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A7I1A0 (BIOB_CAMHC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin synthase

EC=2.8.1.6
Gene names
Name:bioB
Ordered Locus Names:CHAB381_0711
OrganismCampylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A) [Complete proteome] [HAMAP]
Taxonomic identifier360107 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length324 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 – 324324Biotin synthase HAMAP-Rule MF_01694
PRO_0000381283

Sites

Metal binding611Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding651Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding681Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1051Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1381Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1981Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2681Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A7I1A0 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 649526ECC70354B9

FASTA32435,899
        10         20         30         40         50         60 
MDLQKIKNQI LDGRNLCIED AYELENAPLN ELLEAANEVR AKFCGNYFNF CSIINVKSGK 

        70         80         90        100        110        120 
CSENCKYCAQ SAHFDTKCEI YDILPFEKIM PLAKLNDDAG VARFSLVASG KGLHKKDDLQ 

       130        140        150        160        170        180 
KVIEIYKKLK SHTKFHLCAS FGIVSKEILA ELKKSGVKTY HHNLETSRKF FPKICTTHTY 

       190        200        210        220        230        240 
DDRINTIKSA LCVGLDVCSG GIFGLGESLK DRIDMAYELK NLKVSSVPIN ILTPIKGTPL 

       250        260        270        280        290        300 
ENSAPLCVDE ILRSIAIFRL ILPHVFLRLA GGRNNLKNSV KTALNGGINS AITGDFLTTC 

       310        320 
GDVAQSDKNL VSECGFVYKK SFDV 

« Hide

References

[1]"Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000776 Genomic DNA. Translation: ABS52409.1.
RefSeqYP_001406291.1. NC_009714.1.

3D structure databases

ProteinModelPortalA7I1A0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360107.CHAB381_0711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS52409; ABS52409; CHAB381_0711.
GeneID5408849.
KEGGcha:CHAB381_0711.
PATRIC20039572. VBICamHom81367_0687.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBPRK06256.

Enzyme and pathway databases

BioCycCHOM360107:GHCX-716-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_CAMHC
AccessionPrimary (citable) accession number: A7I1A0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 47 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