SQRD_AQUAE
ID SQRD_AQUAE Reviewed; 430 AA.
AC O67931;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Sulfide-quinone reductase;
DE Short=SQR;
DE EC=1.8.5.4 {ECO:0000303|PubMed:10816041, ECO:0000303|PubMed:19487671};
DE AltName: Full=Sulfide:quinone oxidoreductase {ECO:0000303|PubMed:10816041, ECO:0000303|PubMed:19487671};
GN Name=sqr {ECO:0000312|EMBL:AAC07903.1};
GN OrderedLocusNames=aq_2186 {ECO:0000312|EMBL:AAC07903.1};
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP SUBCELLULAR LOCATION, IDENTIFICATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10816041; DOI=10.1007/s002030000135;
RA Nuebel T., Klughammer C., Huber R., Hauska G., Schuetz M.;
RT "Sulfide:quinone oxidoreductase in membranes of the hyperthermophilic
RT bacterium Aquifex aeolicus (VF5).";
RL Arch. Microbiol. 173:233-244(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FAD AND UBIQUINONE
RP ANALOG, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DISULFIDE BOND.
RX PubMed=19487671; DOI=10.1073/pnas.0904165106;
RA Marcia M., Ermler U., Peng G., Michel H.;
RT "The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis
RT to understand sulfide detoxification and respiration.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9625-9630(2009).
CC -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the help of
CC a quinone. Consecutive reaction cycles lead to the accumulation of a
CC polysulfide product on the active site Cys residues; these products are
CC released when they exceed a critical length, typically as
CC cyclooctasulfur. {ECO:0000303|PubMed:10816041,
CC ECO:0000303|PubMed:19487671}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n a quinone + n H(+) + n hydrogen sulfide = n a quinol + n
CC sulfur; Xref=Rhea:RHEA:30239, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:26833, ChEBI:CHEBI:29919, ChEBI:CHEBI:132124; EC=1.8.5.4;
CC Evidence={ECO:0000303|PubMed:10816041, ECO:0000303|PubMed:19487671};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19487671};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:19487671};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:19487671}.
CC -!- INTERACTION:
CC O67931; O67931: sqr; NbExp=2; IntAct=EBI-15785206, EBI-15785206;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10816041,
CC ECO:0000269|PubMed:19487671}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10816041, ECO:0000269|PubMed:19487671}.
CC -!- SIMILARITY: Belongs to the SQRD family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07903.1; -; Genomic_DNA.
DR PIR; G70487; G70487.
DR RefSeq; NP_214500.1; NC_000918.1.
DR RefSeq; WP_010881436.1; NC_000918.1.
DR PDB; 3HYV; X-ray; 2.30 A; A/B/C/D/E/F=1-430.
DR PDB; 3HYW; X-ray; 2.00 A; A/B/C/D/E/F=1-430.
DR PDB; 3HYX; X-ray; 2.90 A; A/B/C/D/E/F=1-430.
DR PDBsum; 3HYV; -.
DR PDBsum; 3HYW; -.
DR PDBsum; 3HYX; -.
DR AlphaFoldDB; O67931; -.
DR SMR; O67931; -.
DR DIP; DIP-48896N; -.
DR STRING; 224324.aq_2186; -.
DR DrugBank; DB07640; 2-decyl-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione.
DR EnsemblBacteria; AAC07903; AAC07903; aq_2186.
DR KEGG; aae:aq_2186; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_030742_5_2_0; -.
DR InParanoid; O67931; -.
DR OMA; PPRNVNW; -.
DR OrthoDB; 403436at2; -.
DR BRENDA; 1.8.5.4; 396.
DR EvolutionaryTrace; O67931; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0070224; F:sulfide:quinone oxidoreductase activity; IEA:RHEA.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; FAD; Flavoprotein; Membrane;
KW Nucleotide-binding; Oxidoreductase; Quinone; Reference proteome.
FT CHAIN 1..430
FT /note="Sulfide-quinone reductase"
FT /id="PRO_0000430824"
FT ACT_SITE 156
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7ZAG8,
FT ECO:0000303|PubMed:19487671"
FT ACT_SITE 347
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7ZAG8,
FT ECO:0000303|PubMed:19487671"
FT BINDING 9..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19487671"
FT BINDING 34..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19487671"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19487671"
FT BINDING 105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19487671"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19487671"
FT BINDING 314
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19487671"
FT BINDING 346
FT /ligand="a quinone"
FT /ligand_id="ChEBI:CHEBI:132124"
FT /evidence="ECO:0000269|PubMed:19487671"
FT BINDING 382
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19487671"
FT DISULFID 280..422
FT /evidence="ECO:0000269|PubMed:19487671"
FT DISULFID 419..430
FT /evidence="ECO:0000269|PubMed:19487671"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3HYW"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3HYW"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 158..173
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3HYW"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:3HYW"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:3HYW"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 314..332
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 352..366
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 377..395
FT /evidence="ECO:0007829|PDB:3HYW"
FT HELIX 401..411
FT /evidence="ECO:0007829|PDB:3HYW"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:3HYW"
SQ SEQUENCE 430 AA; 47449 MW; 7489B07FADEAA9A8 CRC64;
MAKHVVVIGG GVGGIATAYN LRNLMPDLKI TLISDRPYFG FTPAFPHLAM GWRKFEDISV
PLAPLLPKFN IEFINEKAES IDPDANTVTT QSGKKIEYDY LVIATGPKLV FGAEGQEENS
TSICTAEHAL ETQKKLQELY ANPGPVVIGA IPGVSCFGPA YEFALMLHYE LKKRGIRYKV
PMTFITSEPY LGHFGVGGIG ASKRLVEDLF AERNIDWIAN VAVKAIEPDK VIYEDLNGNT
HEVPAKFTMF MPSFQGPEVV ASAGDKVANP ANKMVIVNRC FQNPTYKNIF GVGVVTAIPP
IEKTPIPTGV PKTGMMIEQM AMAVAHNIVN DIRNNPDKYA PRLSAICIAD FGEDAGFFFA
DPVIPPRERV ITKMGKWAHY FKTAFEKYFL WKVRNGNIAP SFEEKVLEIF LKVHPIELCK
DCEGAPGSRC
