[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0167-4781(95)00068-R; PubMed=7599189 [NCBI, ExPASy, EBI, Israel, Japan] Garrett R.M., Bellissimo D.B., Rajagopalan K.V.; "Molecular cloning of human liver sulfite oxidase."; Biochim. Biophys. Acta 1262:147-149(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pancreas; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-545. Coyne K.E., Johnson J.L., Rajagopalan K.V.; "Genomic DNA sequence of human sulfite oxidase SUOX."; Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[4]	X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 79-160. DOI=10.1107/S0907444903009934; PubMed=12832761 [NCBI, ExPASy, EBI, Israel, Japan] Rudolph M.J., Johnson J.L., Rajagopalan K.V., Kisker C.; "The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain."; Acta Crystallogr. D 59:1183-1191(2003).
[5]	VARIANTS ISOD GLN-217; ASP-265; TYR-427 AND ASP-530. DOI=10.1016/S0092-8674(00)80488-2; PubMed=9428520 [NCBI, ExPASy, EBI, Israel, Japan] Kisker C., Schindelin H., Pacheco A., Wehbi W.A., Garrett R.M., Rajagopalan K.V., Enemark J.H., Rees D.C.; "Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase."; Cell 91:973-983(1997).
[6]	VARIANT ISOD GLN-217. DOI=10.1073/pnas.95.11.6394; PubMed=9600976 [NCBI, ExPASy, EBI, Israel, Japan] Garrett R.M., Johnson J.L., Graf T.N., Feigenbaum A., Rajagopalan K.V.; "Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme."; Proc. Natl. Acad. Sci. U.S.A. 95:6394-6398(1998).
[7]	VARIANTS ISOD ASP-265 AND TYR-427. DOI=10.1016/S0161-6420(99)90408-6; PubMed=10519592 [NCBI, ExPASy, EBI, Israel, Japan] Edwards M.C., Johnson J.L., Marriage B., Graf T.N., Coyne K.E., Rajagopalan K.V., MacDonald I.M.; "Isolated sulfite oxidase deficiency: review of two cases in one family."; Ophthalmology 106:1957-1961(1999).
[8]	VARIANTS ISOD LEU-258; GLN-268; SER-362; HIS-366; ARG-379; ARG-396 AND ARG-450. DOI=10.1002/humu.9038; PubMed=12112661 [NCBI, ExPASy, EBI, Israel, Japan] Johnson J.L., Coyne K.E., Garrett R.M., Zabot M.-T., Dorche C., Kisker C., Rajagopalan K.V.; "Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients."; Hum. Mutat. 20:74-74(2002).
[9]	VARIANT ISOD GLN-217. DOI=10.1055/s-2002-34491; PubMed=12368985 [NCBI, ExPASy, EBI, Israel, Japan] Lee H.F., Mak B.S., Chi C.S., Tsai C.R., Chen C.H., Shu S.G.; "A novel mutation in neonatal isolated sulphite oxidase deficiency."; Neuropediatrics 33:174-179(2002).

Comments

CATALYTIC ACTIVITY: Sulfite + O₂ + H₂O = sulfate + H₂O₂.
COFACTOR: Binds 1 protoheme group.
COFACTOR: Molybdenum (molybdopterin).
PATHWAY: Energy metabolism; sulfur metabolism .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
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.
SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=SUOX";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L31573; AAA74886.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065193; AAH65193.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056018; AAL08048.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S55874; S55874.

RefSeq

NP_000447.2; -.
NP_001027558.1; -.
NP_001027559.1; -.

UniGene

Hs.558403

3D structure databases

PDB

1MJ4; X-ray; 1.20 A; A=79-160.

[ExPASy / RCSB / EBI]

1MJ4; -.

PTM databases

P51687; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12466; -.

Organism-specific databases

HIX0036815; -.

HGNC:11460; SUOX.

272300; phenotype. [NCBI / EBI]
606887; gene. [NCBI / EBI]

Orphanet

833; Encephalopathy due to sulphite oxidase deficiency.

