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Protein

Sulfite oxidase, mitochondrial

Gene

SUOX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Sulfite + O2 + H2O = sulfate + H2O2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi118 – 1181Iron (heme axial ligand)
Metal bindingi143 – 1431Iron (heme axial ligand)
Binding sitei145 – 1451Heme b1 Publication
Binding sitei147 – 1471Heme b1 Publication
Metal bindingi264 – 2641MolybdenumBy similarity
Binding sitei322 – 3221MolybdopterinBy similarity
Binding sitei361 – 3611MolybdopterinBy similarity
Binding sitei366 – 3661MolybdopterinBy similarity

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. heme binding Source: InterPro
  3. molybdenum ion binding Source: InterPro
  4. molybdopterin cofactor binding Source: InterPro
  5. sulfite oxidase activity Source: Reactome

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. small molecule metabolic process Source: Reactome
  3. sulfide oxidation, using sulfide:quinone oxidoreductase Source: Reactome
  4. sulfur amino acid catabolic process Source: Reactome
  5. sulfur amino acid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciMetaCyc:HS06627-MONOMER.
ReactomeiREACT_116010. Sulfide oxidation to sulfate.
SABIO-RKP51687.
UniPathwayiUPA00096.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite oxidase, mitochondrial (EC:1.8.3.1)
Gene namesi
Name:SUOX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11460. SUOX.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: UniProtKB-SubCell
  2. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Isolated sulfite oxidase deficiency5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionCharacterized by neurological abnormalities including multicystic leukoencephalopathy with brain atrophy. Patients often suffer from seizures. Often leads to death at an early age.

See also OMIM:272300
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171R → Q in ISOD; 2% of activity. 3 Publications
VAR_002200
Natural varianti258 – 2581I → L in ISOD. 1 Publication
VAR_015724
Natural varianti265 – 2651A → D in ISOD. 2 Publications
VAR_002201
Natural varianti268 – 2681R → Q in ISOD. 1 Publication
VAR_015725
Natural varianti362 – 3621G → S in ISOD. 1 Publication
VAR_015726
Natural varianti366 – 3661R → H in ISOD. 1 Publication
VAR_015727
Natural varianti379 – 3791K → R in ISOD. 1 Publication
VAR_015728
Natural varianti396 – 3961Q → R in ISOD. 1 Publication
VAR_015729
Natural varianti427 – 4271S → Y in ISOD. 2 Publications
VAR_002202
Natural varianti450 – 4501W → R in ISOD. 1 Publication
VAR_015730
Natural varianti530 – 5301G → D in ISOD. 1 Publication
VAR_002203

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi272300. phenotype.
Orphaneti99731. Isolated sulfite oxidase deficiency.
PharmGKBiPA36250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7979MitochondrionBy similarityAdd
BLAST
Chaini80 – 545466Sulfite oxidase, mitochondrialPRO_0000006481Add
BLAST

Proteomic databases

MaxQBiP51687.
PaxDbiP51687.
PRIDEiP51687.

PTM databases

PhosphoSiteiP51687.

Expressioni

Gene expression databases

BgeeiP51687.
CleanExiHS_SUOX.
ExpressionAtlasiP51687. baseline and differential.
GenevestigatoriP51687.

Organism-specific databases

HPAiHPA038209.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi112690. 4 interactions.
IntActiP51687. 2 interactions.
STRINGi9606.ENSP00000266971.

Structurei

Secondary structure

1
545
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni96 – 983Combined sources
Beta strandi99 – 1046Combined sources
Beta strandi107 – 1104Combined sources
Turni112 – 1143Combined sources
Helixi115 – 1173Combined sources
Helixi122 – 1265Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 1333Combined sources
Helixi134 – 1374Combined sources
Helixi141 – 1433Combined sources
Helixi146 – 1538Combined sources
Beta strandi156 – 1594Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MJ4X-ray1.20A79-160[»]
ProteinModelPortaliP51687.
SMRiP51687. Positions 81-543.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 16180Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 17410HingeBy similarity
Regioni175 – 401227Moco domainBy similarityAdd
BLAST
Regioni215 – 2195Molybdopterin-bindingBy similarity
Regioni377 – 3793Molybdopterin-bindingBy similarity
Regioni402 – 538137HomodimerizationBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 cytochrome b5 heme-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2041.
GeneTreeiENSGT00390000003749.
HOGENOMiHOG000252609.
HOVERGENiHBG017865.
InParanoidiP51687.
KOiK00387.
OMAiAVHNQSH.
OrthoDBiEOG7P8P7Z.
PhylomeDBiP51687.
TreeFamiTF300905.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. 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]
PfamiPF00173. Cyt-b5. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSiPR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51687-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLLHRAVVL RLQQACRLKS IPSRICIQAC STNDSFQPQR PSLTFSGDNS
60 70 80 90 100
STQGWRVMGT LLGLGAVLAY QDHRCRAAQE STHIYTKEEV SSHTSPETGI
110 120 130 140 150
WVTLGSEVFD VTEFVDLHPG GPSKLMLAAG GPLEPFWALY AVHNQSHVRE
160 170 180 190 200
LLAQYKIGEL NPEDKVAPTV ETSDPYADDP VRHPALKVNS QRPFNAEPPP
210 220 230 240 250
ELLTENYITP NPIFFTRNHL PVPNLDPDTY RLHVVGAPGG QSLSLSLDDL
260 270 280 290 300
HNFPRYEITV TLQCAGNRRS EMTQVKEVKG LEWRTGAIST ARWAGARLCD
310 320 330 340 350
VLAQAGHQLC ETEAHVCFEG LDSDPTGTAY GASIPLARAM DPEAEVLLAY
360 370 380 390 400
EMNGQPLPRD HGFPVRVVVP GVVGARHVKW LGRVSVQPEE SYSHWQRRDY
410 420 430 440 450
KGFSPSVDWE TVDFDSAPSI QELPVQSAIT EPRDGETVES GEVTIKGYAW
460 470 480 490 500
SGGGRAVIRV DVSLDGGLTW QVAKLDGEEQ RPRKAWAWRL WQLKAPVPAG
510 520 530 540
QKELNIVCKA VDDGYNVQPD TVAPIWNLRG VLSNAWHRVH VYVSP
Length:545
Mass (Da):60,283
Last modified:July 10, 2007 - v2
Checksum:i39B842C55D39E11F
GO

