SOR_ACIAM
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 03-AUG-2022, entry version 92.
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; Crenarchaeota; 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 H2O + O2 + 4 sulfur = 6 H(+) + 2 hydrogen sulfide + 2
CC sulfite; 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.
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DR EMBL; X56616; CAA39952.1; -; Genomic_DNA.
DR PIR; B43331; B43331.
DR PDB; 2CB2; X-ray; 1.70 A; A/B/C/D/E/F=2-309.
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 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 AlphaFoldDB; P29082; -.
DR SMR; P29082; -.
DR KEGG; ag:CAA39952; -.
DR BioCyc; MetaCyc:MON-12389; -.
DR BRENDA; 1.13.11.55; 86.
DR EvolutionaryTrace; P29082; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033755; F:sulfur oxygenase/reductase activity; IEA:UniProtKB-EC.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR011661; S_Oase_red.
DR Pfam; PF07682; SOR; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
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 wild-
FT 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 103..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 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 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
