BIOB_LYSSH
ID BIOB_LYSSH Reviewed; 332 AA.
AC P19206;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Biotin synthase {ECO:0000255|HAMAP-Rule:MF_01694};
DE EC=2.8.1.6 {ECO:0000255|HAMAP-Rule:MF_01694};
GN Name=bioB {ECO:0000255|HAMAP-Rule:MF_01694};
OS Lysinibacillus sphaericus (Bacillus sphaericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=T-178-367;
RX PubMed=2507401; DOI=10.1016/0378-1119(89)90248-5;
RA Ohsawa I., Speck D., Kisou T., Hayakawa K., Zinsius M., Gloeckler R.,
RA Lemoine Y., Kamogawa K.;
RT "Cloning of the biotin synthetase gene from Bacillus sphaericus and
RT expression in Escherichia coli and Bacilli.";
RL Gene 80:39-48(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2110099; DOI=10.1016/0378-1119(90)90496-e;
RA Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M.,
RA Villeval D., Kisou T., Kamogawa K., Lemoine Y.;
RT "Cloning and characterization of the Bacillus sphaericus genes controlling
RT the bioconversion of pimelate into dethiobiotin.";
RL Gene 87:63-70(1990).
CC -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by
CC the insertion of a sulfur atom into dethiobiotin via a radical-based
CC mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-
CC 2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine +
CC [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:29917, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:57586, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:149473; EC=2.8.1.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|HAMAP-Rule:MF_01694};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694};
CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC cysteines and 1 arginine. {ECO:0000255|HAMAP-Rule:MF_01694};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01694}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC family. {ECO:0000255|HAMAP-Rule:MF_01694}.
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DR EMBL; M27867; AAA22268.1; -; Genomic_DNA.
DR EMBL; M29292; AAB02327.1; -; Genomic_DNA.
DR PIR; JS0274; JS0274.
DR RefSeq; WP_024361129.1; NZ_UFSZ01000001.1.
DR AlphaFoldDB; P19206; -.
DR SMR; P19206; -.
DR STRING; 1421.A2J09_09950; -.
DR GeneID; 48276410; -.
DR UniPathway; UPA00078; UER00162.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01694; BioB; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR002684; Biotin_synth/BioAB.
DR InterPro; IPR024177; Biotin_synthase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR22976; PTHR22976; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF001619; Biotin_synth; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00433; bioB; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 4Fe-4S; Biotin biosynthesis; Direct protein sequencing; Iron;
KW Iron-sulfur; Metal-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..332
FT /note="Biotin synthase"
FT /id="PRO_0000185545"
FT DOMAIN 46..275
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 140
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 200
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 270
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
SQ SEQUENCE 332 AA; 37015 MW; B5FF14F5CA9903EF CRC64;
MNWLQLADEV IAGKVISDDE ALAILNSDDD DILKLMDGAF AIRKHYYGKK VKLNMIMNAK
SGYCPEDCGY CSQSSKSTAP IEKYPFITKE EILAGAKRAF ENKIGTYCIV ASGRGPTRKD
VNVVSEAVEE IKAKYGLKVC ACLGLLKEEQ AQQLKEAGVD RYNHNLNTSE RHHSYITTTH
TYEDRVNTVE VVKKHGISPC SGAIIGMKET KMDVVEIARA LHQLDADSIP VNFLHAIDGT
KLEGTQDLNP RYCLKVLALF RYMNPSKEIR ISGGREVNLG FLQPFGLYAA NSIFVGDYLT
TEGQEANSDY RMLEDLGFEI ELTQKQEEAF CS
