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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)DescriptionActionsGraphical viewLength
    Metal bindingi86Iron; via tele nitrogen1 Publication1
    Metal bindingi90Iron; via tele nitrogen1 Publication1
    Metal bindingi114Iron1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi31C → A or S: No enzyme activity. Still binds iron. 1 Publication1
    Mutagenesisi86H → A: No enzyme activity and no iron bound. 1 Publication1
    Mutagenesisi90H → A: No enzyme activity and no iron bound. 1 Publication1
    Mutagenesisi101C → A: 10% residual activity. 1 Publication1
    Mutagenesisi101C → S: 1% residual enzyme activity, and no iron bound. 1 Publication1
    Mutagenesisi104C → A or S: 10% residual activity. 1 Publication1
    Mutagenesisi114E → A: No enzyme activity and no iron bound. 1 Publication1
    Mutagenesisi114E → D: 1% residual enzyme activity and 4% of wild-type levels of iron bound. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000720422 – 309Sulfur oxygenase/reductaseAdd BLAST308

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei31Cysteine persulfide1 Publication1

    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

    1309
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 14Combined sources10
    Helixi17 – 34Combined sources18
    Beta strandi40 – 51Combined sources12
    Turni54 – 60Combined sources7
    Turni66 – 68Combined sources3
    Beta strandi70 – 82Combined sources13
    Helixi83 – 92Combined sources10
    Helixi94 – 102Combined sources9
    Helixi103 – 107Combined sources5
    Beta strandi108 – 113Combined sources6
    Beta strandi115 – 123Combined sources9
    Turni130 – 132Combined sources3
    Helixi133 – 142Combined sources10
    Helixi146 – 148Combined sources3
    Beta strandi156 – 168Combined sources13
    Helixi173 – 187Combined sources15
    Beta strandi193 – 204Combined sources12
    Turni206 – 210Combined sources5
    Helixi214 – 221Combined sources8
    Beta strandi225 – 227Combined sources3
    Helixi231 – 233Combined sources3
    Helixi239 – 241Combined sources3
    Beta strandi244 – 256Combined sources13
    Helixi257 – 269Combined sources13
    Helixi271 – 281Combined sources11
    Beta strandi284 – 299Combined sources16
    Helixi302 – 307Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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
    PDB 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.
    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: November 2, 2016
    This is version 77 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.