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Protein

Sulfite oxidase, mitochondrial

Gene

Suox

Organism
Rattus norvegicus (Rat)
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:
  • heme b1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per subunit.1 Publication
  • Mo-molybdopterin1 PublicationNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.1 Publication

Pathwayi: sulfur metabolism

This protein is involved in the pathway sulfur metabolism, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway sulfur metabolism and in Energy metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191Iron (heme axial ligand)PROSITE-ProRule annotation
Metal bindingi144 – 1441Iron (heme axial ligand)PROSITE-ProRule annotation
Binding sitei146 – 1461Heme bBy similarity
Binding sitei148 – 1481Heme bBy similarity
Metal bindingi265 – 2651MolybdenumBy similarity
Binding sitei323 – 3231MolybdopterinBy similarity
Binding sitei362 – 3621MolybdopterinBy similarity
Binding sitei367 – 3671MolybdopterinBy similarity

GO - Molecular functioni

  • heme binding Source: RGD
  • molybdenum ion binding Source: InterPro
  • molybdopterin cofactor binding Source: RGD
  • sulfite oxidase activity Source: RGD

GO - Biological processi

  • nitrate assimilation Source: InterPro
  • response to nutrient Source: RGD
  • sulfur compound metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, Molybdenum

Enzyme and pathway databases

UniPathwayiUPA00096.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite oxidase, mitochondrial (EC:1.8.3.1)
Gene namesi
Name:Suox
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619994. Suox.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • mitochondrial intermembrane space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8080MitochondrionAdd
BLAST
Chaini81 – 546466Sulfite oxidase, mitochondrialPRO_0000006484Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ07116.
PRIDEiQ07116.

PTM databases

iPTMnetiQ07116.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008018.

Structurei

3D structure databases

ProteinModelPortaliQ07116.
SMRiQ07116. Positions 86-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 16280Cytochrome b5 heme-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 17510HingeBy similarity
Regioni176 – 402227Moco domainBy similarityAdd
BLAST
Regioni216 – 2205Molybdopterin-bindingBy similarity
Regioni378 – 3803Molybdopterin-bindingBy similarity
Regioni403 – 539137HomodimerizationBy similarityAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0535. Eukaryota.
KOG4576. Eukaryota.
COG2041. LUCA.
HOGENOMiHOG000252609.
HOVERGENiHBG017865.
InParanoidiQ07116.
KOiK00387.
PhylomeDBiQ07116.

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.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
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.

Q07116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPRLYRSVA VGLPRAIRAK STPLRLCIQA CSSSDSLKPQ HPSLTFSDDN
60 70 80 90 100
SRTRGWKVMG TLIGLGAVLA YHDHRCRASQ ESPRIYSKED VRSHNNLKTG
110 120 130 140 150
VWVTLGSEVF DVTKFVDLHP GGQSKLMLAA GGPLEPFWAL YAVHNQPHVR
160 170 180 190 200
ELLAEYKIGE LNPEDRMSPP LEASDPYSND PMRHPALRIN SQRPFNAEPP
210 220 230 240 250
PELLTESYIT PNPIFFTRNH LPVPNLDPDT YRLHVVGAPG GQSLSLSLDD
260 270 280 290 300
LHKFPKHEVT VTLQCAGNRR SEMNKVKEVK GLEWRTGAIS TARWAGARLC
310 320 330 340 350
DVLAQAGHRL RETEAHVCFE GLDSDPTGTA YGASIPLARA MDPQAEVLLA
360 370 380 390 400
YEMNGQPLPR DHGFPVRVVV PGVVGARHVK WLGRVSVESE ESYSHWQRRD
410 420 430 440 450
YKGFSPSVDW DTVDFDLAPS IQELPIQSAI TQPQDGTTVE SGEVIIKGYA
460 470 480 490 500
WSGGGRAVIR VDVSMDGGLT WQEAELEGEE QHPRKAWAWR IWQLKAHVPA
510 520 530 540
EQKELNIICK AVDDSYNVQP DTVAPIWNLR GVLSNAWHRV HVQVVP
Length:546
Mass (Da):60,806
Last modified:July 10, 2007 - v2
Checksum:iB4A4E46A8F15765D
GO

