A3DBD3 (BIOB_CLOTH) 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:	Cthe_0020

Organism

Clostridium thermocellum (strain ATCC 27405 / DSM 1237) [Complete proteome] [HAMAP]

Taxonomic identifier

203119 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium thermocellum

Protein attributes

Sequence length	320 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-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 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. HAMAP-Rule MF_01694
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: UniProtKB-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: UniProtKB-HAMAP iron ion binding Inferred from electronic annotation. Source: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 320	320	Biotin synthase HAMAP-Rule MF_01694		PRO_0000381323
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)
	A3DBD3 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: BC7DA44046DA398F	FASTA	320	35,743
	10 20 30 40 50 60 MDFLTLMENK LDEGRMITFE EAVELAKGKI EDEKLFLLAD KLCKKNMGRR VDLCSIINAK 70 80 90 100 110 120 SGGCSENCKF CAQSGHYDTG VKIYPLLDVD DVLKAAKENE KEGVHRFSLV TSGKSVSDEE 130 140 150 160 170 180 FEKILGIYSV LRKETNLKLC ASLGSLSYER AVRLKEAGVS MYHHNIETCR EYYPKICDTH 190 200 210 220 230 240 TYDDRINTVK NAAKAGLEIC CGGIIGMGES MEQRIKMAFE IRELGVKSVP INVLNPIKGT 250 260 270 280 290 300 PFENVRSLSP DEILRTIALF RLIMPYAHIR YAGGRMCLGE HQSKGFKAGV SAMLVGNYLT 310 320 TVGNKISDDL EMIQRMGLEI

References

[1]

"Complete sequence of Clostridium thermocellum ATCC 27405." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., Newcomb M., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27405 / DSM 1237.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000568 Genomic DNA. Translation: ABN51262.1.
RefSeq	YP_001036455.1. NC_009012.1.
3D structure databases
ProteinModelPortal	A3DBD3.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
STRING	203119.Cthe_0020.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABN51262; ABN51262; Cthe_0020.
GeneID	4808785.
KEGG	cth:Cthe_0020.
PATRIC	19513635. VBICloThe47081_0020.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0502.
HOGENOM	HOG000239958.
KO	K01012.
OMA	NCRFCAQ.
OrthoDB	EOG622PMP.
ProtClustDB	CLSK734793.
Enzyme and pathway databases
BioCyc	CTHE203119:GIW8-19-MONOMER.
UniPathway	UPA00078; UER00162.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01694. BioB.
InterPro	IPR013785. Aldolase_TIM. IPR010722. BATS_dom. 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_CLOTH

Accession

Primary (citable) accession number: A3DBD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 20, 2007
Last modified:	February 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program