SQRD_ACIF2
ID SQRD_ACIF2 Reviewed; 434 AA.
AC B7JBP8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Sulfide-quinone reductase;
DE Short=SQR;
DE EC=1.8.5.4 {ECO:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586};
DE AltName: Full=Sulfide:quinone oxidoreductase;
GN OrderedLocusNames=AFE_1792 {ECO:0000312|EMBL:ACK80359.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH FAD; UBIQUINONE AND
RP HYDROGEN SULFIDE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR,
RP SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-128; CYS-160 AND CYS-356.
RX PubMed=20303979; DOI=10.1016/j.jmb.2010.03.018;
RA Cherney M.M., Zhang Y., Solomonson M., Weiner J.H., James M.N.;
RT "Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus
RT ferrooxidans: insights into sulfidotrophic respiration and
RT detoxification.";
RL J. Mol. Biol. 398:292-305(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-434 IN COMPLEX WITH FAD;
RP UBIQUINONE AND HYDROGEN SULFIDE, ACTIVE SITE, AND MUTAGENESIS OF SER-126;
RP CYS-128; HIS-132; CYS-160; HIS-198 AND CYS-356.
RX PubMed=22542586; DOI=10.1016/j.jsb.2012.04.007;
RA Cherney M.M., Zhang Y., James M.N., Weiner J.H.;
RT "Structure-activity characterization of sulfide:quinone oxidoreductase
RT variants.";
RL J. Struct. Biol. 178:319-328(2012).
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:0000269|PubMed:20303979,
CC ECO:0000269|PubMed:22542586}.
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:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20303979, ECO:0000269|PubMed:22542586};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:20303979,
CC ECO:0000269|PubMed:22542586};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 uM for sodium sulfide {ECO:0000269|PubMed:20303979};
CC KM=22 uM for decylubiquinone {ECO:0000269|PubMed:20303979};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20303979}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000303|PubMed:20303979};
CC Peripheral membrane protein {ECO:0000303|PubMed:20303979}.
CC -!- SIMILARITY: Belongs to the SQRD family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001219; ACK80359.1; -; Genomic_DNA.
DR RefSeq; WP_012536761.1; NC_011761.1.
DR PDB; 3KPK; X-ray; 2.05 A; A=1-434.
DR PDB; 3SX6; X-ray; 1.80 A; A=2-434.
DR PDB; 3SXI; X-ray; 2.18 A; A=2-434.
DR PDB; 3SY4; X-ray; 1.91 A; A=2-434.
DR PDB; 3SYI; X-ray; 2.20 A; A=2-434.
DR PDB; 3SZ0; X-ray; 2.15 A; A=2-434.
DR PDB; 3SZC; X-ray; 2.20 A; A=2-434.
DR PDB; 3SZF; X-ray; 2.10 A; A=2-434.
DR PDB; 3SZW; X-ray; 2.20 A; A=2-434.
DR PDB; 3T0K; X-ray; 2.00 A; A=2-434.
DR PDB; 3T14; X-ray; 2.21 A; A=2-434.
DR PDB; 3T2K; X-ray; 2.35 A; A=2-434.
DR PDB; 3T2Y; X-ray; 2.50 A; A=1-434.
DR PDB; 3T2Z; X-ray; 2.30 A; A/B=2-434.
DR PDB; 3T31; X-ray; 2.30 A; A=2-434.
DR PDBsum; 3KPK; -.
DR PDBsum; 3SX6; -.
DR PDBsum; 3SXI; -.
DR PDBsum; 3SY4; -.
DR PDBsum; 3SYI; -.
DR PDBsum; 3SZ0; -.
DR PDBsum; 3SZC; -.
DR PDBsum; 3SZF; -.
DR PDBsum; 3SZW; -.
DR PDBsum; 3T0K; -.
DR PDBsum; 3T14; -.
DR PDBsum; 3T2K; -.
DR PDBsum; 3T2Y; -.
DR PDBsum; 3T2Z; -.
DR PDBsum; 3T31; -.
