BIOB_NITWN
ID BIOB_NITWN Reviewed; 341 AA.
AC Q3SW30;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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}; OrderedLocusNames=Nwi_0243;
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000115; ABA03511.1; -; Genomic_DNA.
DR RefSeq; WP_011313577.1; NC_007406.1.
DR AlphaFoldDB; Q3SW30; -.
DR SMR; Q3SW30; -.
DR STRING; 323098.Nwi_0243; -.
DR EnsemblBacteria; ABA03511; ABA03511; Nwi_0243.
DR KEGG; nwi:Nwi_0243; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_033172_1_2_5; -.
DR OMA; AMGVHRY; -.
DR OrthoDB; 940969at2; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000002531; 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 Gene3D; 3.20.20.70; -; 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/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR22976; PTHR22976; 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 SMART; SM00876; BATS; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00433; bioB; 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 Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..341
FT /note="Biotin synthase"
FT /id="PRO_0000381507"
FT DOMAIN 53..272
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 68
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 72
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 75
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 112
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 143
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 203
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 276
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
SQ SEQUENCE 341 AA; 37433 MW; 224545513FF7C5C0 CRC64;
MKSDPVSFDS SHDLMARPRH DWTRVEAETL YTTPFPDLLF QAQTIHRRHF DPNHVETASL
LSIKTGGCPE DCGYCAQSAH YDAGVKATKL MDKDAVLETA RRAKDAGAGR FCMAAAWRHP
KDRDLDRVCD MISAVKALGM ETCATLGMLT PEQARRLQEA GLDFYNHNVD TSPEFYDKII
TTRTMQDRIE TLACAREAGL KLCCGGIIGM GEQVGDRLGM LILLANLDEH PESVPINLWN
EVRGVPVNDT ADRPDPIALV RMIAVARIMM PKSVVRLSAG RQYMTDELQA LCFVAGANSI
FIGDVLLTTK NPATLRDAAL LDRLGMSSPL DGVKMPAASP S
