SUOX_HUMAN
ID SUOX_HUMAN Reviewed; 545 AA.
AC P51687;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Sulfite oxidase, mitochondrial {ECO:0000303|PubMed:7599189};
DE EC=1.8.3.1 {ECO:0000250|UniProtKB:Q07116};
DE Flags: Precursor;
GN Name=SUOX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7599189; DOI=10.1016/0167-4781(95)00068-r;
RA Garrett R.M., Bellissimo D.B., Rajagopalan K.V.;
RT "Molecular cloning of human liver sulfite oxidase.";
RL Biochim. Biophys. Acta 1262:147-149(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-545.
RA Coyne K.E., Johnson J.L., Rajagopalan K.V.;
RT "Genomic DNA sequence of human sulfite oxidase SUOX.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 79-160 IN COMPLEX WITH HEME,
RP COFACTOR, AND SUBUNIT.
RX PubMed=12832761; DOI=10.1107/s0907444903009934;
RA Rudolph M.J., Johnson J.L., Rajagopalan K.V., Kisker C.;
RT "The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.";
RL Acta Crystallogr. D 59:1183-1191(2003).
RN [6]
RP VARIANTS ISOD GLN-217; ASP-265; TYR-427 AND ASP-530.
RX PubMed=9428520; DOI=10.1016/s0092-8674(00)80488-2;
RA Kisker C., Schindelin H., Pacheco A., Wehbi W.A., Garrett R.M.,
RA Rajagopalan K.V., Enemark J.H., Rees D.C.;
RT "Molecular basis of sulfite oxidase deficiency from the structure of
RT sulfite oxidase.";
RL Cell 91:973-983(1997).
RN [7]
RP VARIANT ISOD GLN-217.
RX PubMed=9600976; DOI=10.1073/pnas.95.11.6394;
RA Garrett R.M., Johnson J.L., Graf T.N., Feigenbaum A., Rajagopalan K.V.;
RT "Human sulfite oxidase R160Q: identification of the mutation in a sulfite
RT oxidase-deficient patient and expression and characterization of the mutant
RT enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6394-6398(1998).
RN [8]
RP VARIANTS ISOD ASP-265 AND TYR-427.
RX PubMed=10519592; DOI=10.1016/s0161-6420(99)90408-6;
RA Edwards M.C., Johnson J.L., Marriage B., Graf T.N., Coyne K.E.,
RA Rajagopalan K.V., MacDonald I.M.;
RT "Isolated sulfite oxidase deficiency: review of two cases in one family.";
RL Ophthalmology 106:1957-1961(1999).
RN [9]
RP VARIANTS ISOD LEU-258; GLN-268; SER-362; HIS-366; ARG-379; ARG-396 AND
RP ARG-450.
RX PubMed=12112661; DOI=10.1002/humu.9038;
RA Johnson J.L., Coyne K.E., Garrett R.M., Zabot M.-T., Dorche C., Kisker C.,
RA Rajagopalan K.V.;
RT "Isolated sulfite oxidase deficiency: identification of 12 novel SUOX
RT mutations in 10 patients.";
RL Hum. Mutat. 20:74-74(2002).
RN [10]
RP VARIANT ISOD GLN-217.
RX PubMed=12368985; DOI=10.1055/s-2002-34491;
RA Lee H.F., Mak B.S., Chi C.S., Tsai C.R., Chen C.H., Shu S.G.;
RT "A novel mutation in neonatal isolated sulphite oxidase deficiency.";
RL Neuropediatrics 33:174-179(2002).
CC -!- FUNCTION: Catalyzes the oxidation of sulfite to sulfate, the terminal
CC reaction in the oxidative degradation of sulfur-containing amino acids.
CC {ECO:0000250|UniProtKB:Q07116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sulfite = H2O2 + sulfate; Xref=Rhea:RHEA:24600,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17359; EC=1.8.3.1;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24601;
CC Evidence={ECO:0000250|UniProtKB:Q07116};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:12832761};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000269|PubMed:12832761};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000250|UniProtKB:P07850};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250|UniProtKB:P07850};
CC -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC {ECO:0000250|UniProtKB:Q07116}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12832761}.
