ID   BIOB_CHRFK              Reviewed;         363 AA.
AC   A0M7A9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
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};
GN   OrderedLocusNames=GFO_3566;
OS   Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803)
OS   (Gramella forsetii).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17595 / CGMCC 1.15422 / KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL68504.1; -; Genomic_DNA.
DR   RefSeq; WP_011711405.1; NC_008571.1.
DR   AlphaFoldDB; A0M7A9; -.
DR   SMR; A0M7A9; -.
DR   STRING; 411154.GFO_3566; -.
DR   KEGG; gfo:GFO_3566; -.
DR   eggNOG; COG0502; Bacteria.
DR   HOGENOM; CLU_033172_1_2_10; -.
DR   OrthoDB; 9786826at2; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000000755; Chromosome.
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; SFLDS00029; Radical_SAM; 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; 4Fe-4S; Biotin biosynthesis; Iron; Iron-sulfur; Metal-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..363
FT                   /note="Biotin synthase"
FT                   /id="PRO_0000381412"
FT   DOMAIN          38..266
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   REGION          315..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53
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         57
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         60
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         97
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   BINDING         129
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   BINDING         189
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT   BINDING         261
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
SQ   SEQUENCE   363 AA;  40474 MW;  FC799A4D3A865CD4 CRC64;
     MALKHDWTKE EILEIYNKPF MELLYDAATI HREHHDPNTV QVSTLLSIKT GGCPEDCGYC
     PQAARYHTDL EGNDLMSVNQ VKAQALRAKA SGSSRVCMGA AWRNVKDGEE FDNVLEMVRS
     INKLDMEVCC TLGMLTENQA QRLAEAGLYA YNHNLDSSEE YYKEVISTRG YQDRLDTIGN
     VRKTNVTVCS GGIIGMGESE ADRAGMLVAL STLNPQPESV PINALVPVEG TPMEEQEPVP
     IWEMIRMVAT TRIVMPETQV RLSAGRTQMS REGQAMCFFA GANSIFAGDK LLTTPNPDVS
     EDMEMFKMLG LNPQKAFEKK SQPESVAAEK SKYQSQGEKP RWSRPEHKID RNLEAQQNAK
     TKA
//