SQOR_DICDI
ID SQOR_DICDI Reviewed; 452 AA.
AC Q54DK1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial {ECO:0000250|UniProtKB:Q9Y6N5};
DE EC=1.8.5.8 {ECO:0000250|UniProtKB:Q9Y6N5};
DE Flags: Precursor;
GN Name=sqor {ECO:0000250|UniProtKB:Q9Y6N5};
GN Synonyms=sqrdl {ECO:0000250|UniProtKB:Q9Y6N5}; ORFNames=DDB_G0292250;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the help of
CC a quinone. {ECO:0000250|UniProtKB:Q9Y6N5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + hydrogen sulfide + sulfite + ubiquinone-10 =
CC thiosulfate + ubiquinol-10; Xref=Rhea:RHEA:38359, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:33542,
CC ChEBI:CHEBI:46245, ChEBI:CHEBI:64183;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + glutathione + H(+) + hydrogen sulfide = a quinol +
CC S-sulfanylglutathione; Xref=Rhea:RHEA:55156, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29919, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58905, ChEBI:CHEBI:132124; EC=1.8.5.8;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6N5};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q9Y6N5};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9Y6N5}.
CC -!- SIMILARITY: Belongs to the SQRD family. {ECO:0000305}.
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DR EMBL; AAFI02000188; EAL61335.1; -; Genomic_DNA.
DR RefSeq; XP_629726.1; XM_629724.1.
DR AlphaFoldDB; Q54DK1; -.
DR SMR; Q54DK1; -.
DR STRING; 44689.DDB0252562; -.
DR PaxDb; Q54DK1; -.
DR EnsemblProtists; EAL61335; EAL61335; DDB_G0292250.
DR GeneID; 8628554; -.
DR KEGG; ddi:DDB_G0292250; -.
DR dictyBase; DDB_G0292250; sqrdl.
DR eggNOG; KOG3851; Eukaryota.
DR HOGENOM; CLU_030742_2_0_1; -.
DR InParanoid; Q54DK1; -.
DR OMA; FPWVYYN; -.
DR PhylomeDB; Q54DK1; -.
DR PRO; PR:Q54DK1; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0070224; F:sulfide:quinone oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042762; P:regulation of sulfur metabolic process; ISS:dictyBase.
DR GO; GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR015904; Sulphide_quinone_reductase.
DR PANTHER; PTHR10632; PTHR10632; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Quinone;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..452
FT /note="Sulfide:quinone oxidoreductase, mitochondrial"
FT /id="PRO_0000328203"
FT ACT_SITE 204
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT ACT_SITE 380
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 54..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT BINDING 345..348
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
FT DISULFID 204..380
FT /evidence="ECO:0000250|UniProtKB:Q9Y6N5"
SQ SEQUENCE 452 AA; 50145 MW; 2F9F8A1DF3B2A06D CRC64;
MFKSIMYALA VAPAVTSSSD KLPNGVVSAS QLGSEKEKRK LKNVTKIVIV GGGAGGLSVA
SQLEHKFKNK GDIVIVEPSE KHYYQPLWTL VGGGIFSRKD SEKDEKDFIP KGATWVKDSV
TVFKPEENIV LTKDGKEIDY DYLVVSTGLE LYWDRVKGLK ENLGKNGVTS NYSYDSCEKT
FEFIKSLKPG NVAIFTVPTT GVKCGGAPQK ILWLCDDYLR KHGIRDKVRL DFNSAGASMF
PVKKYSEVLD KMAKERGVNQ NFAHNLVEIK GDSKEAVFET PQGNKTVKYD MIHVVPPMGP
HSVIKNSPLA DPATGFVNVD KGTLQHVKYD NVFSLGDTSN LPTSKTAAAI TSQAPILVGN
LINHKLGLPL NHKYDGYTSC PITTSYSKII LAEFKYGFEV DESLPFDQSK ESYFPMFLKK
YVFPTAYWEG MLKGRWFGKN TLFNPIKTPE IN