CC -!- INTERACTION:
CC P51687; Q8WXI4-2: ACOT11; NbExp=3; IntAct=EBI-3921347, EBI-17721098;
CC P51687; O95429: BAG4; NbExp=3; IntAct=EBI-3921347, EBI-2949658;
CC P51687; Q13901: C1D; NbExp=3; IntAct=EBI-3921347, EBI-3844053;
CC P51687; A0A0C4DGW6: C5orf51; NbExp=3; IntAct=EBI-3921347, EBI-12836808;
CC P51687; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-3921347, EBI-1383687;
CC P51687; Q8IW40: CCDC103; NbExp=3; IntAct=EBI-3921347, EBI-10261970;
CC P51687; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-3921347, EBI-1773949;
CC P51687; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-3921347, EBI-742887;
CC P51687; Q96BR5: COA7; NbExp=3; IntAct=EBI-3921347, EBI-6269632;
CC P51687; Q99627: COPS8; NbExp=3; IntAct=EBI-3921347, EBI-2510102;
CC P51687; O43186: CRX; NbExp=3; IntAct=EBI-3921347, EBI-748171;
CC P51687; P78358: CTAG1B; NbExp=3; IntAct=EBI-3921347, EBI-1188472;
CC P51687; Q6BCY4-2: CYB5R2; NbExp=3; IntAct=EBI-3921347, EBI-12102608;
CC P51687; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-3921347, EBI-742054;
CC P51687; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-3921347, EBI-399105;
CC P51687; Q9H596: DUSP21; NbExp=3; IntAct=EBI-3921347, EBI-7357329;
CC P51687; O00303: EIF3F; NbExp=3; IntAct=EBI-3921347, EBI-711990;
CC P51687; A6NGS2: ERICH4; NbExp=3; IntAct=EBI-3921347, EBI-18398448;
CC P51687; O00167-2: EYA2; NbExp=3; IntAct=EBI-3921347, EBI-12807776;
CC P51687; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-3921347, EBI-19153639;
CC P51687; O15287: FANCG; NbExp=3; IntAct=EBI-3921347, EBI-81610;
CC P51687; Q8IXW7: FMR1; NbExp=3; IntAct=EBI-3921347, EBI-11976595;
CC P51687; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-3921347, EBI-10242151;
CC P51687; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-3921347, EBI-5916454;
CC P51687; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-3921347, EBI-740641;
CC P51687; Q0VD86: INCA1; NbExp=5; IntAct=EBI-3921347, EBI-6509505;
CC P51687; Q8WYH8: ING5; NbExp=3; IntAct=EBI-3921347, EBI-488533;
CC P51687; Q86U28: ISCA2; NbExp=3; IntAct=EBI-3921347, EBI-10258659;
CC P51687; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-3921347, EBI-712105;
CC P51687; Q2KHM9: KIAA0753; NbExp=3; IntAct=EBI-3921347, EBI-2805604;
CC P51687; Q7Z3Y9: KRT26; NbExp=3; IntAct=EBI-3921347, EBI-12084444;
CC P51687; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-3921347, EBI-3044087;
CC P51687; O76011: KRT34; NbExp=3; IntAct=EBI-3921347, EBI-1047093;
CC P51687; Q6A162: KRT40; NbExp=3; IntAct=EBI-3921347, EBI-10171697;
CC P51687; P61968: LMO4; NbExp=3; IntAct=EBI-3921347, EBI-2798728;
CC P51687; P43364: MAGEA11; NbExp=3; IntAct=EBI-3921347, EBI-739552;
CC P51687; Q96LZ2: MAGEB10; NbExp=5; IntAct=EBI-3921347, EBI-3957156;
CC P51687; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-3921347, EBI-12516603;
CC P51687; Q99750: MDFI; NbExp=3; IntAct=EBI-3921347, EBI-724076;
CC P51687; Q9H204: MED28; NbExp=3; IntAct=EBI-3921347, EBI-514199;
CC P51687; Q99687-3: MEIS3; NbExp=3; IntAct=EBI-3921347, EBI-18582591;
CC P51687; Q6PF18: MORN3; NbExp=3; IntAct=EBI-3921347, EBI-9675802;
CC P51687; Q01449: MYL7; NbExp=3; IntAct=EBI-3921347, EBI-10222416;
CC P51687; O43795: MYO1B; NbExp=3; IntAct=EBI-3921347, EBI-351119;
CC P51687; P37198: NUP62; NbExp=6; IntAct=EBI-3921347, EBI-347978;
CC P51687; P40855: PEX19; NbExp=3; IntAct=EBI-3921347, EBI-594747;
CC P51687; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-3921347, EBI-10232538;
CC P51687; P01189: POMC; NbExp=3; IntAct=EBI-3921347, EBI-12219503;
CC P51687; P54821: PRRX1; NbExp=3; IntAct=EBI-3921347, EBI-12828023;
CC P51687; Q9NZH5-2: PTTG2; NbExp=3; IntAct=EBI-3921347, EBI-17630019;