Sequence cautioni

The sequence AAA74886.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL08048.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171R → Q in ISOD; 2% of activity. 3 Publications
VAR_002200
Natural varianti258 – 2581I → L in ISOD. 1 Publication
VAR_015724
Natural varianti265 – 2651A → D in ISOD. 2 Publications
VAR_002201
Natural varianti268 – 2681R → Q in ISOD. 1 Publication
VAR_015725
Natural varianti362 – 3621G → S in ISOD. 1 Publication
VAR_015726
Natural varianti366 – 3661R → H in ISOD. 1 Publication
VAR_015727
Natural varianti379 – 3791K → R in ISOD. 1 Publication
VAR_015728
Natural varianti396 – 3961Q → R in ISOD. 1 Publication
VAR_015729
Natural varianti427 – 4271S → Y in ISOD. 2 Publications
VAR_002202
Natural varianti450 – 4501W → R in ISOD. 1 Publication
VAR_015730
Natural varianti530 – 5301G → D in ISOD. 1 Publication
VAR_002203

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31573 mRNA. Translation: AAA74886.1. Different initiation.
BC065193 mRNA. Translation: AAH65193.2.
AY056018 Genomic DNA. Translation: AAL08048.1. Different initiation.
CCDSiCCDS8901.2.
PIRiS55874.
RefSeqiNP_000447.2. NM_000456.2.
NP_001027558.1. NM_001032386.1.
NP_001027559.1. NM_001032387.1.
UniGeneiHs.558403.

Genome annotation databases

EnsembliENST00000266971; ENSP00000266971; ENSG00000139531.
ENST00000356124; ENSP00000348440; ENSG00000139531.
ENST00000394109; ENSP00000377668; ENSG00000139531.
ENST00000394115; ENSP00000377674; ENSG00000139531.
ENST00000548274; ENSP00000450245; ENSG00000139531.
ENST00000550065; ENSP00000450264; ENSG00000139531.
GeneIDi6821.
KEGGihsa:6821.
UCSCiuc001six.3. human.

Polymorphism databases

DMDMi152031695.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L31573 mRNA. Translation: AAA74886.1. Different initiation.
BC065193 mRNA. Translation: AAH65193.2.
AY056018 Genomic DNA. Translation: AAL08048.1. Different initiation.
CCDSiCCDS8901.2.
PIRiS55874.
RefSeqiNP_000447.2. NM_000456.2.
NP_001027558.1. NM_001032386.1.
NP_001027559.1. NM_001032387.1.
UniGeneiHs.558403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MJ4X-ray1.20A79-160[»]
ProteinModelPortaliP51687.
SMRiP51687. Positions 81-543.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112690. 4 interactions.
IntActiP51687. 2 interactions.
STRINGi9606.ENSP00000266971.

PTM databases

PhosphoSiteiP51687.

Polymorphism databases

DMDMi152031695.

Proteomic databases

MaxQBiP51687.
PaxDbiP51687.
PRIDEiP51687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266971; ENSP00000266971; ENSG00000139531.
ENST00000356124; ENSP00000348440; ENSG00000139531.
ENST00000394109; ENSP00000377668; ENSG00000139531.
ENST00000394115; ENSP00000377674; ENSG00000139531.
ENST00000548274; ENSP00000450245; ENSG00000139531.
ENST00000550065; ENSP00000450264; ENSG00000139531.
GeneIDi6821.
KEGGihsa:6821.
UCSCiuc001six.3. human.

Organism-specific databases

CTDi6821.
GeneCardsiGC12P056391.
HGNCiHGNC:11460. SUOX.
HPAiHPA038209.
MIMi272300. phenotype.
606887. gene.
neXtProtiNX_P51687.
Orphaneti99731. Isolated sulfite oxidase deficiency.
PharmGKBiPA36250.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2041.
GeneTreeiENSGT00390000003749.
HOGENOMiHOG000252609.
HOVERGENiHBG017865.
InParanoidiP51687.
KOiK00387.
OMAiAVHNQSH.
OrthoDBiEOG7P8P7Z.
PhylomeDBiP51687.
TreeFamiTF300905.

Enzyme and pathway databases

UniPathwayiUPA00096.
BioCyciMetaCyc:HS06627-MONOMER.
ReactomeiREACT_116010. Sulfide oxidation to sulfate.
SABIO-RKP51687.

Miscellaneous databases

ChiTaRSiSUOX. human.
EvolutionaryTraceiP51687.
GeneWikiiSulfite_oxidase.
GenomeRNAii6821.
NextBioi26639.
PROiP51687.
SOURCEiSearch...

Gene expression databases

BgeeiP51687.
CleanExiHS_SUOX.
ExpressionAtlasiP51687. baseline and differential.
GenevestigatoriP51687.

Family and domain databases

Gene3Di2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProiIPR001199. 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]
PfamiPF00173. Cyt-b5. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view]
PRINTSiPR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SUPFAMiSSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiSUOX_HUMAN
AccessioniPrimary (citable) accession number: P51687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 10, 2007
Last modified: January 7, 2015
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.