ID A0A0C4Y472_9BURK Unreviewed; 348 AA.
AC A0A0C4Y472;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=RR42_m0188 {ECO:0000313|EMBL:AJG17603.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG17603.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG17603.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG17603.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010536; AJG17603.1; -; Genomic_DNA.
DR RefSeq; WP_043342973.1; NZ_CP010536.1.
DR AlphaFoldDB; A0A0C4Y472; -.
DR STRING; 68895.RR42_m0188; -.
DR KEGG; cbw:RR42_m0188; -.
DR OrthoDB; 9786826at2; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000031843; Chromosome main.
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:UP000031843};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01694};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01694, ECO:0000313|EMBL:AJG17603.1}.
FT DOMAIN 69..296
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 84
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 88
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 91
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 128
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 159
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 219
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 291
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 348 AA; 37517 MW; D44248F9211BEDEE CRC64;
MTATTHAGET VATISADTLR QTARRFTEPA PATKPGDWTV AEVAALYALP FNDLLFRAQQ
VHREHFDANA VQLSTLLSIK TGGCEEDCGY CPQSAHHDAG VTAGKLMALD EVLEAARAAK
ASGAGRFCMG AAWRSPKDRH LEPVIEMVKE VKAMGLETCV TLGMLEAEQA QRLKDAGLDY
YNHNLDTSPE FYGEIIGTRT YQDRLDTIGH VREAGINVCC GGIVGMGESR EARAGLIAQL
ANLDPYPESV PINNLVAVKG TPLADTAPID PFEFVRTIAV ARITMPSAMV RLSAGRETMD
DALQALCFMA GANSIFYGER LLTTANPQAD RDRALLARLD IRTEGYAG
//