CC P51687; Q15293: RCN1; NbExp=3; IntAct=EBI-3921347, EBI-948278;
CC P51687; Q04864-2: REL; NbExp=3; IntAct=EBI-3921347, EBI-10829018;
CC P51687; Q96CP1: RELA; NbExp=3; IntAct=EBI-3921347, EBI-10489476;
CC P51687; Q15669: RHOH; NbExp=3; IntAct=EBI-3921347, EBI-1244971;
CC P51687; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-3921347, EBI-726876;
CC P51687; P05386: RPLP1; NbExp=3; IntAct=EBI-3921347, EBI-354582;
CC P51687; Q96LW2: RSKR; NbExp=3; IntAct=EBI-3921347, EBI-1054572;
CC P51687; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-3921347, EBI-6257312;
CC P51687; Q9UJW9: SERTAD3; NbExp=5; IntAct=EBI-3921347, EBI-748621;
CC P51687; O43765: SGTA; NbExp=3; IntAct=EBI-3921347, EBI-347996;
CC P51687; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-3921347, EBI-747389;
CC P51687; Q96H20: SNF8; NbExp=5; IntAct=EBI-3921347, EBI-747719;
CC P51687; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-3921347, EBI-12288855;
CC P51687; Q8NBT2: SPC24; NbExp=3; IntAct=EBI-3921347, EBI-999900;
CC P51687; P51692: STAT5B; NbExp=3; IntAct=EBI-3921347, EBI-1186119;
CC P51687; Q8IWL8: STH; NbExp=3; IntAct=EBI-3921347, EBI-12843506;
CC P51687; Q9H668: STN1; NbExp=3; IntAct=EBI-3921347, EBI-746930;
CC P51687; Q96PV0: SYNGAP1; NbExp=3; IntAct=EBI-3921347, EBI-2682386;
CC P51687; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-3921347, EBI-12090309;
CC P51687; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-3921347, EBI-492476;
CC P51687; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-3921347, EBI-10259086;
CC P51687; Q86WV8: TSC1; NbExp=3; IntAct=EBI-3921347, EBI-12806590;
CC P51687; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-3921347, EBI-947187;
CC P51687; Q8IWV8-2: UBR2; NbExp=3; IntAct=EBI-3921347, EBI-17923957;
CC P51687; P61758: VBP1; NbExp=3; IntAct=EBI-3921347, EBI-357430;
CC P51687; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-3921347, EBI-12146727;
CC P51687; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-3921347, EBI-11419867;
CC P51687; P52747: ZNF143; NbExp=3; IntAct=EBI-3921347, EBI-2849334;
CC P51687; Q8N1W2: ZNF710; NbExp=3; IntAct=EBI-3921347, EBI-18096911;
CC P51687; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-3921347, EBI-1538838;
CC P51687; Q6ZN96; NbExp=3; IntAct=EBI-3921347, EBI-10255097;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q07116}.
CC -!- DISEASE: Sulfite oxidase deficiency, isolated (ISOD) [MIM:272300]: A
CC life-threatening, autosomal recessive neurometabolic disorder
CC characterized by severe neurological impairment. Classic ISOD manifests
CC in the first few hours to days of life and is characterized by
CC intractable seizures, feeding difficulties, rapidly progressive
CC encephalopathy, microcephaly, and profound intellectual disability.
CC Children usually die during the first few months of life. Mild ISOD
CC manifests in infancy or early childhood and is characterized by ectopia
CC lentis that is variably present, developmental delay and regression,
CC movement disorder characterized by dystonia and choreoathetosis,
CC ataxia, and rarely acute hemiplegia due to metabolic stroke.
CC {ECO:0000269|PubMed:10519592, ECO:0000269|PubMed:12112661,
CC ECO:0000269|PubMed:12368985, ECO:0000269|PubMed:9428520,
CC ECO:0000269|PubMed:9600976}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74886.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL08048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L31573; AAA74886.1; ALT_INIT; mRNA.
DR EMBL; BC065193; AAH65193.2; -; mRNA.
DR EMBL; AY056018; AAL08048.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS8901.2; -.
DR PIR; S55874; S55874.
DR RefSeq; NP_000447.2; NM_000456.2.
DR RefSeq; NP_001027558.1; NM_001032386.1.