PharmGKB

PA36250; -.

GeneCards

P51687.

Gene expression databases

ArrayExpress

P51687; -.

CleanEx

HS_SUOX; -.

GermOnline

ENSG00000139531; Homo sapiens.

Ontologies

GO:0008482;	Molecular function: sulfite oxidase activity (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001199; Cyt_B5.
IPR005066; MoCF_OxRdtse_dimer.
IPR008335; Mopterin_OxRdtase_euk.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.120.10; Cyt_B5; 1.
G3DSA:2.60.40.650; MoCF_oxrdtse_dimer; 1.
G3DSA:3.90.420.10; Oxred_molyb_bd; 1.

Pfam

PF00173; Cyt-b5; 1.
PF03404; Mo-co_dimer; 1.
PF00174; Oxidored_molyb; 1.
Pfam graphical view of domain structure.

PRINTS

PR00363; CYTOCHROMEB5.
PR00407; EUMOPTERIN.

ProDom

PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PS00559; MOLYBDOPTERIN_EUK; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P51687.

Genome annotation databases

Ensembl

ENSG00000139531; Homo sapiens. [Contig view]

GeneID

6821; -.

KEGG

hsa:6821; -.

Phylogenomic databases

HOGENOM

P51687; -.

HOVERGEN

P51687; -.

Other

P51687; -.

SUOX; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Disease mutation; Heme; Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase; Phosphoprotein; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 79`	`79`	`Mitochondrion (By similarity).`
`CHAIN`	`80 545`	`466`	`Sulfite oxidase, mitochondrial.`	`PRO_0000006481`
`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).`
`METAL`	`118 118`		`Iron (heme axial ligand).`
`METAL`	`143 143`		`Iron (heme axial ligand).`
`METAL`	`264 264`		`Molybdenum-pterin (By similarity).`
`METAL`	`317 317`		`Molybdenum-pterin (By similarity).`
`MOD_RES`	`285 285`		`Phosphothreonine (By similarity).`
`VARIANT`	`217 217`	`1`	`R -> Q (in ISOD; 2% of activity).`	`VAR_002200`
`VARIANT`	`258 258`	`1`	`I -> L (in ISOD).`	`VAR_015724`
`VARIANT`	`265 265`	`1`	`A -> D (in ISOD).`	`VAR_002201`
`VARIANT`	`268 268`	`1`	`R -> Q (in ISOD).`	`VAR_015725`
`VARIANT`	`362 362`	`1`	`G -> S (in ISOD).`	`VAR_015726`
`VARIANT`	`366 366`	`1`	`R -> H (in ISOD).`	`VAR_015727`
`VARIANT`	`379 379`	`1`	`K -> R (in ISOD).`	`VAR_015728`
`VARIANT`	`396 396`	`1`	`Q -> R (in ISOD).`	`VAR_015729`
`VARIANT`	`427 427`	`1`	`S -> Y (in ISOD).`	`VAR_002202`
`VARIANT`	`450 450`	`1`	`W -> R (in ISOD).`	`VAR_015730`
`VARIANT`	`530 530`	`1`	`G -> D (in ISOD).`	`VAR_002203`
`TURN`	`96 98`	`3`
`STRAND`	`99 104`	`6`
`STRAND`	`107 110`	`4`
`TURN`	`112 114`	`3`
`HELIX`	`115 117`	`3`
`HELIX`	`122 126`	`5`
`TURN`	`127 130`	`4`
`STRAND`	`131 133`	`3`
`HELIX`	`134 137`	`4`
`HELIX`	`141 143`	`3`
`HELIX`	`146 153`	`8`
`STRAND`	`156 159`	`4`

Sequence information

Length: 545 AA [This is the length of the unprocessed precursor]

Molecular weight: 60283 Da [This is the MW of the unprocessed precursor]

CRC64: 39B842C55D39E11F [This is a checksum on the sequence]

        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

P51687 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools