466

Sulfite oxidase, mitochondrial

PRO_0000006481

Regions

Domain

82 – 161

80

Cytochrome b5 heme-binding

Region

165 – 181

17

Hinge By similarity

Region

182 – 545

364

Molybdenum-pterin domain By similarity

Region

215 – 219

5

Molybdenum-pterin-binding By similarity

Region

320 – 322

3

Molybdenum-pterin-binding By similarity

Region

366 – 379

14

Molybdenum-pterin-binding By similarity

Sites

Metal binding

118

1

Iron (heme axial ligand)

Metal binding

143

1

Iron (heme axial ligand)

Metal binding

264

1

Molybdenum-pterin By similarity

Metal binding

317

1

Molybdenum-pterin By similarity

Amino acid modifications

Modified residue

285

1

Phosphothreonine By similarity

Natural variations

Natural variant

217

1

R → Q in ISOD; 2% of activity.

VAR_002200

Natural variant

258

1

I → L in ISOD.

VAR_015724

Natural variant

265

1

A → D in ISOD.

VAR_002201

Natural variant

268

1

R → Q in ISOD.

VAR_015725

Natural variant

362

1

G → S in ISOD.

VAR_015726

Natural variant

366

1

R → H in ISOD.

VAR_015727

Natural variant

379

1

K → R in ISOD.

VAR_015728

Natural variant

396

1

Q → R in ISOD.

VAR_015729

Natural variant

427

1

S → Y in ISOD.

VAR_002202

Natural variant

450

1

W → R in ISOD.

VAR_015730

Natural variant

530

1

G → D in ISOD.

VAR_002203

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

545

Helix Strand Turn

Details...

Turn

96 – 98

3

Beta strand

99 – 104

6

Beta strand

107 – 110

4

Turn

112 – 114

3

Helix

115 – 117

3

Helix

122 – 126

5

Turn

127 – 130

4

Beta strand

131 – 133

3

Helix

134 – 137

4

Helix

141 – 143

3

Helix

146 – 153

8

Beta strand

156 – 159

4

Sequences

	Sequence		Length	Mass (Da)
	P51687-1 [UniParc]. Last modified July 10, 2007. Version 2. Checksum: 39B842C55D39E11F	FASTA	545	60,283
	10 20 30 40 50 60 MLLLHRAVVL RLQQACRLKS IPSRICIQAC STNDSFQPQR PSLTFSGDNS STQGWRVMGT 70 80 90 100 110 120 LLGLGAVLAY QDHRCRAAQE STHIYTKEEV SSHTSPETGI WVTLGSEVFD VTEFVDLHPG 130 140 150 160 170 180 GPSKLMLAAG GPLEPFWALY AVHNQSHVRE LLAQYKIGEL NPEDKVAPTV ETSDPYADDP 190 200 210 220 230 240 VRHPALKVNS QRPFNAEPPP ELLTENYITP NPIFFTRNHL PVPNLDPDTY RLHVVGAPGG 250 260 270 280 290 300 QSLSLSLDDL HNFPRYEITV TLQCAGNRRS EMTQVKEVKG LEWRTGAIST ARWAGARLCD 310 320 330 340 350 360 VLAQAGHQLC ETEAHVCFEG LDSDPTGTAY GASIPLARAM DPEAEVLLAY EMNGQPLPRD 370 380 390 400 410 420 HGFPVRVVVP GVVGARHVKW LGRVSVQPEE SYSHWQRRDY KGFSPSVDWE TVDFDSAPSI 430 440 450 460 470 480 QELPVQSAIT EPRDGETVES GEVTIKGYAW SGGGRAVIRV DVSLDGGLTW QVAKLDGEEQ 490 500 510 520 530 540 RPRKAWAWRL WQLKAPVPAG QKELNIVCKA VDDGYNVQPD TVAPIWNLRG VLSNAWHRVH VYVSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of human liver sulfite oxidase." Garrett R.M., Bellissimo D.B., Rajagopalan K.V. Biochim. Biophys. Acta 1262:147-149(1995) [PubMed: 7599189] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[3]	"Genomic DNA sequence of human sulfite oxidase SUOX." Coyne K.E., Johnson J.L., Rajagopalan K.V. Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-545.
[4]	"The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain." Rudolph M.J., Johnson J.L., Rajagopalan K.V., Kisker C. Acta Crystallogr. D 59:1183-1191(2003) [PubMed: 12832761] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 79-160.
[5]	"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: VARIANTS ISOD GLN-217; ASP-265; TYR-427 AND ASP-530.
[6]	"Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme." Garrett R.M., Johnson J.L., Graf T.N., Feigenbaum A., Rajagopalan K.V. Proc. Natl. Acad. Sci. U.S.A. 95:6394-6398(1998) [PubMed: 9600976] [Abstract] Cited for: VARIANT ISOD GLN-217.
[7]	"Isolated sulfite oxidase deficiency: review of two cases in one family." Edwards M.C., Johnson J.L., Marriage B., Graf T.N., Coyne K.E., Rajagopalan K.V., MacDonald I.M. Ophthalmology 106:1957-1961(1999) [PubMed: 10519592] [Abstract] Cited for: VARIANTS ISOD ASP-265 AND TYR-427.
[8]	"Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients." Johnson J.L., Coyne K.E., Garrett R.M., Zabot M.-T., Dorche C., Kisker C., Rajagopalan K.V. Hum. Mutat. 20:74-74(2002) [PubMed: 12112661] [Abstract] Cited for: VARIANTS ISOD LEU-258; GLN-268; SER-362; HIS-366; ARG-379; ARG-396 AND ARG-450.
[9]	"A novel mutation in neonatal isolated sulphite oxidase deficiency." Lee H.F., Mak B.S., Chi C.S., Tsai C.R., Chen C.H., Shu S.G. Neuropediatrics 33:174-179(2002) [PubMed: 12368985] [Abstract] Cited for: VARIANT ISOD GLN-217.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

L31573 mRNA. Translation: AAA74886.1. Different initiation.
BC065193 mRNA. Translation: AAH65193.2.
AY056018 Genomic DNA. Translation: AAL08048.1. Different initiation.

PIR

S55874.

RefSeq

NP_000447.2.
NP_001027558.1.
NP_001027559.1.

UniGene

Hs.558403

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MJ4	X-ray	1.20	A	79-160	[»]

ModBase

Search...

PTM databases

PhosphoSite

P51687.

Genome annotation databases

Ensembl

ENSG00000139531. Homo sapiens. [Contig view]

GeneID

6821.

KEGG

hsa:6821.

Organism-specific databases

H-InvDB

HIX0036815.

HGNC

HGNC:11460. SUOX.

MIM

272300. phenotype.
606887. gene.

Orphanet

833. Encephalopathy due to sulphite oxidase deficiency.

PharmGKB

PA36250.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P51687.

HOVERGEN

P51687.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12466.

Gene expression databases

ArrayExpress

P51687.

CleanEx

HS_SUOX.

GermOnline

ENSG00000139531. Homo sapiens.

Family and domain databases

InterPro

IPR001199. Cyt_B5.
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...

Other Resources

LinkHub

P51687.

NextBio

26639.

SOURCE

Search...

Entry information

Entry name

SUOX_HUMAN

Accession

Primary (citable) accession number: P51687

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 10, 2007
Last modified:	November 25, 2008
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)