ID SOR_ACIAM Reviewed; 309 AA. AC P29082; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 102. DE RecName: Full=Sulfur oxygenase/reductase; DE EC=1.13.11.55; DE AltName: Full=Sulfur oxygenase reductase; DE Short=SOR; GN Name=sor; OS Acidianus ambivalens (Desulfurolobus ambivalens). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Acidianus. OX NCBI_TaxID=2283; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29. RC STRAIN=Lei 10 / DSM 3772 / JCM 9191; RX PubMed=1522063; DOI=10.1128/jb.174.18.5854-5859.1992; RA Kletzin A.; RT "Molecular characterization of the sor gene, which encodes the sulfur RT oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus RT ambivalens."; RL J. Bacteriol. 174:5854-5859(1992). RN [2] RP FUNCTION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RP ACTIVITY REGULATION, AND SUBUNIT. RX PubMed=15030315; DOI=10.1042/bj20040003; RA Urich T., Bandeiras T.M., Leal S.S., Rachel R., Albrecht T., Zimmermann P., RA Scholz C., Teixeira M., Gomes C.M., Kletzin A.; RT "The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric RT protein containing a low-potential mononuclear non-haem iron centre."; RL Biochem. J. 381:137-146(2004). RN [3] RP MUTAGENESIS OF CYS-31; HIS-86; HIS-90; CYS-101; CYS-104 AND GLU-114. RX PubMed=15970399; DOI=10.1016/j.femsle.2005.05.031; RA Urich T., Kroke A., Bauer C., Seyfarth K., Reuff M., Kletzin A.; RT "Identification of core active site residues of the sulfur oxygenase RT reductase from Acidianus ambivalens by site-directed mutagenesis."; RL FEMS Microbiol. Lett. 248:171-176(2005). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH IRON, SUBUNIT, RP SULFHYDRATION AT CYS-31, AND REACTION MECHANISM. RX PubMed=16484493; DOI=10.1126/science.1120306; RA Urich T., Gomes C.M., Kletzin A., Frazao C.; RT "X-ray structure of a self-compartmentalizing sulfur cycle metalloenzyme."; RL Science 311:996-1000(2006). CC -!- FUNCTION: Catalyzes the simultaneous oxidation and reduction of CC elemental sulfur in the presence of oxygen, with sulfite and hydrogen CC sulfide as products. {ECO:0000269|PubMed:15030315}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 sulfur + O2 + 4 H2O = 2 hydrogen sulfide + 2 sulfite + 6 CC H(+); Xref=Rhea:RHEA:13957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17359, ChEBI:CHEBI:26833, CC ChEBI:CHEBI:29919; EC=1.13.11.55; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000269|PubMed:15030315}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:15030315}; CC -!- ACTIVITY REGULATION: Inhibited by zinc. {ECO:0000269|PubMed:15030315}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=23 mM for sulfur (at 65 degrees Celsius, with the oxygenase CC reaction) {ECO:0000269|PubMed:15030315}; CC KM=13 mM for sulfur (at 65 degrees Celsius, with the reductase CC reaction) {ECO:0000269|PubMed:15030315}; CC -!- SUBUNIT: Homoicosatetramer. The resulting structure is a hollow sphere CC where catalysis takes place in the inside cavity. CC {ECO:0000269|PubMed:15030315, ECO:0000269|PubMed:16484493}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: Aerobically induced. 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; X56616; CAA39952.1; -; Genomic_DNA. DR PIR; B43331; B43331. DR RefSeq; WP_152941501.1; NZ_CP045482.1. DR PDB; 2CB2; X-ray; 1.70 A; A/B/C/D/E/F=1-309. DR PDB; 2YAV; X-ray; 1.70 A; A/B/C/D/E/F=1-308. DR PDB; 2YAW; X-ray; 2.50 A; A/B/C/D/E/F=1-308. DR PDB; 2YAX; X-ray; 1.80 A; A/B/C/D/E/F=1-308. DR PDB; 6QJC; X-ray; 1.70 A; A/B/C/D=1-309. DR PDB; 6QKA; X-ray; 2.10 A; A/B/C/D/E/F=1-308. DR PDB; 6QKM; X-ray; 2.10 A; A/B/C/D/E/F=1-308. DR PDB; 6QMV; X-ray; 1.87 A; A/B/C/D/E/F=1-308. DR PDB; 6QNE; X-ray; 1.80 A; A/B/C/D/E/F=1-308. DR PDB; 6QO0; X-ray; 1.65 A; A/B/C/D=1-308. DR PDB; 7X9W; EM; 2.78 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-308. DR AlphaFoldDB; P29082; -. DR EMDB; EMD-33084; -. DR SMR; P29082; -. DR GeneID; 42779582; -. DR KEGG; ag:CAA39952; -. DR BioCyc; MetaCyc:MONOMER-12389; -. DR BRENDA; 1.13.11.55; 86. DR EvolutionaryTrace; P29082; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033755; F:sulfur oxygenase/reductase activity; IEA:UniProtKB-EC. DR Gene3D; 3.30.70.100; -; 1. