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Q477A1 (BIOB_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biotin synthase

EC=2.8.1.6
Gene names
Name:bioB
Ordered Locus Names:Reut_A0150
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Biotin synthase HAMAP-Rule MF_01694
PRO_0000381573

Sites

Metal binding781Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding821Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding851Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1221Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1531Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2131Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2851Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q477A1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 917A19728C5815FC

FASTA34237,249
        10         20         30         40         50         60 
MNQAAQTVAT ISAEALRQTA RNTHALPEDA RWRVDDVAAL FALPFNDLLF RAQQVHRENF 

        70         80         90        100        110        120 
DANTVQLSTL LSIKTGGCEE DCGYCPQSAH HDAGVKAEKL MELDEVLEAA RAAKANGATR 

       130        140        150        160        170        180 
FCMGAAWRSP KDRHLEPVMD MVREVKAMGL ETCVTLGMLK AEQAQQLKDA GLDYYNHNLD 

       190        200        210        220        230        240 
TSPEFYGKII TTRTYQDRLD TIGHVRDAGI NVCCGGIVGM GESREARAGL IAQLANMDPY 

       250        260        270        280        290        300 
PESVPINNLV QVEGTPLAGT EALDPFEFVR TIAVARITMP GAMVRLSAGR EAMDEALQAL 

       310        320        330        340 
CFMAGANSIF YGEKLLTTGN PQADRDRALL ARLDIRAEGY AG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ59532.1.
RefSeqYP_294376.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ477A1.
SMRQ477A1. Positions 31-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A0150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59532; AAZ59532; Reut_A0150.
GeneID3610716.
KEGGreu:Reut_A0150.
PATRIC20225731. VBIRalEut24049_0744.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2309864.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-150-MONOMER.
UniPathwayUPA00078; UER00162.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01694. BioB.
InterProIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF001619. Biotin_synth. 1 hit.
SMARTSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00433. bioB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBIOB_CUPPJ
AccessionPrimary (citable) accession number: Q477A1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways