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P51687

- SUOX_HUMAN

UniProt

P51687 - SUOX_HUMAN

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Protein
Sulfite oxidase, mitochondrial
Gene
SUOX
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Sulfite + O2 + H2O = sulfate + H2O2.

Cofactori

Binds 1 heme B (iron-protoporphyrin IX) group non-covalently per subunit.1 Publication
Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit By similarity.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi118 – 1181Iron (heme axial ligand)
Metal bindingi143 – 1431Iron (heme axial ligand)
Binding sitei145 – 1451Heme b
Binding sitei147 – 1471Heme b
Metal bindingi264 – 2641Molybdenum By similarity
Binding sitei322 – 3221Molybdopterin By similarity
Binding sitei361 – 3611Molybdopterin By similarity
Binding sitei366 – 3661Molybdopterin By 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 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.5 Publications
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 – 7979Mitochondrion By similarity
Add
BLAST
Chaini80 – 545466Sulfite oxidase, mitochondrial
PRO_0000006481Add
BLAST

Proteomic databases

MaxQBiP51687.
PaxDbiP51687.
PRIDEiP51687.

PTM databases

PhosphoSiteiP51687.

Expressioni

Gene expression databases

ArrayExpressiP51687.
BgeeiP51687.
CleanExiHS_SUOX.
GenevestigatoriP51687.

Organism-specific databases

HPAiHPA038209.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi112690. 3 interactions.
IntActiP51687. 2 interactions.
STRINGi9606.ENSP00000266971.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MJ4X-ray1.20A79-160[»]
ProteinModelPortaliP51687.
SMRiP51687. Positions 81-543.

Miscellaneous databases

EvolutionaryTraceiP51687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 16180Cytochrome b5 heme-binding
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 17410Hinge By similarity
Regioni175 – 401227Moco domain By similarity
Add
BLAST
Regioni215 – 2195Molybdopterin-binding By similarity
Regioni377 – 3793Molybdopterin-binding By similarity
Regioni402 – 538137Homodimerization By similarity
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2041.
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

MLLLHRAVVL RLQQACRLKS IPSRICIQAC STNDSFQPQR PSLTFSGDNS    50
STQGWRVMGT LLGLGAVLAY QDHRCRAAQE STHIYTKEEV SSHTSPETGI 100
WVTLGSEVFD VTEFVDLHPG GPSKLMLAAG GPLEPFWALY AVHNQSHVRE 150
LLAQYKIGEL NPEDKVAPTV ETSDPYADDP VRHPALKVNS QRPFNAEPPP 200
ELLTENYITP NPIFFTRNHL PVPNLDPDTY RLHVVGAPGG QSLSLSLDDL 250
HNFPRYEITV TLQCAGNRRS EMTQVKEVKG LEWRTGAIST ARWAGARLCD 300
VLAQAGHQLC ETEAHVCFEG LDSDPTGTAY GASIPLARAM DPEAEVLLAY 350
EMNGQPLPRD HGFPVRVVVP GVVGARHVKW LGRVSVQPEE SYSHWQRRDY 400
KGFSPSVDWE TVDFDSAPSI QELPVQSAIT EPRDGETVES GEVTIKGYAW 450
SGGGRAVIRV DVSLDGGLTW QVAKLDGEEQ RPRKAWAWRL WQLKAPVPAG 500
QKELNIVCKA VDDGYNVQPD TVAPIWNLRG VLSNAWHRVH VYVSP 545
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.
The sequence AAL08048.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L31573 mRNA. Translation: AAA74886.1 . Different initiation.
BC065193 mRNA. Translation: AAH65193.2 .
AY056018 Genomic DNA. Translation: AAL08048.1 . Different initiation.
CCDSi CCDS8901.2.
PIRi S55874.
RefSeqi NP_000447.2. NM_000456.2.
NP_001027558.1. NM_001032386.1.
NP_001027559.1. NM_001032387.1.
UniGenei Hs.558403.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MJ4 X-ray 1.20 A 79-160 [» ]
ProteinModelPortali P51687.
SMRi P51687. Positions 81-543.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112690. 3 interactions.
IntActi P51687. 2 interactions.
STRINGi 9606.ENSP00000266971.

PTM databases

PhosphoSitei P51687.

Polymorphism databases

DMDMi 152031695.

Proteomic databases

MaxQBi P51687.
PaxDbi P51687.
PRIDEi P51687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000266971 ; ENSP00000266971 ; ENSG00000139531 .
ENST00000356124 ; ENSP00000348440 ; ENSG00000139531 .
ENST00000394109 ; ENSP00000377668 ; ENSG00000139531 .
ENST00000394115 ; ENSP00000377674 ; ENSG00000139531 .
ENST00000548274 ; ENSP00000450245 ; ENSG00000139531 .
ENST00000550065 ; ENSP00000450264 ; ENSG00000139531 .
GeneIDi 6821.
KEGGi hsa:6821.
UCSCi uc001six.3. human.

Organism-specific databases

CTDi 6821.
GeneCardsi GC12P056391.
HGNCi HGNC:11460. SUOX.
HPAi HPA038209.
MIMi 272300. phenotype.
606887. gene.
neXtProti NX_P51687.
Orphaneti 99731. Isolated sulfite oxidase deficiency.
PharmGKBi PA36250.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2041.
HOGENOMi HOG000252609.
HOVERGENi HBG017865.
InParanoidi P51687.
KOi K00387.
OMAi AVHNQSH.
OrthoDBi EOG7P8P7Z.
PhylomeDBi P51687.
TreeFami TF300905.

Enzyme and pathway databases

UniPathwayi UPA00096 .
BioCyci MetaCyc:HS06627-MONOMER.
Reactomei REACT_116010. Sulfide oxidation to sulfate.
SABIO-RK P51687.

Miscellaneous databases

EvolutionaryTracei P51687.
GeneWikii Sulfite_oxidase.
GenomeRNAii 6821.
NextBioi 26639.
PROi P51687.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51687.
Bgeei P51687.
CleanExi HS_SUOX.
Genevestigatori P51687.

Family and domain databases

Gene3Di 2.60.40.650. 1 hit.
3.10.120.10. 1 hit.
3.90.420.10. 1 hit.
InterProi IPR001199. 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 ]
Pfami PF00173. Cyt-b5. 1 hit.
PF03404. Mo-co_dimer. 1 hit.
PF00174. Oxidored_molyb. 1 hit.
[Graphical view ]
PRINTSi PR00363. CYTOCHROMEB5.
PR00407. EUMOPTERIN.
SUPFAMi SSF55856. SSF55856. 1 hit.
SSF56524. SSF56524. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 156 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

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