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Entry: A0A0X8JB58_9FLAO
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ID   A0A0X8JB58_9FLAO        Unreviewed;       362 AA.
AC   A0A0X8JB58;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=AXF12_09040 {ECO:0000313|EMBL:AMD85644.1};
OS   Capnocytophaga haemolytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=45243 {ECO:0000313|EMBL:AMD85644.1, ECO:0000313|Proteomes:UP000065822};
RN   [1] {ECO:0000313|Proteomes:UP000065822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 32990 {ECO:0000313|Proteomes:UP000065822};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; CP014227; AMD85644.1; -; Genomic_DNA.
DR   RefSeq; WP_066430442.1; NZ_LT906449.1.
DR   AlphaFoldDB; A0A0X8JB58; -.
DR   STRING; 45243.AXF12_09040; -.
DR   KEGG; chg:AXF12_09040; -.
DR   OrthoDB; 9786826at2; -.
DR   UniPathway; UPA00078; UER00162.
DR   Proteomes; UP000065822; 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 {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};
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          39..268
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          334..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54
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         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         61
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         99
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         131
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         191
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         263
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   362 AA;  40550 MW;  EEFFA5DC6EE16647 CRC64;
     MSETRHNWTK EEVMEIYNRP LMDLLYEAAT VHRKYHDPNT VQVSTLLSIK TGGCSEDCAY
     CSQSARYDTS VKVEHDMMTV PHVKAQALRA KASGASRVCM GAAWRNVKDG PEFEDVLEMV
     RTINKLDMEV CCTLGMITEN QAQRLAEAGL YAYNHNLDTS EDYYKEIIST RSYEDRLKTI
     ENVRKTSITV CSGGIIGMGE SLEDRASMLV ALSTLNPQPE SVPINALVPI EGTPLEELPP
     VEVWDLVRMI ATARIVMPET QVRLSAGRTQ MSPEGQAMCF FAGANSIFAG DKLLTTPNPD
     INADMQMLKA LGMRLQKPFE THPHPTTVEA CDSQFPSLGE KPKWSRPTHT IERNQEKYKI
     KK
//
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