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A8G5G3 (BIOB_PROM2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:P9215_12291
OrganismProchlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]
Taxonomic identifier93060 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length335 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 – 335335Biotin synthase HAMAP-Rule MF_01694
PRO_0000381538

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 binding1371Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1971Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2691Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A8G5G3 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 6B7FB559E82B4D97

FASTA33537,581
        10         20         30         40         50         60 
MANSNNQLLK EIRFDWNKEE ILEILNMPLI DLMWESQTIH RKFNKYDIQL ASLFSVKTGG 

        70         80         90        100        110        120 
CEENCSYCSQ SIYSASEIKS HPQFQVEEVL ARAQIAKKEG ADRFCMGWAW REIRDGKSFN 

       130        140        150        160        170        180 
AMLEMVSGVR DLGMEACVTA GMLTEEQAAR LADAGLTAYN HNLDTSPEHY KNIITTRTYQ 

       190        200        210        220        230        240 
DRLDTIKRVR NAGINVCCGG IIGLGETNGD RASLLKVLSN MNPHPESVPI NSLVAIEGTG 

       250        260        270        280        290        300 
LEDNQEIDSI EMIRMIATAR ILMPKSKIRL SAGREKLSKE AQILCFQCGA NSIFYGDELL 

       310        320        330 
TTSNPSFQSD RKLLKEVGVS FNKDFETREK TLSSL 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9215.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000825 Genomic DNA. Translation: ABV50844.1.
RefSeqYP_001484430.1. NC_009840.1.

3D structure databases

ProteinModelPortalA8G5G3.
SMRA8G5G3. Positions 13-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93060.P9215_12291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV50844; ABV50844; P9215_12291.
GeneID5615150.
KEGGpmh:P9215_12291.
PATRIC22991960. VBIProMar119824_1250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAIDLMWEA.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycPMAR93060:GI08-1262-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_PROM2
AccessionPrimary (citable) accession number: A8G5G3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 13, 2007
Last modified: May 14, 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