Sulfite oxidase, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P51687 (SUOX_HUMAN)

Last modified June 16, 2009. Version 105. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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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

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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.

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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 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Sequence similarities	Contains 1 cytochrome b5 heme-binding domain.

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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 molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW sulfite oxidase activity Ref.5 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 79

Mitochondrion By similarity

Chain

80 – 545

466

Sulfite oxidase, mitochondrial

PRO_0000006481

Regions

Domain

82 – 161

Cytochrome b5 heme-binding

Region

165 – 181

Hinge By similarity

Region

182 – 545

364

Molybdenum-pterin domain By similarity

Region

215 – 219

Molybdenum-pterin-binding By similarity

Region

320 – 322

Molybdenum-pterin-binding By similarity

Region

366 – 379

Molybdenum-pterin-binding By similarity

Sites

Metal binding

118

Iron (heme axial ligand)

Metal binding

143

Iron (heme axial ligand)

Metal binding

264

Molybdenum-pterin By similarity

Metal binding

317

Molybdenum-pterin By similarity

Amino acid modifications

Modified residue

285

Phosphothreonine By similarity

Natural variations

Natural variant

217

R → Q in ISOD; 2% of activity. Ref.5 Ref.6 Ref.9

VAR_002200

Natural variant

258

I → L in ISOD. Ref.8

VAR_015724

Natural variant

265

A → D in ISOD. Ref.5 Ref.7

VAR_002201

Natural variant

268

R → Q in ISOD. Ref.8

VAR_015725

Natural variant

362

G → S in ISOD. Ref.8

VAR_015726

Natural variant

366

R → H in ISOD. Ref.8

VAR_015727

Natural variant

379

K → R in ISOD. Ref.8

VAR_015728

Natural variant

396

Q → R in ISOD. Ref.8

VAR_015729

Natural variant

427

S → Y in ISOD. Ref.5 Ref.7

VAR_002202

Natural variant

450

W → R in ISOD. Ref.8

VAR_015730

Natural variant

530

G → D in ISOD. Ref.5

VAR_002203

Secondary structure

545

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P51687-1 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 39B842C55D39E11F
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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

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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.

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Web resources

GeneReviews

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Cross-references

Sequence databases

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

IPI

IPI00745906.

PIR

S55874.

RefSeq

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

UniGene

Hs.558403

3D structure databases

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

ModBase

Search...

PTM databases

PhosphoSite

P51687.

Proteomic databases

PRIDE

P51687.

Genome annotation databases

Ensembl

ENSG00000139531. Homo sapiens. [Contig view]

GeneID

6821.

KEGG

hsa:6821.

Organism-specific databases

GeneCards

GC12P054677.

H-InvDB

HIX0036815.

HGNC

HGNC:11460. SUOX.

MIM

272300. phenotype.
606887. gene.

Orphanet

833. Encephalopathy due to sulphite oxidase deficiency.

PharmGKB

PA36250.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P51687.

HOVERGEN

P51687.

OMA

P51687. RAVIRVD.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12466.

BRENDA

1.8.3.1. 247.

Gene expression databases

ArrayExpress

P51687.

Bgee

P51687.

CleanEx

HS_SUOX.

GermOnline

ENSG00000139531. Homo sapiens.

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...

Other Resources

NextBio

26639.

SOURCE

Search...

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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:	June 16, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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