A3M4U4 (BIOB_ACIBT) 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:	A1S_1511

Organism

Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]

Taxonomic identifier

400667 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex › Acinetobacter baumannii

Protein attributes

Sequence length	329 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 – 329	329	Biotin synthase HAMAP-Rule MF_01694		PRO_0000381172
Sites
	Metal binding	53	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	57	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	60	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	97	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	128	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	188	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	260	1	Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3M4U4 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: BB5D85217A783FF3	FASTA	329	36,659
	10 20 30 40 50 60 MTLRNDWTRE EIQALYEQPF LDLVFKAQQV HREHFTANTI QVSTLLSIKT GKCPEDCKYC 70 80 90 100 110 120 SQSAHYDSKL EAEKRIAVEK VISEAKAAKD SGSSRFCMGA AWRNPHERDM PYVLEMVREV 130 140 150 160 170 180 KALGMETCMT LGMLNQSQAE RLKDAGLDYY NHNLDTSREY YSHIISTRTF DDRLNTLDYV 190 200 210 220 230 240 RQAGMKVCSG GIVGLGESRE DRIGLLHELA TLPIHPESVP INMLVPIEGT PLADVEKLDV 250 260 270 280 290 300 IEWIRTIAVA RIIMPHSYIR LSAGRESLSD SDQALAFMAG ANSLFSGDKL LTTPNAGEGK 310 320 DQALFNKLGL TAEKPKPTVS DLSVDAMSA

References

[1]

"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000521 Genomic DNA. Translation: ABO11938.2.
3D structure databases
ProteinModelPortal	A3M4U4.
ModBase	Search...
Protein-protein interaction databases
STRING	400667.A1S_1511.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	20719266. VBIAciBau103176_1541.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0502.
HOGENOM	HOG000239957.
ProtClustDB	CLSK2307451.
Enzyme and pathway databases
BioCyc	ABAU400667:GI0Q-1529-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_ACIBT

Accession

Primary (citable) accession number: A3M4U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	September 2, 2008
Last modified:	May 1, 2013
This is version 46 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program