Q4UM45 (BIOB_RICFE) 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:	RF_0527

Organism

Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) [Complete proteome] [HAMAP]

Taxonomic identifier

315456 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group › Rickettsia felis

Protein attributes

Sequence length	309 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 – 309	309	Biotin synthase HAMAP-Rule MF_01694		PRO_0000381590
Sites
	Metal binding	50	1	Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	54	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	94	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	125	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	185	1	Iron-sulfur 2 (2Fe-2S) By similarity
	Metal binding	257	1	Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4UM45 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 5E7BCC700C4B475B	FASTA	309	34,987
	10 20 30 40 50 60 MKKWTFDEAK EIFSFSFMEL VYQAQTIHRA NFDPNKIQIS SLLSIKTGSC PENCKFCPQS 70 80 90 100 110 120 SHYKTYVKKE PLMQIEDVIT AAKRAKAAGS TRFCMGAAWR GPRDEDLKLV CEMIKEVKKL 130 140 150 160 170 180 GLETCVTLGL LKEHQAVTLK EAGLDFYNHN IDTSEEFYNK IITTRTFQDR LDTLRYVRAS 190 200 210 220 230 240 GMKVCCGGIL GMGETNDDRI NMILTLANLE EPAESVTINK LIKIPGTPLE NVQDIDPFDF 250 260 270 280 290 300 VRVIALARIM IPKSYIRLSA GREQMSDELQ ALCIMAGVYS IFYGEKILTS ANPMPERDND LFQKLGIIH

References

[1]

"The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite." Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D. PLoS Biol. 3:1-12(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-1525 / URRWXCal2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000053 Genomic DNA. Translation: AAY61378.1.
RefSeq	YP_246543.1. NC_007109.1.
3D structure databases
HSSP	HSSP built from PDB template 1R30 based on UniProtKB P12996.
ProteinModelPortal	Q4UM45.
SMR	Q4UM45. Positions 2-308.
ModBase	Search...
Protein-protein interaction databases
STRING	315456.RF_0527.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAY61378; AAY61378; RF_0527.
GeneID	3401189.
KEGG	rfe:RF_0527.
PATRIC	17891578. VBIRicFel64634_0622.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0502.
HOGENOM	HOG000239957.
KO	K01012.
OMA	RIMMPAS.
ProtClustDB	CLSK2309044.
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_RICFE

Accession

Primary (citable) accession number: Q4UM45

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program