DR RefSeq; NP_001027559.1; NM_001032387.1.
DR RefSeq; XP_016875396.1; XM_017019907.1.
DR RefSeq; XP_016875397.1; XM_017019908.1.
DR PDB; 1MJ4; X-ray; 1.20 A; A=79-160.
DR PDBsum; 1MJ4; -.
DR AlphaFoldDB; P51687; -.
DR SMR; P51687; -.
DR BioGRID; 112690; 97.
DR IntAct; P51687; 91.
DR STRING; 9606.ENSP00000377668; -.
DR DrugBank; DB03983; {[2-Amino-4-oxo-6,7-di(sulfanyl-KappaS)-3,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2-) phosphate}(dioxo)sulfanylmolybdenum.
DR iPTMnet; P51687; -.
DR PhosphoSitePlus; P51687; -.
DR BioMuta; SUOX; -.
DR DMDM; 152031695; -.
DR EPD; P51687; -.
DR jPOST; P51687; -.
DR MassIVE; P51687; -.
DR MaxQB; P51687; -.
DR PaxDb; P51687; -.
DR PeptideAtlas; P51687; -.
DR PRIDE; P51687; -.
DR ProteomicsDB; 56372; -.
DR Antibodypedia; 27840; 385 antibodies from 29 providers.
DR DNASU; 6821; -.
DR Ensembl; ENST00000266971.8; ENSP00000266971.3; ENSG00000139531.13.
DR Ensembl; ENST00000356124.8; ENSP00000348440.4; ENSG00000139531.13.
DR Ensembl; ENST00000394109.7; ENSP00000377668.3; ENSG00000139531.13.
DR Ensembl; ENST00000394115.6; ENSP00000377674.2; ENSG00000139531.13.
DR Ensembl; ENST00000548274.5; ENSP00000450245.1; ENSG00000139531.13.
DR Ensembl; ENST00000550065.1; ENSP00000450264.1; ENSG00000139531.13.
DR GeneID; 6821; -.
DR KEGG; hsa:6821; -.
DR MANE-Select; ENST00000266971.8; ENSP00000266971.3; NM_001032386.2; NP_001027558.1.
DR UCSC; uc001six.4; human.
DR CTD; 6821; -.
DR DisGeNET; 6821; -.
DR GeneCards; SUOX; -.
DR GeneReviews; SUOX; -.
DR HGNC; HGNC:11460; SUOX.
DR HPA; ENSG00000139531; Low tissue specificity.
DR MalaCards; SUOX; -.
DR MIM; 272300; phenotype.
DR MIM; 606887; gene.
DR neXtProt; NX_P51687; -.
DR OpenTargets; ENSG00000139531; -.
DR Orphanet; 99731; Isolated sulfite oxidase deficiency.
DR PharmGKB; PA36250; -.
DR VEuPathDB; HostDB:ENSG00000139531; -.
DR eggNOG; KOG0535; Eukaryota.
DR eggNOG; KOG4576; Eukaryota.
DR GeneTree; ENSGT00390000003749; -.
DR HOGENOM; CLU_003827_5_1_1; -.
DR InParanoid; P51687; -.
DR OMA; WARHVQF; -.
DR OrthoDB; 804989at2759; -.
DR PhylomeDB; P51687; -.
DR TreeFam; TF300905; -.
DR BioCyc; MetaCyc:HS06627-MON; -.
DR BRENDA; 1.8.3.1; 2681.
DR PathwayCommons; P51687; -.
DR Reactome; R-HSA-1614517; Sulfide oxidation to sulfate.
DR SABIO-RK; P51687; -.
DR SignaLink; P51687; -.
DR UniPathway; UPA00096; -.
DR BioGRID-ORCS; 6821; 17 hits in 1080 CRISPR screens.
DR ChiTaRS; SUOX; human.
DR EvolutionaryTrace; P51687; -.
DR GeneWiki; Sulfite_oxidase; -.
DR GenomeRNAi; 6821; -.
DR Pharos; P51687; Tbio.
DR PRO; PR:P51687; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P51687; protein.
DR Bgee; ENSG00000139531; Expressed in right lobe of liver and 180 other tissues.
DR ExpressionAtlas; P51687; baseline and differential.
DR Genevisible; P51687; HS.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IBA:GO_Central.
