BTRN_NIACI
ID BTRN_NIACI Reviewed; 250 AA.
AC Q8G907;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-inosamine dehydrogenase;
DE EC=1.1.99.38;
DE AltName: Full=Butirosin biosynthesis protein N;
DE AltName: Full=Radical S-adenosylmethionine dehydrogenase BtrN;
DE Short=RS dehydrogenase BtrN;
DE Short=Radical SAM dehydrogenase BtrN;
GN Name=btrN;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11132962; DOI=10.7164/antibiotics.53.1158;
RA Ota Y., Tamegai H., Kudo F., Kuriki H., Koike-Takeshita A., Eguchi T.,
RA Kakinuma K.;
RT "Butirosin-biosynthetic gene cluster from Bacillus circulans.";
RL J. Antibiot. 53:1158-1167(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Huang F.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=18001019; DOI=10.1021/ja072481t;
RA Yokoyama K., Numakura M., Kudo F., Ohmori D., Eguchi T.;
RT "Characterization and mechanistic study of a radical SAM dehydrogenase in
RT the biosynthesis of butirosin.";
RL J. Am. Chem. Soc. 129:15147-15155(2007).
RN [4]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=18672902; DOI=10.1021/bi800509x;
RA Yokoyama K., Ohmori D., Kudo F., Eguchi T.;
RT "Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by
RT electron paramagnetic resonance spectroscopy.";
RL Biochemistry 47:8950-8960(2008).
RN [5]
RP COFACTOR, AND MUTAGENESIS OF CYS-16; CYS-20; CYS-23; CYS-68; CYS-169;
RP CYS-187; CYS-232 AND CYS-235.
RX PubMed=20377206; DOI=10.1021/bi9022126;
RA Grove T.L., Ahlum J.H., Sharma P., Krebs C., Booker S.J.;
RT "A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN
RT contains two [4Fe-4S] clusters.";
RL Biochemistry 49:3783-3785(2010).
CC -!- FUNCTION: Catalyzes the radical S-adenosyl-L-methionine (SAM)-dependent
CC two-electron oxidation of 2-deoxy-scyllo-inosamine (DOIA) to amino-
CC dideoxy-scyllo-inosose (amino-DOI) in the biosynthetic pathway of
CC butirosin. {ECO:0000269|PubMed:18001019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-
CC 2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + H(+) + L-methionine;
CC Xref=Rhea:RHEA:34275, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65002,
CC ChEBI:CHEBI:65003; EC=1.1.99.38;
CC Evidence={ECO:0000269|PubMed:18001019, ECO:0000269|PubMed:18672902};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:18672902, ECO:0000305|PubMed:20377206};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. A second
CC auxiliary cluster is also in contact with the substrate and is proposed
CC to facilitate the loss of the second electron in the oxidation.
CC {ECO:0000305|PubMed:18672902, ECO:0000305|PubMed:20377206};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.022 mM for DOIA {ECO:0000269|PubMed:18001019};
CC Note=Kinetic parameter was determined with saturating SAM. DOIA
CC displays substrate inhibition.;
CC -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC {ECO:0000269|PubMed:18001019}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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; AB097196; BAE07062.1; -; Genomic_DNA.
DR EMBL; AJ494863; CAD41948.1; -; Genomic_DNA.
DR PDB; 4M7S; X-ray; 2.02 A; A=1-250.
DR PDB; 4M7T; X-ray; 1.56 A; A=1-250.
DR PDBsum; 4M7S; -.
DR PDBsum; 4M7T; -.
DR AlphaFoldDB; Q8G907; -.
DR SMR; Q8G907; -.
DR KEGG; ag:BAE07062; -.
DR BioCyc; MetaCyc:MON-17280; -.
DR BRENDA; 1.1.99.38; 649.
DR UniPathway; UPA00964; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR034386; BtrN-like.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDF00424; 2-deoxy-scyllo-inosamine_dehyd; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Antibiotic biosynthesis; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; S-adenosyl-L-methionine.
FT CHAIN 1..250
FT /note="S-adenosyl-L-methionine-dependent 2-deoxy-scyllo-
FT inosamine dehydrogenase"
FT /id="PRO_0000424206"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000305"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000305"
FT BINDING 223
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000305"
FT MUTAGEN 16
FT /note="C->A: Reduced iron-sulfur content by 50%; when
FT associated with A-20 and A-23."
FT /evidence="ECO:0000269|PubMed:20377206"
FT MUTAGEN 20
FT /note="C->A: Reduced iron-sulfur content by 50%; when
FT associated with A-16 and A-23."
FT /evidence="ECO:0000269|PubMed:20377206"
FT MUTAGEN 23
FT /note="C->A: Reduced iron-sulfur content by 50%; when
FT associated with A-16 and A-20."
FT /evidence="ECO:0000269|PubMed:20377206"
FT MUTAGEN 68
FT /note="C->A: Soluble protein."
FT /evidence="ECO:0000269|PubMed:20377206"
FT MUTAGEN 169
FT /note="C->A: Insoluble protein."
FT /evidence="ECO:0000269|PubMed:20377206"
FT MUTAGEN 187
FT /note="C->A: Insoluble protein."
FT /evidence="ECO:0000269|PubMed:20377206"
FT MUTAGEN 232
FT /note="C->A: Insoluble protein."
FT /evidence="ECO:0000269|PubMed:20377206"
FT MUTAGEN 235
FT /note="C->A: Soluble protein; reduces activity."
FT /evidence="ECO:0000269|PubMed:20377206"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4M7T"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:4M7S"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:4M7T"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:4M7T"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4M7T"
FT TURN 230..234
FT /evidence="ECO:0007829|PDB:4M7T"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4M7S"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:4M7S"
SQ SEQUENCE 250 AA; 28456 MW; 30C113758BC60830 CRC64;
MDKLFSMIEV EVNSQCNRTC WYCPNSVSKR KETGEMDPAL YKTLMEQLSS LDFAGRISFH
FYGEPLLCKN LDLFVGMTTE YIPRARPIIY TNGDFLTEKR LQTLTELGIQ KFIVTQHAGA
KHKFRGVYDQ LAGADKEKVV YLDHSDLVLS NRGGILDNIP QASKANMSCM VPSNLAVVTV
LGNVLPCFED FNQKMVMGNI GEQHISDIWH NDKFTSFRKM LKEGHRGKSD LCKNCNNVSV
QTEEQYDYVL
