ID BIOB_CHLPN Reviewed; 331 AA. AC Q9Z6L5; Q7AHW6; Q7BWK9; Q7DE82; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 24-JAN-2024, entry version 147. 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=CPn_1044, CP_0808, CpB1084; OS Chlamydia pneumoniae (Chlamydophila pneumoniae). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=83558; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CWL029; RX PubMed=10192388; DOI=10.1038/7716; RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.; RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; RL Nat. Genet. 21:385-389(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J138; RX PubMed=10871362; DOI=10.1093/nar/28.12.2311; RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from RT Japan and CWL029 from USA."; RL Nucleic Acids Res. 28:2311-2314(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TW-183; RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.; RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with RT other Chlamydia strains based on whole genome sequence analysis."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR39; RX PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., RA Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae RT AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). 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; AE001363; AAD19181.1; -; Genomic_DNA. DR EMBL; AE002161; AAF38605.1; -; Genomic_DNA. DR EMBL; AE009440; AAP99013.1; -; Genomic_DNA. DR EMBL; BA000008; BAA99251.1; -; Genomic_DNA. DR PIR; A86621; A86621. DR PIR; H72004; H72004. DR RefSeq; NP_225238.1; NC_000922.1. DR RefSeq; WP_010883677.1; NZ_LN847257.1. DR AlphaFoldDB; Q9Z6L5; -. DR SMR; Q9Z6L5; -. DR STRING; 406984.CPK_ORF00471; -. DR GeneID; 45051102; -. DR KEGG; cpa:CP_0808; -. DR KEGG; cpj:bioB; -. DR KEGG; cpn:CPn_1044; -. DR KEGG; cpt:CpB1084; -. DR PATRIC; fig|115713.3.peg.1143; -. DR eggNOG; COG0502; Bacteria. DR HOGENOM; CLU_033172_1_2_0; -. DR OrthoDB; 9786826at2; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000000583; Chromosome. DR Proteomes; UP000000801; 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; SFLDG01278; biotin_synthase_like; 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..331 FT /note="Biotin synthase" FT /id="PRO_0000381303" FT DOMAIN 39..264 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 54 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 58 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 61 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 98 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 130 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 190 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" FT BINDING 262 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01694" SQ SEQUENCE 331 AA; 37075 MW; 7ADA2C0E732C1370 CRC64; MREETVSWSL EDIREIYHTP VFELIHKANA ILRSNFLHSE LQTCYLISIK TGGCVEDCAY CAQSSRYHTH VTPEPMMKIV DVVERAKRAV ELGATRVCLG AAWRNAKDDR YFDRVLAMVK SITDLGAEVC CALGMLSEEQ AKKLYDAGLY AYNHNLDSSP EFYETIITTR SYEDRLNTLD VVNKSGISTC CGGIVGMGES EEDRIKLLHV LATRDHIPES VPVNLLWPID GTPLQDQPPI SFWEVLRTIA TARVVFPRSM VRLAAGRAFL TVEQQTLCFL AGANSIFYGD KLLTVENNDI DEDAEMIKLL GLIPRPSFGI ERGNPCYANN S //