Q2T1Q4 (BIOB_BURTA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biotin synthase
EC=2.8.1.6

Gene names

Name:	bioB
Ordered Locus Names:	BTH_I0337

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group › Burkholderia thailandensis

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism By similarity. HAMAP-Rule MF_01694
Catalytic activity	Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_01694
Cofactor	Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity. Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine By similarity.
Pathway	Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. HAMAP-Rule MF_01694
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the radical SAM superfamily. Biotin synthase family.
Sequence caution	The sequence ABC36299.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Biotin biosynthesis
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	biotin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW biotin synthase activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 336	336	Biotin synthase HAMAP-Rule MF_01694		PRO_0000381276
Sites
	Metal binding	69	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	73	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	76	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	113	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	144	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	204	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	276	1	Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2T1Q4 [UniParc]. Last modified July 28, 2009. Version 2. Checksum: 5BC1B6DB549064CE	FASTA	336	36,766
	10 20 30 40 50 60 MTEAQTACPT TETPVAAPVA PRWRVADVIA LYELPFNDLL FRAQQTHREH FDANAIQLST 70 80 90 100 110 120 LLSIKTGGCE EDCGYCSQSA HHDTGLKAEK LMEVDAVLAA ARTAKENGAT RFCMGAAWRN 130 140 150 160 170 180 PKDRHIEPIK EMIRGVKDMG LETCVTLGML EEHQAKALAE AGLDYYNHNL DTSPEFYGQI 190 200 210 220 230 240 ISTRTYQDRL DTLERVRDAG INVCCGGIIG MGESRRERAG LIAQLANMNP YPESVPINNL 250 260 270 280 290 300 VAIEGTPLEN AQALDPFEFV RTIAVARITM PKAMVRLSAG REQLDDSMQA LCFLAGANSM 310 320 330 FYGDVLLTTG NPRAEADRKL LARLGMSATE ATQLSA

References

[1]

"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies." Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D. BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000086 Genomic DNA. Translation: ABC36299.1. Different initiation.
RefSeq	YP_440895.1. NC_007651.1.
3D structure databases
ProteinModelPortal	Q2T1Q4.
ModBase	Search...
Protein-protein interaction databases
STRING	271848.BTH_I0337.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABC36299; ABC36299; BTH_I0337.
GeneID	3846946.
KEGG	bte:BTH_I0337.
PATRIC	19303362. VBIBurTha36512_3000.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0502.
HOGENOM	HOG000239957.
KO	K01012.
ProtClustDB	CLSK2391468.
Enzyme and pathway databases
BioCyc	BTHA271848:GJMY-337-MONOMER.
UniPathway	UPA00078; UER00162.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01694. BioB.
InterPro	IPR013785. Aldolase_TIM. IPR010722. Biotin/thiamin_synth-assoc. IPR002684. Biotin_synth/BioAB. IPR024177. Biotin_synthase. IPR006638. Elp3/MiaB/NifB. IPR007197. rSAM. [Graphical view]
Pfam	PF06968. BATS. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF001619. Biotin_synth. 1 hit.
SMART	SM00876. BATS. 1 hit. SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00433. bioB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BIOB_BURTA

Accession

Primary (citable) accession number: Q2T1Q4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	July 28, 2009
Last modified:	May 1, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program