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Protein

S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-inosamine dehydrogenase

Gene

btrN

Organism
Bacillus circulans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the radical S-adenosyl-L-methionine (SAM)-dependent two-electron oxidation of 2-deoxy-scyllo-inosamine (DOIA) to amino-dideoxy-scyllo-inosose (amino-DOI) in the biosynthetic pathway of butirosin.1 Publication

Catalytic activityi

2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + L-methionine.2 Publications

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. A second auxiliary cluster is also in contact with the substrate and is proposed to facilitate the loss of the second electron in the oxidation.2 Publications

Kineticsi

Kinetic parameter was determined with saturating SAM. DOIA displays substrate inhibition.

  1. KM=0.022 mM for DOIA1 Publication

    Pathwayi: butirosin biosynthesis

    This protein is involved in the pathway butirosin biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway butirosin biosynthesis and in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi16Iron-sulfur 1 (4Fe-4S-S-AdoMet)Curated1
    Metal bindingi20Iron-sulfur 1 (4Fe-4S-S-AdoMet)Curated1
    Metal bindingi23Iron-sulfur 1 (4Fe-4S-S-AdoMet)Curated1
    Metal bindingi169Iron-sulfur 2 (4Fe-4S-substrate)Curated1
    Metal bindingi187Iron-sulfur 2 (4Fe-4S-substrate)Curated1
    Metal bindingi223Iron-sulfur 2 (4Fe-4S-substrate)Curated1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17280.
    BRENDAi1.1.99.38. 649.
    UniPathwayiUPA00964.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-inosamine dehydrogenase (EC:1.1.99.38)
    Alternative name(s):
    Butirosin biosynthesis protein N
    Radical S-adenosylmethionine dehydrogenase BtrN
    Short name:
    RS dehydrogenase BtrN
    Short name:
    Radical SAM dehydrogenase BtrN
    Gene namesi
    Name:btrN
    OrganismiBacillus circulans
    Taxonomic identifieri1397 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi16C → A: Reduced iron-sulfur content by 50%; when associated with A-20 and A-23. 1 Publication1
    Mutagenesisi20C → A: Reduced iron-sulfur content by 50%; when associated with A-16 and A-23. 1 Publication1
    Mutagenesisi23C → A: Reduced iron-sulfur content by 50%; when associated with A-16 and A-20. 1 Publication1
    Mutagenesisi68C → A: Soluble protein. 1 Publication1
    Mutagenesisi169C → A: Insoluble protein. 1 Publication1
    Mutagenesisi187C → A: Insoluble protein. 1 Publication1
    Mutagenesisi232C → A: Insoluble protein. 1 Publication1
    Mutagenesisi235C → A: Soluble protein; reduces activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004242061 – 250S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-inosamine dehydrogenaseAdd BLAST250

    Structurei

    Secondary structure

    1250
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 10Combined sources5
    Helixi24 – 26Combined sources3
    Helixi38 – 50Combined sources13
    Beta strandi55 – 58Combined sources4
    Beta strandi61 – 63Combined sources3
    Helixi65 – 67Combined sources3
    Helixi71 – 81Combined sources11
    Beta strandi85 – 91Combined sources7
    Helixi98 – 107Combined sources10
    Beta strandi111 – 116Combined sources6
    Beta strandi118 – 120Combined sources3
    Helixi124 – 130Combined sources7
    Helixi133 – 136Combined sources4
    Beta strandi139 – 143Combined sources5
    Helixi144 – 146Combined sources3
    Turni152 – 155Combined sources4
    Helixi163 – 166Combined sources4
    Helixi171 – 174Combined sources4
    Beta strandi175 – 178Combined sources4
    Beta strandi182 – 186Combined sources5
    Turni200 – 202Combined sources3
    Helixi205 – 209Combined sources5
    Helixi212 – 222Combined sources11
    Helixi226 – 228Combined sources3
    Turni230 – 234Combined sources5
    Beta strandi239 – 241Combined sources3
    Helixi243 – 246Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4M7SX-ray2.02A1-250[»]
    4M7TX-ray1.56A1-250[»]
    ProteinModelPortaliQ8G907.
    SMRiQ8G907.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the radical SAM superfamily.Curated

    Phylogenomic databases

    KOiK13549.

    Family and domain databases

    Gene3Di3.20.20.70. 2 hits.
    InterProiIPR023885. 4Fe4S-binding_SPASM_dom.
    IPR013785. Aldolase_TIM.
    [Graphical view]
    PfamiPF13186. SPASM. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR04085. rSAM_more_4Fe4S. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8G907-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDKLFSMIEV EVNSQCNRTC WYCPNSVSKR KETGEMDPAL YKTLMEQLSS
    60 70 80 90 100
    LDFAGRISFH FYGEPLLCKN LDLFVGMTTE YIPRARPIIY TNGDFLTEKR
    110 120 130 140 150
    LQTLTELGIQ KFIVTQHAGA KHKFRGVYDQ LAGADKEKVV YLDHSDLVLS
    160 170 180 190 200
    NRGGILDNIP QASKANMSCM VPSNLAVVTV LGNVLPCFED FNQKMVMGNI
    210 220 230 240 250
    GEQHISDIWH NDKFTSFRKM LKEGHRGKSD LCKNCNNVSV QTEEQYDYVL
    Length:250
    Mass (Da):28,456
    Last modified:March 1, 2003 - v1
    Checksum:i30C113758BC60830
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB097196 Genomic DNA. Translation: BAE07062.1.
    AJ494863 Genomic DNA. Translation: CAD41948.1.

    Genome annotation databases

    KEGGiag:BAE07062.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB097196 Genomic DNA. Translation: BAE07062.1.
    AJ494863 Genomic DNA. Translation: CAD41948.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4M7SX-ray2.02A1-250[»]
    4M7TX-ray1.56A1-250[»]
    ProteinModelPortaliQ8G907.
    SMRiQ8G907.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAE07062.

    Phylogenomic databases

    KOiK13549.

    Enzyme and pathway databases

    UniPathwayiUPA00964.
    BioCyciMetaCyc:MONOMER-17280.
    BRENDAi1.1.99.38. 649.

    Family and domain databases

    Gene3Di3.20.20.70. 2 hits.
    InterProiIPR023885. 4Fe4S-binding_SPASM_dom.
    IPR013785. Aldolase_TIM.
    [Graphical view]
    PfamiPF13186. SPASM. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR04085. rSAM_more_4Fe4S. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiBTRN_BACCI
    AccessioniPrimary (citable) accession number: Q8G907
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 16, 2013
    Last sequence update: March 1, 2003
    Last modified: November 2, 2016
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    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.