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P51687 (SUOX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfite oxidase, mitochondrial

EC=1.8.3.1
Gene names
Name:SUOX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Sulfite + O2 + H2O = sulfate + H2O2.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group non-covalently per subunit. Ref.4

Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit By similarity. Ref.4

Pathway

Energy metabolism; sulfur metabolism.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion intermembrane space.

Involvement in disease

Isolated sulfite oxidase deficiency (ISOD) [MIM:272300]: Characterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Sequence similarities

Contains 1 cytochrome b5 heme-binding domain.

Sequence caution

The sequence AAA74886.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAL08048.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7979Mitochondrion By similarity
Chain80 – 545466Sulfite oxidase, mitochondrial
PRO_0000006481

Regions

Domain82 – 16180Cytochrome b5 heme-binding
Region165 – 17410Hinge By similarity
Region175 – 401227Moco domain By similarity
Region215 – 2195Molybdopterin-binding By similarity
Region377 – 3793Molybdopterin-binding By similarity
Region402 – 538137Homodimerization By similarity

Sites

Metal binding1181Iron (heme axial ligand)
Metal binding1431Iron (heme axial ligand)
Metal binding2641Molybdenum By similarity
Binding site1451Heme b
Binding site1471Heme b
Binding site3221Molybdopterin By similarity
Binding site3611Molybdopterin By similarity
Binding site3661Molybdopterin By similarity

Natural variations

Natural variant2171R → Q in ISOD; 2% of activity. Ref.5 Ref.6 Ref.9
VAR_002200
Natural variant2581I → L in ISOD. Ref.8
VAR_015724
Natural variant2651A → D in ISOD. Ref.5 Ref.7
VAR_002201
Natural variant2681R → Q in ISOD. Ref.8
VAR_015725
Natural variant3621G → S in ISOD. Ref.8
VAR_015726
Natural variant3661R → H in ISOD. Ref.8
VAR_015727
Natural variant3791K → R in ISOD. Ref.8
VAR_015728
Natural variant3961Q → R in ISOD. Ref.8
VAR_015729
Natural variant4271S → Y in ISOD. Ref.5 Ref.7
VAR_002202
Natural variant4501W → R in ISOD. Ref.8
VAR_015730
Natural variant5301G → D in ISOD. Ref.5
VAR_002203

Secondary structure

.................... 545
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51687 [UniParc].

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

FASTA54560,283
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 79-160 IN COMPLEX WITH HEME, COFACTOR.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: VARIANT ISOD GLN-217.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31573 mRNA. Translation: AAA74886.1. Different initiation.
BC065193 mRNA. Translation: AAH65193.2.
AY056018 Genomic DNA. Translation: AAL08048.1. Different initiation.
PIRS55874.
RefSeqNP_000447.2. NM_000456.2.
NP_001027558.1. NM_001032386.1.
NP_001027559.1. NM_001032387.1.
UniGeneHs.558403.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MJ4X-ray1.20A79-160[»]
ProteinModelPortalP51687.
SMRP51687. Positions 81-543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112690. 3 interactions.
IntActP51687. 2 interactions.
STRING9606.ENSP00000266971.

PTM databases

PhosphoSiteP51687.

Polymorphism databases

DMDM152031695.

Proteomic databases

PaxDbP51687.
PRIDEP51687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266971; ENSP00000266971; ENSG00000139531.
ENST00000356124; ENSP00000348440; ENSG00000139531.
ENST00000394109; ENSP00000377668; ENSG00000139531.
ENST00000394115; ENSP00000377674; ENSG00000139531.
ENST00000548274; ENSP00000450245; ENSG00000139531.
ENST00000550065; ENSP00000450264; ENSG00000139531.
GeneID6821.
KEGGhsa:6821.
UCSCuc001six.3. human.

Organism-specific databases

CTD6821.
GeneCardsGC12P056391.
HGNCHGNC:11460. SUOX.
HPAHPA038209.
MIM272300. phenotype.
606887. gene.
neXtProtNX_P51687.
Orphanet99731. Isolated sulfite oxidase deficiency.
PharmGKBPA36250.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2041.
HOGENOMHOG000252609.
HOVERGENHBG017865.
InParanoidP51687.
KOK00387.
OMAAVHNQSH.
OrthoDBEOG7P8P7Z.
PhylomeDBP51687.
TreeFamTF300905.

Enzyme and pathway databases

BioCycMetaCyc:HS06627-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP51687.
UniPathwayUPA00096.

Gene expression databases

ArrayExpressP51687.
BgeeP51687.
CleanExHS_SUOX.
GenevestigatorP51687.

Family and domain databases

Gene3D2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProIPR001199. 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]
PfamPF00173. Cyt-b5. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSPR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SUPFAMSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51687.
GeneWikiSulfite_oxidase.
GenomeRNAi6821.
NextBio26639.
PROP51687.
SOURCESearch...

Entry information

Entry nameSUOX_HUMAN
AccessionPrimary (citable) accession number: P51687
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM