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B0CC69 (BIOB_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:AM1_1733
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris

Protein attributes

Sequence length346 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 – 346346Biotin synthase HAMAP-Rule MF_01694
PRO_0000381165

Sites

Metal binding541Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding581Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding611Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding981Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1301Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1901Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2601Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B0CC69 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 3D7A8E08BEFF488E

FASTA34638,083
        10         20         30         40         50         60 
MSEETFPQAS ALTLLSDPNI DLLSLVAAAG EVRMTYFGRQ VMLHRINDIQ NGLCPEDCGY 

        70         80         90        100        110        120 
CAQSKISDAP IKKYPLKSEE DIIQEAYEAK AKGVYRYCMV SSGRGPTAER TEHLAHIIRR 

       130        140        150        160        170        180 
IKNEVGIQTC LSAGLMDHEQ AAVLKEAGLD RLNHNLNTSE SHTPDIVTTH TFQDRINTLK 

       190        200        210        220        230        240 
AARSAGLDLC SGMIAGMGET DQDIVDIAYQ LHEYQVPSIP INFLIPISGN PIYDCNQLTP 

       250        260        270        280        290        300 
QRCLRILCLF RFVNPKAEIR IGGGREGHLR SLQALALYPA NSLFVEGYLA TRGHSVDQVY 

       310        320        330        340 
QLIHDAGFEV AGETSLTGDL SATSQFQLDD NPNILNPQTT ISFSNS 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW26754.1.
RefSeqYP_001516068.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0CC69.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING329726.AM1_1733.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW26754; ABW26754; AM1_1733.
GeneID5680549.
KEGGamr:AM1_1733.
PATRIC20617842. VBIAcaMar40141_1559.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBCLSK960888.

Enzyme and pathway databases

BioCycAMAR329726:GCZJ-1724-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_ACAM1
AccessionPrimary (citable) accession number: B0CC69
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 26, 2008
Last modified: February 19, 2014
This is version 46 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