DR GO; GO:0008482; F:sulfite oxidase activity; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.90.420.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR022407; OxRdtase_Mopterin_BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Epilepsy; Heme; Intellectual disability;
KW Iron; Metal-binding; Mitochondrion; Molybdenum; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..79
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q07116"
FT CHAIN 80..545
FT /note="Sulfite oxidase, mitochondrial"
FT /id="PRO_0000006481"
FT DOMAIN 82..161
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 165..174
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 175..401
FT /note="Moco domain"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT REGION 402..538
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 118
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12832761"
FT BINDING 143
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12832761"
FT BINDING 145
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:12832761"
FT BINDING 147
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:12832761"
FT BINDING 215..219
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 264
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 322
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 361
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 366
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT BINDING 377..379
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000250|UniProtKB:P07850"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 217
FT /note="R -> Q (in ISOD; 2% of activity; dbSNP:rs121908007)"
FT /evidence="ECO:0000269|PubMed:12368985,
FT ECO:0000269|PubMed:9428520, ECO:0000269|PubMed:9600976"
FT /id="VAR_002200"
FT VARIANT 258
FT /note="I -> L (in ISOD)"
FT /evidence="ECO:0000269|PubMed:12112661"
FT /id="VAR_015724"
FT VARIANT 265
FT /note="A -> D (in ISOD; dbSNP:rs121908008)"
FT /evidence="ECO:0000269|PubMed:10519592,
FT ECO:0000269|PubMed:9428520"
FT /id="VAR_002201"
FT VARIANT 268
FT /note="R -> Q (in ISOD; dbSNP:rs1041681662)"
FT /evidence="ECO:0000269|PubMed:12112661"
FT /id="VAR_015725"
FT VARIANT 362
FT /note="G -> S (in ISOD; dbSNP:rs757559168)"
FT /evidence="ECO:0000269|PubMed:12112661"
FT /id="VAR_015726"
FT VARIANT 366
FT /note="R -> H (in ISOD; dbSNP:rs776690106)"
FT /evidence="ECO:0000269|PubMed:12112661"
FT /id="VAR_015727"
FT VARIANT 379
FT /note="K -> R (in ISOD; dbSNP:rs777114729)"
FT /evidence="ECO:0000269|PubMed:12112661"
FT /id="VAR_015728"
FT VARIANT 396
FT /note="Q -> R (in ISOD)"
FT /evidence="ECO:0000269|PubMed:12112661"
FT /id="VAR_015729"
FT VARIANT 427
FT /note="S -> Y (in ISOD)"
FT /evidence="ECO:0000269|PubMed:10519592,
FT ECO:0000269|PubMed:9428520"
FT /id="VAR_002202"
FT VARIANT 450
FT /note="W -> R (in ISOD)"
FT /evidence="ECO:0000269|PubMed:12112661"
FT /id="VAR_015730"
FT VARIANT 530
FT /note="G -> D (in ISOD; dbSNP:rs121908009)"
FT /evidence="ECO:0000269|PubMed:9428520"
FT /id="VAR_002203"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1MJ4"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1MJ4"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1MJ4"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1MJ4"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1MJ4"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:1MJ4"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:1MJ4"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1MJ4"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1MJ4"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1MJ4"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:1MJ4"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1MJ4"
SQ SEQUENCE 545 AA; 60283 MW; 39B842C55D39E11F CRC64;
MLLLHRAVVL RLQQACRLKS IPSRICIQAC STNDSFQPQR PSLTFSGDNS STQGWRVMGT
LLGLGAVLAY QDHRCRAAQE STHIYTKEEV SSHTSPETGI WVTLGSEVFD VTEFVDLHPG
GPSKLMLAAG GPLEPFWALY AVHNQSHVRE LLAQYKIGEL NPEDKVAPTV ETSDPYADDP
VRHPALKVNS QRPFNAEPPP ELLTENYITP NPIFFTRNHL PVPNLDPDTY RLHVVGAPGG
QSLSLSLDDL HNFPRYEITV TLQCAGNRRS EMTQVKEVKG LEWRTGAIST ARWAGARLCD
VLAQAGHQLC ETEAHVCFEG LDSDPTGTAY GASIPLARAM DPEAEVLLAY EMNGQPLPRD
HGFPVRVVVP GVVGARHVKW LGRVSVQPEE SYSHWQRRDY KGFSPSVDWE TVDFDSAPSI
QELPVQSAIT EPRDGETVES GEVTIKGYAW SGGGRAVIRV DVSLDGGLTW QVAKLDGEEQ
RPRKAWAWRL WQLKAPVPAG QKELNIVCKA VDDGYNVQPD TVAPIWNLRG VLSNAWHRVH
VYVSP
