Q8E6Q1 (BIOB_STRA3) 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:	gbs0511

Organism

Streptococcus agalactiae serotype III (strain NEM316) [Complete proteome] [HAMAP]

Taxonomic identifier

211110 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › Streptococcus agalactiae › Streptococcus agalactiae serogroup III

Protein attributes

Sequence length	330 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.

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 – 330	330	Biotin synthase HAMAP-Rule MF_01694		PRO_0000381661
Sites
	Metal binding	68	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	72	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	75	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	112	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	274	1	Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8E6Q1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: F47B4AC1B7DC6F29	FASTA	330	37,337
	10 20 30 40 50 60 MSFQTNYIHL ADEILSGKTS ISYEQALEIL NSDENWWEIY AAALYLKNQV SRNNIRLNVL 70 80 90 100 110 120 LSAKQGLCAE NCGYCSQSKE STADIDKFGL LPQNVILKQA IVAHQNGASV FCIAMSGTKP 130 140 150 160 170 180 SKREIEQLCQ VIPEIKKSLP LEICLTAGFL DREQLHQLKQ AGIDRINHNL NTPEENYPNI 190 200 210 220 230 240 ATTHSFKDRC DTLERIHNED IDVCSGFICG MGESDEGLIT LAFRLKELNP YSIPVNFLLA 250 260 270 280 290 300 VEGTPLGKYN YLTPIKCLKI MAMLRFVFPF KELRLSAGRE VHFENFESLV TLLVDSTFLG 310 320 330 NYLTEGGRNQ HTDIEFLEKL QLNHTKKELI

References

[1]

"Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease." Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F. Mol. Microbiol. 45:1499-1513(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NEM316.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL766845 Genomic DNA. Translation: CAD46155.1.
RefSeq	NP_734976.1. NC_004368.1.
3D structure databases
HSSP	HSSP built from PDB template 1R30 based on UniProtKB P12996.
ProteinModelPortal	Q8E6Q1.
ModBase	Search...
Protein-protein interaction databases
STRING	211110.gbs0511.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD46155; CAD46155; CAD46155.
GeneID	1031523.
KEGG	san:gbs0511.
PATRIC	19636868. VBIStrAga3577_0526.
Organism-specific databases
GenoList	gbs0511.
CMR	Search...
Phylogenomic databases
eggNOG	COG0502.
HOGENOM	HOG000239958.
KO	K01012.
OMA	TSERYHD.
ProtClustDB	CLSK296924.
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_STRA3

Accession

Primary (citable) accession number: Q8E6Q1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program