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Entry: A0A0Q7DWL4_9CAUL
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Original site: A0A0Q7DWL4_9CAUL 
ID   A0A0Q7DWL4_9CAUL        Unreviewed;       333 AA.
AC   A0A0Q7DWL4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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   ORFNames=ASC65_11780 {ECO:0000313|EMBL:KQW81955.1};
OS   Brevundimonas sp. Root1279.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736443 {ECO:0000313|EMBL:KQW81955.1, ECO:0000313|Proteomes:UP000050923};
RN   [1] {ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|Proteomes:UP000050923};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW81955.1, ECO:0000313|Proteomes:UP000050923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1279 {ECO:0000313|EMBL:KQW81955.1,
RC   ECO:0000313|Proteomes:UP000050923};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQW81955.1}.
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DR   EMBL; LMEB01000007; KQW81955.1; -; Genomic_DNA.
DR   RefSeq; WP_056453343.1; NZ_LMEB01000007.1.
DR   AlphaFoldDB; A0A0Q7DWL4; -.
DR   STRING; 1736443.ASC65_11780; -.
DR   OrthoDB; 9786826at2; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000050923; 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; SFLDF00272; biotin_synthase; 1.
DR   SFLD; SFLDG01278; biotin_synthase_like; 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:UP000050923};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01694};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01694}.
FT   DOMAIN          43..265
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         58
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         62
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         65
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         102
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         133
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         193
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         269
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   333 AA;  35982 MW;  C38C6B766DDD58A5 CRC64;
     MTRDLSIPRH DWTLEEVEAL FARPFMELVF DAATAHRRWF DPSEVQKSQL LSIKTGGCAE
     NCGYCSQSAS FDTGLKAEKL MDAQAVIAEA MAAKAGGASR FCMGAAWREL KDRDTPKLAT
     MIAGVKALGL ETCATLGMLT ADQARQLKDA GLDYYNHNLD TGPDYYAEVV TTRTYQDRLD
     TLQHVRDAGM NTCCGGIVGM GEARRDRAGL LHALATLPEH PDSLPVNALV PVTGTPLGDR
     VKKEGEIDPI EFVRTVAVAR LVCPKAMVRL SAGRETMSPE MQALCFLAGA NSIFVGGKLL
     TTPNPEQDED ARLFALLDLK AMEPRGEGAA CAA
//
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