Sequence cautioni

The sequence AAA16618.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981K → Q in AAA16618 (PubMed:8276806).Curated
Sequence conflicti178 – 1781S → T AA sequence (PubMed:2249998).Curated
Sequence conflicti294 – 2941W → R AA sequence (PubMed:2249998).Curated
Sequence conflicti318 – 3181C → Q AA sequence (PubMed:2249998).Curated
Sequence conflicti338 – 3381A → G AA sequence (PubMed:2249998).Curated
Sequence conflicti362 – 3621H → S AA sequence (PubMed:2249998).Curated
Sequence conflicti362 – 3621H → S AA sequence (PubMed:3393528).Curated
Sequence conflicti394 – 3963SHW → HYL AA sequence (PubMed:2249998).Curated
Sequence conflicti432 – 4321Q → V AA sequence (PubMed:2249998).Curated
Sequence conflicti514 – 5141D → A AA sequence (PubMed:2249998).Curated
Sequence conflicti527 – 5271W → A AA sequence (PubMed:2249998).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061991 mRNA. Translation: AAH61991.2.
L05084 mRNA. Translation: AAA16618.1. Different initiation.
PIRiA53107.
RefSeqiNP_112389.3. NM_031127.3.
UniGeneiRn.25720.

Genome annotation databases

GeneIDi81805.
KEGGirno:81805.
UCSCiRGD:619994. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061991 mRNA. Translation: AAH61991.2.
L05084 mRNA. Translation: AAA16618.1. Different initiation.
PIRiA53107.
RefSeqiNP_112389.3. NM_031127.3.
UniGeneiRn.25720.

3D structure databases

ProteinModelPortaliQ07116.
SMRiQ07116. Positions 86-544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008018.

PTM databases

iPTMnetiQ07116.

Proteomic databases

PaxDbiQ07116.
PRIDEiQ07116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81805.
KEGGirno:81805.
UCSCiRGD:619994. rat.

Organism-specific databases

CTDi6821.
RGDi619994. Suox.

Phylogenomic databases

eggNOGiKOG0535. Eukaryota.
KOG4576. Eukaryota.
COG2041. LUCA.
HOGENOMiHOG000252609.
HOVERGENiHBG017865.
InParanoidiQ07116.
KOiK00387.
PhylomeDBiQ07116.

Enzyme and pathway databases

UniPathwayiUPA00096.

Miscellaneous databases

PROiQ07116.

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.
SMARTiSM01117. Cyt-b5. 1 hit.
[Graphical view]
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. "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: Prostate.
  2. "Molecular cloning of rat liver sulfite oxidase. Expression of a eukaryotic Mo-pterin-containing enzyme in Escherichia coli."
    Garrett R.M., Rajagopalan K.V.
    J. Biol. Chem. 269:272-276(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 43-546, COFACTOR.
    Tissue: Liver.
  3. "A conserved cysteine in molybdenum oxotransferases."
    Barber M.J., Neame P.J.
    J. Biol. Chem. 265:20912-20915(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 98-253; 256-275; 280-433; 485-495 AND 503-537.
    Tissue: Liver.
  4. "Sequence and nitrate regulation of the Arabidopsis thaliana mRNA encoding nitrate reductase, a metalloflavoprotein with three functional domains."
    Crawford N.M., Smith M., Bellissimo D.B., Davis R.W.
    Proc. Natl. Acad. Sci. U.S.A. 85:5006-5010(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 187-201 AND 340-368.
    Tissue: Liver.
  5. Maurya D.K., Bhargava P.
    Submitted (DEC-2008) to UniProtKB
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSUOX_RAT
AccessioniPrimary (citable) accession number: Q07116
Secondary accession number(s): Q6P6W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 10, 2007
Last modified: June 8, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.