ID A0A3N7EJ60_9BURK Unreviewed; 365 AA.
AC A0A3N7EJ60;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Biotin synthase {ECO:0000256|ARBA:ARBA00012236, ECO:0000256|HAMAP-Rule:MF_01694};
DE EC=2.8.1.6 {ECO:0000256|ARBA:ARBA00012236, ECO:0000256|HAMAP-Rule:MF_01694};
GN Name=bioB {ECO:0000256|HAMAP-Rule:MF_01694,
GN ECO:0000313|EMBL:RQO55594.1};
GN ORFNames=DBR47_20280 {ECO:0000313|EMBL:RQO55594.1};
OS Paucibacter sp. KBW04.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=2153361 {ECO:0000313|EMBL:RQO55594.1, ECO:0000313|Proteomes:UP000274884};
RN [1] {ECO:0000313|EMBL:RQO55594.1, ECO:0000313|Proteomes:UP000274884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBW04 {ECO:0000313|EMBL:RQO55594.1,
RC ECO:0000313|Proteomes:UP000274884};
RA Lee F., Williams K.B., Levin M., Wolfe B.E.;
RT "The microbiome of the planarian worm Dugesia japonica mediates outcomes of
RT regeneration via indole production.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00023417, ECO:0000256|HAMAP-
CC Rule:MF_01694};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01694};
CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC cysteines and 1 arginine. {ECO:0000256|HAMAP-Rule:MF_01694};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR001619-1};
CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3
CC cysteines and 1 arginine. {ECO:0000256|PIRSR:PIRSR001619-1};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01694,
CC ECO:0000256|PIRSR:PIRSR001619-1};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000256|PIRSR:PIRSR001619-1};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-
CC diaminononanoate: step 2/2. {ECO:0000256|ARBA:ARBA00004942,
CC ECO:0000256|HAMAP-Rule:MF_01694}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01694}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin synthase
CC family. {ECO:0000256|ARBA:ARBA00010765, ECO:0000256|HAMAP-
CC Rule:MF_01694}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RQO55594.1}.
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DR EMBL; QAJN01000016; RQO55594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N7EJ60; -.
DR OrthoDB; 9786826at2; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000274884; Unassembled WGS sequence.
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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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/MiaA/NifB-like_rSAM.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00433; bioB; 1.
DR PANTHER; PTHR22976; BIOTIN SYNTHASE; 1.
DR PANTHER; PTHR22976:SF2; BIOTIN SYNTHASE, MITOCHONDRIAL; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF001619; Biotin_synth; 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 1.
DR SFLD; SFLDF00272; biotin_synthase; 1.
DR SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_01694};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01694};
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756, ECO:0000256|HAMAP-
KW Rule:MF_01694};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01694};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01694};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01694}; Reference proteome {ECO:0000313|Proteomes:UP000274884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01694}; Transferase {ECO:0000256|HAMAP-Rule:MF_01694}.
FT DOMAIN 61..288
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694,
FT ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694,
FT ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694,
FT ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694,
FT ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 151
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694,
FT ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 211
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694,
FT ECO:0000256|PIRSR:PIRSR001619-1"
FT BINDING 283
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01694,
FT ECO:0000256|PIRSR:PIRSR001619-1"
SQ SEQUENCE 365 AA; 40199 MW; CD7DA8BD8AE88C97 CRC64;
MSHPVHSQTT NQIQSLTPTR DEDRRNAKPW TVNEVAALYD LPFNDLMFKA QSVHRQYFDA
NAVQLSTLLS IKTGGCEEDC KYCPQSAHFD TGLKAEKLIP LQEVLEAARA AKENGATRFC
MGAAWRAPKE RHLEAIGEMV KEVKAMGLET CLTAGMLGDG QAEQLREAGL DYYNHNLDTS
PEFYGQIITT RTYQDRLDTL DRVRNVGLKV CSGGIVGMGE TRRQRAGLIV QLANLDPYPE
SVPINNLVQV EGTPLSGTEA LDPFEFIRSI AVARITMPRA MVRLSAGREE MPESMQALCF
LAGANSMFYG DKLLTTSNPQ AEKDRALLKR LGMHCATEAD LAAEGKVNLC RNAEDGAQDK
ACASH
//
