BIOB_NITMS
ID BIOB_NITMS Reviewed; 326 AA.
AC A9A5K6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Nmar_0821;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX12717.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A5K6; -.
DR SMR; A9A5K6; -.
DR STRING; 436308.Nmar_0821; -.
DR PRIDE; A9A5K6; -.
DR EnsemblBacteria; ABX12717; ABX12717; Nmar_0821.
DR KEGG; nmr:Nmar_0821; -.
DR eggNOG; arCOG00658; Archaea.
DR HOGENOM; CLU_033172_2_1_2; -.
DR OMA; ADRFCMG; -.
DR PhylomeDB; A9A5K6; -.
DR UniPathway; UPA00078; UER00162.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004076; F:biotin synthase activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
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; SFLDS00029; Radical_SAM; 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..326
FT /note="Biotin synthase"
FT /id="PRO_0000381503"
FT DOMAIN 50..279
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 145
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 204
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
FT BINDING 274
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694"
SQ SEQUENCE 326 AA; 36271 MW; 81B17EEB1B67D9ED CRC64;
MSTLEFIKEC QEKVFSGNHI TAEDAEKLLN IPEENLKDLA RCANEITRDF NGEKVDVEQL
NNIKKNACSE DCTFCGQSAF FDTGIETYQL PSPEEVVSKA QKAKEEGAES YCLVAAWREP
SRTDFEKVCK IITEINDKVG ISVECSLGFL TQEQAKKLKD LKVKRYNHNL ETAKSKFPEI
CTTHTYEDRL ETLGIARDAG LELCTGGIIG LGETREQRLE LTLELARLYP EEVTINILVP
VPGTPLELQT DLPNSEIVRM FSVIRFLLPE SVIKISGGRE TNLEDSGEEL LQSGANGIIT
SGYLTMGGNE AQKDHAMIEK IGLKSQ