DR AlphaFoldDB; B7JBP8; -.
DR SMR; B7JBP8; -.
DR STRING; 243159.AFE_1792; -.
DR DrugBank; DB07640; 2-decyl-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione.
DR PaxDb; B7JBP8; -.
DR EnsemblBacteria; ACK80359; ACK80359; AFE_1792.
DR GeneID; 66432574; -.
DR KEGG; afr:AFE_1792; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_030742_5_2_6; -.
DR OMA; PPRNVNW; -.
DR OrthoDB; 403436at2; -.
DR BRENDA; 1.8.5.4; 91.
DR EvolutionaryTrace; B7JBP8; -.
DR Proteomes; UP000001362; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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; FAD; Flavoprotein; Membrane; Nucleotide-binding;
KW Oxidoreductase; Quinone; Reference proteome.
FT CHAIN 1..434
FT /note="Sulfide-quinone reductase"
FT /id="PRO_0000430825"
FT ACT_SITE 160
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT ACT_SITE 356
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT BINDING 8..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT BINDING 77..78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT BINDING 322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT BINDING 391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT MUTAGEN 126
FT /note="S->A: No effect on FAD reduction. Strongly reduced
FT activity with decylubiquinone."
FT /evidence="ECO:0000269|PubMed:22542586"
FT MUTAGEN 128
FT /note="C->A: No effect on FAD reduction. Strongly reduced
FT activity with decylubiquinone."
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT MUTAGEN 128
FT /note="C->S: No effect on FAD reduction. Abolishes activity
FT with decylubiquinone."
FT /evidence="ECO:0000269|PubMed:22542586"
FT MUTAGEN 132
FT /note="H->A: No effect on FAD reduction. Reduced activity
FT with decylubiquinone."
FT /evidence="ECO:0000269|PubMed:22542586"
FT MUTAGEN 160
FT /note="C->A: Strongly reduces FAD reduction. Abolishes
FT activity with decylubiquinone."
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT MUTAGEN 198
FT /note="H->A: No effect on FAD reduction. Reduced activity
FT with decylubiquinone."
FT /evidence="ECO:0000269|PubMed:22542586"
FT MUTAGEN 356
FT /note="C->A: Complete loss of enzyme activity. Abolishes
FT enzyme FAD reduction. Abolishes activity with
FT decylubiquinone."
FT /evidence="ECO:0000269|PubMed:20303979,
FT ECO:0000269|PubMed:22542586"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:3SX6"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3SX6"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3T0K"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3SX6"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:3SX6"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:3T0K"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:3SX6"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 322..339
FT /evidence="ECO:0007829|PDB:3SX6"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 364..375
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:3SX6"
FT HELIX 385..404
FT /evidence="ECO:0007829|PDB:3SX6"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:3SY4"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:3SX6"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:3T2Z"
SQ SEQUENCE 434 AA; 47406 MW; FEADC108550141FB CRC64;
MAHVVILGAG TGGMPAAYEM KEALGSGHEV TLISANDYFQ FVPSNPWVGV GWKERDDIAF
PIRHYVERKG IHFIAQSAEQ IDAEAQNITL ADGNTVHYDY LMIATGPKLA FENVPGSDPH
EGPVQSICTV DHAERAFAEY QALLREPGPI VIGAMAGASC FGPAYEYAMI VASDLKKRGM
RDKIPSFTFI TSEPYIGHLG IQGVGDSKGI LTKGLKEEGI EAYTNCKVTK VEDNKMYVTQ
VDEKGETIKE MVLPVKFGMM IPAFKGVPAV AGVEGLCNPG GFVLVDEHQR SKKYANIFAA
GIAIAIPPVE TTPVPTGAPK TGYMIESMVS AAVHNIKADL EGRKGEQTMG TWNAVCFADM
GDRGAAFIAL PQLKPRKVDV FAYGRWVHLA KVAFEKYFIR KMKMGVSEPF YEKVLFKMMG
ITRLKEEDTH RKAS
