AC   MF_01694;
DC   Protein; auto
TR   HAMAP; MF_01694; -; 1; level=0
XX
Names: BioB
XX
ID   BIOB
DE   RecName: Full=Biotin synthase;
DE            EC=2.8.1.6;
GN   Name=bioB;
XX
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.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC       Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC       cysteines and 1 arginine.;
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC       diaminononanoate: step 2/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC       family.
XX
DR   Pfam; PF06968; BATS; 1; trigger=no
DR   Pfam; PF04055; Radical_SAM; 1; trigger=no
DR   NCBIfam; TIGR00433; BioB; 1; trigger=no
XX
KW   2Fe-2S
KW   4Fe-4S
KW   Biotin biosynthesis
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
KW   S-adenosyl-L-methionine
KW   Transferase
XX
GO   GO:0004076; F:biotin synthase activity
GO   GO:0005506; F:iron ion binding
GO   GO:0051536; F:iron-sulfur cluster binding
GO   GO:0009102; P:biotin biosynthetic process
XX
FT   From: BIOB_ECOLI (P12996)
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Condition: C
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Condition: C
FT   BINDING         60
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Condition: C
FT   BINDING         97
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Condition: [CS]
FT   BINDING         128
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Condition: [CS]
FT   BINDING         188
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Condition: C
FT   BINDING         260
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT   Condition: [KR]
XX
Size: 275-804;
Related: None;
Template: P12996;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: MF_00834 (bioA)
Duplicate: in CORDI, FRACC, PARDP, POLSJ
Plasmid: in RHILO
Comments: Bacteroides encode a fusion between BioA (7,8-diamino-pelargonic acid
 aminotransferase) and BioB.
XX
# Revision 1.21 2023/06/01
//