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Protein

Sulfur oxygenase/reductase

Gene

sor

Organism
Acidianus ambivalens (Desulfurolobus ambivalens)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.1 Publication

Catalytic activityi

4 sulfur + 4 H2O + O2 = 2 H2S + 2 HSO3- + 2 H+.

Cofactori

Fe cation1 PublicationNote: Binds 1 Fe cation per subunit.1 Publication

Enzyme regulationi

Inhibited by zinc.1 Publication

Kineticsi

  1. KM=23 mM for sulfur (at 65 degrees Celsius, with the oxygenase reaction)1 Publication
  2. KM=13 mM for sulfur (at 65 degrees Celsius, with the reductase reaction)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi86 – 861Iron; via tele nitrogen1 Publication
    Metal bindingi90 – 901Iron; via tele nitrogen1 Publication
    Metal bindingi114 – 1141Iron1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12389.
    BRENDAi1.13.11.55. 86.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfur oxygenase/reductase (EC:1.13.11.55)
    Alternative name(s):
    Sulfur oxygenase reductase
    Short name:
    SOR
    Gene namesi
    Name:sor
    OrganismiAcidianus ambivalens (Desulfurolobus ambivalens)
    Taxonomic identifieri2283 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeAcidianus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311C → A or S: No enzyme activity. Still binds iron. 1 Publication
    Mutagenesisi86 – 861H → A: No enzyme activity and no iron bound. 1 Publication
    Mutagenesisi90 – 901H → A: No enzyme activity and no iron bound. 1 Publication
    Mutagenesisi101 – 1011C → A: 10% residual activity. 1 Publication
    Mutagenesisi101 – 1011C → S: 1% residual enzyme activity, and no iron bound. 1 Publication
    Mutagenesisi104 – 1041C → A or S: 10% residual activity. 1 Publication
    Mutagenesisi114 – 1141E → A: No enzyme activity and no iron bound. 1 Publication
    Mutagenesisi114 – 1141E → D: 1% residual enzyme activity and 4% of wild-type levels of iron bound. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 309308Sulfur oxygenase/reductasePRO_0000072042Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311Cysteine persulfide1 Publication

    Expressioni

    Inductioni

    Aerobically induced.

    Interactioni

    Subunit structurei

    Homoicosatetramer. The resulting structure is a hollow sphere where catalysis takes place in the inside cavity.2 Publications

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1410Combined sources
    Helixi17 – 3418Combined sources
    Beta strandi40 – 5112Combined sources
    Turni54 – 607Combined sources
    Turni66 – 683Combined sources
    Beta strandi70 – 8213Combined sources
    Helixi83 – 9210Combined sources
    Helixi94 – 1029Combined sources
    Helixi103 – 1075Combined sources
    Beta strandi108 – 1136Combined sources
    Beta strandi115 – 1239Combined sources
    Turni130 – 1323Combined sources
    Helixi133 – 14210Combined sources
    Helixi146 – 1483Combined sources
    Beta strandi156 – 16813Combined sources
    Helixi173 – 18715Combined sources
    Beta strandi193 – 20412Combined sources
    Turni206 – 2105Combined sources
    Helixi214 – 2218Combined sources
    Beta strandi225 – 2273Combined sources
    Helixi231 – 2333Combined sources
    Helixi239 – 2413Combined sources
    Beta strandi244 – 25613Combined sources
    Helixi257 – 26913Combined sources
    Helixi271 – 28111Combined sources
    Beta strandi284 – 29916Combined sources
    Helixi302 – 3076Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CB2X-ray1.70A/B/C/D/E/F2-309[»]
    2YAVX-ray1.70A/B/C/D/E/F1-308[»]
    2YAWX-ray2.50A/B/C/D/E/F1-308[»]
    2YAXX-ray1.80A/B/C/D/E/F1-308[»]
    ProteinModelPortaliP29082.
    SMRiP29082. Positions 2-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29082.

    Family & Domainsi

    Phylogenomic databases

    KOiK16952.

    Family and domain databases

    InterProiIPR011008. Dimeric_a/b-barrel.
    IPR011661. S_Oase_red.
    [Graphical view]
    PfamiPF07682. SOR. 1 hit.
    [Graphical view]
    SUPFAMiSSF54909. SSF54909. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P29082-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPKPYVAINM AELKNEPKTF EMFASVGPKV CMVTARHPGF VGFQNHIQIG
    60 70 80 90 100
    ILPFGNRYGG AKMDMTKESS TVRVLQYTFW KDWKDHEEMH RQNWSYLFRL
    110 120 130 140 150
    CYSCASQMIW GPWEPIYEII YANMPINTEM TDFTAVVGKK FAEGKPLDIP
    160 170 180 190 200
    VISQPYGKRV VAFAEHSVIP GKEKQFEDAI VRTLEMLKKA PGFLGAMVLK
    210 220 230 240 250
    EIGVSGIGSM QFGAKGFHQV LENPGSLEPD PNNVMYSVPE AKNTPQQYIV
    260 270 280 290 300
    HVEWANTDAL MFGMGRVLLY PELRQVHDEV LDTLVYGPYI RILNPMMEGT

    FWREYLNEQ
    Length:309
    Mass (Da):35,318
    Last modified:January 23, 2007 - v3
    Checksum:i95C0EEBF0AD079A6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X56616 Genomic DNA. Translation: CAA39952.1.
    PIRiB43331.

    Genome annotation databases

    KEGGiag:CAA39952.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X56616 Genomic DNA. Translation: CAA39952.1.
    PIRiB43331.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CB2X-ray1.70A/B/C/D/E/F2-309[»]
    2YAVX-ray1.70A/B/C/D/E/F1-308[»]
    2YAWX-ray2.50A/B/C/D/E/F1-308[»]
    2YAXX-ray1.80A/B/C/D/E/F1-308[»]
    ProteinModelPortaliP29082.
    SMRiP29082. Positions 2-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAA39952.

    Phylogenomic databases

    KOiK16952.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12389.
    BRENDAi1.13.11.55. 86.

    Miscellaneous databases

    EvolutionaryTraceiP29082.

    Family and domain databases

    InterProiIPR011008. Dimeric_a/b-barrel.
    IPR011661. S_Oase_red.
    [Graphical view]
    PfamiPF07682. SOR. 1 hit.
    [Graphical view]
    SUPFAMiSSF54909. SSF54909. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSOR_ACIAM
    AccessioniPrimary (citable) accession number: P29082
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: May 11, 2016
    This is version 75 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.