P53557 (BIOB_BACSU) 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:	BSU30200

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	335 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 Reference 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 – 335	335	Biotin synthase HAMAP-Rule MF_01694		PRO_0000185546
Sites
	Metal binding	65	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	69	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	109	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	141	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	201	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	271	1	Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P53557 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D4B2E1A53271ED26	FASTA	335	36,927
	10 20 30 40 50 60 MNQWMELADR VLAGAEVTDE EALSILHCPD EDILLLMHGA FHIRKHFYGK KVKLNMIMNA 70 80 90 100 110 120 KSGLCPENCG YCSQSAISKA PIESYRMVNK ETLLEGAKRA HDLNIGTYCI VASGRGPSNR 130 140 150 160 170 180 EVDQVVDAVQ EIKETYGLKI CACLGLLKPE QAKRLKDAGV DRYNHNLNTS QRNHSNITTS 190 200 210 220 230 240 HTYDDRVNTV EIAKESGLSP CSGAIIGMKE TKQDVIDIAK SLKALDADSI PVNFLHAIDG 250 260 270 280 290 300 TPLEGVNELN PLYCLKVLAL FRFINPSKEI RISGGREVNL RTLQPLGLYA ANSIFVGDYL 310 320 330 TTAGQEETED HKMLSDLGFE VESVEEMKAS LSAKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon." Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J. J. Bacteriol. 178:4122-4130(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U51868 Genomic DNA. Translation: AAB17461.1. AF008220 Genomic DNA. Translation: AAC00265.1. AL009126 Genomic DNA. Translation: CAB14998.1.
PIR	D69594.
RefSeq	NP_390898.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P53557.
SMR	P53557. Positions 15-323.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU30200.
Proteomic databases
PaxDb	P53557.
Protocols and materials databases
DNASU	938180.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB14998; CAB14998; BSU30200.
GeneID	938180.
KEGG	bsu:BSU30200.
PATRIC	18977942. VBIBacSub10457_3159.
Organism-specific databases
GenoList	BSU30200. [Micado]
Phylogenomic databases
eggNOG	COG0502.
HOGENOM	HOG000239958.
KO	K01012.
OMA	MKETKQD.
ProtClustDB	PRK06256.
Enzyme and pathway databases
BioCyc	BSUB:BSU30200-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_BACSU

Accession

Primary (citable) accession number: P53557

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program