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR011661; S_Oase_red. DR NCBIfam; NF047630; SulOxRed; 1. DR Pfam; PF07682; SOR; 1. DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1. DR PDBsum; 2CB2; -. DR PDBsum; 2YAV; -. DR PDBsum; 2YAW; -. DR PDBsum; 2YAX; -. DR PDBsum; 6QJC; -. DR PDBsum; 6QKA; -. DR PDBsum; 6QKM; -. DR PDBsum; 6QMV; -. DR PDBsum; 6QNE; -. DR PDBsum; 6QO0; -. DR PDBsum; 7X9W; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Iron; Metal-binding; KW Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1522063" FT CHAIN 2..309 FT /note="Sulfur oxygenase/reductase" FT /id="PRO_0000072042" FT BINDING 86 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000269|PubMed:16484493" FT BINDING 90 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000269|PubMed:16484493" FT BINDING 114 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000269|PubMed:16484493" FT MOD_RES 31 FT /note="Cysteine persulfide" FT /evidence="ECO:0000269|PubMed:16484493" FT MUTAGEN 31 FT /note="C->A,S: No enzyme activity. Still binds iron." FT /evidence="ECO:0000269|PubMed:15970399" FT MUTAGEN 86 FT /note="H->A: No enzyme activity and no iron bound." FT /evidence="ECO:0000269|PubMed:15970399" FT MUTAGEN 90 FT /note="H->A: No enzyme activity and no iron bound." FT /evidence="ECO:0000269|PubMed:15970399" FT MUTAGEN 101 FT /note="C->A: 10% residual activity." FT /evidence="ECO:0000269|PubMed:15970399" FT MUTAGEN 101 FT /note="C->S: 1% residual enzyme activity, and no iron FT bound." FT /evidence="ECO:0000269|PubMed:15970399" FT MUTAGEN 104 FT /note="C->A,S: 10% residual activity." FT /evidence="ECO:0000269|PubMed:15970399" FT MUTAGEN 114 FT /note="E->A: No enzyme activity and no iron bound." FT /evidence="ECO:0000269|PubMed:15970399" FT MUTAGEN 114 FT /note="E->D: 1% residual enzyme activity and 4% of FT wild-type levels of iron bound." FT /evidence="ECO:0000269|PubMed:15970399" FT STRAND 5..14 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 17..34 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 40..51 FT /evidence="ECO:0007829|PDB:6QO0" FT TURN 54..60 FT /evidence="ECO:0007829|PDB:6QO0" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 70..82 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 83..92 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 94..102 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 115..123 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:6QO0" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 133..142 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 156..168 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 173..187 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 193..204 FT /evidence="ECO:0007829|PDB:6QO0" FT TURN 206..210 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 214..221 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 244..256 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 257..264 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 271..281 FT /evidence="ECO:0007829|PDB:6QO0" FT STRAND 284..299 FT /evidence="ECO:0007829|PDB:6QO0" FT HELIX 302..307 FT /evidence="ECO:0007829|PDB:6QO0" SQ SEQUENCE 309 AA; 35318 MW; 95C0EEBF0AD079A6 CRC64; MPKPYVAINM AELKNEPKTF EMFASVGPKV CMVTARHPGF VGFQNHIQIG ILPFGNRYGG AKMDMTKESS TVRVLQYTFW KDWKDHEEMH RQNWSYLFRL CYSCASQMIW GPWEPIYEII YANMPINTEM TDFTAVVGKK FAEGKPLDIP VISQPYGKRV VAFAEHSVIP GKEKQFEDAI VRTLEMLKKA PGFLGAMVLK EIGVSGIGSM QFGAKGFHQV LENPGSLEPD PNNVMYSVPE AKNTPQQYIV HVEWANTDAL MFGMGRVLLY PELRQVHDEV LDTLVYGPYI RILNPMMEGT FWREYLNEQ //