P19206 (BIOB_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biotin synthase
EC=2.8.1.6

Gene names

Name:

bioB

Organism

Lysinibacillus sphaericus (Bacillus sphaericus)

Taxonomic identifier

1421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Lysinibacillus

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.

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	Direct protein sequencing
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 – 332	332	Biotin synthase HAMAP-Rule MF_01694		PRO_0000185545
Sites
	Metal binding	64	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	68	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	71	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	108	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	140	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	200	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	270	1	Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P19206 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: B5FF14F5CA9903EF	FASTA	332	37,015
	10 20 30 40 50 60 MNWLQLADEV IAGKVISDDE ALAILNSDDD DILKLMDGAF AIRKHYYGKK VKLNMIMNAK 70 80 90 100 110 120 SGYCPEDCGY CSQSSKSTAP IEKYPFITKE EILAGAKRAF ENKIGTYCIV ASGRGPTRKD 130 140 150 160 170 180 VNVVSEAVEE IKAKYGLKVC ACLGLLKEEQ AQQLKEAGVD RYNHNLNTSE RHHSYITTTH 190 200 210 220 230 240 TYEDRVNTVE VVKKHGISPC SGAIIGMKET KMDVVEIARA LHQLDADSIP VNFLHAIDGT 250 260 270 280 290 300 KLEGTQDLNP RYCLKVLALF RYMNPSKEIR ISGGREVNLG FLQPFGLYAA NSIFVGDYLT 310 320 330 TEGQEANSDY RMLEDLGFEI ELTQKQEEAF CS

References

[1]	"Cloning of the biotin synthetase gene from Bacillus sphaericus and expression in Escherichia coli and Bacilli." Ohsawa I., Speck D., Kisou T., Hayakawa K., Zinsius M., Gloeckler R., Lemoine Y., Kamogawa K. Gene 80:39-48(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: T-178-367.
[2]	"Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin." Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M., Villeval D., Kisou T., Kamogawa K., Lemoine Y. Gene 87:63-70(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M27867 Genomic DNA. Translation: AAA22268.1. M29292 Genomic DNA. Translation: AAB02327.1.
PIR	JS0274.
3D structure databases
ProteinModelPortal	P19206.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
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_LYSSH

Accession

Primary (citable) accession number: P19206

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program