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A9BB12 (BIOB_PROM4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:P9211_10931
OrganismProchlorococcus marinus (strain MIT 9211) [Complete proteome] [HAMAP]
Taxonomic identifier93059 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length332 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 – 332332Biotin synthase HAMAP-Rule MF_01694
PRO_0000381540

Sites

Metal binding661Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1101Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1421Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2021Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2741Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BB12 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 881F044B2C7323C6

FASTA33236,790
        10         20         30         40         50         60 
MTLINYKAAD QKEVQLRYDW SFSEVESLLQ KPLMDLLWDA QRVHRLTNPG YKVQLASLLS 

        70         80         90        100        110        120 
VKTGGCEEDC AYCSQSIHNS SDITSYSDFE VEEVLKRAKT AKDAGADRFC MGWAWREIRD 

       130        140        150        160        170        180 
GQPFESMLKM VRGVRDLGME ACVTAGMLTD NQALRLAEAG LTAYNHNLDT SPENYDQIIT 

       190        200        210        220        230        240 
TRTYQERIET LERVRSAGIT LCTGGIIGLG ESLKDRASLL KVLANMSPHP ESVPINALVA 

       250        260        270        280        290        300 
VEGTPLQDLP SIDPIEMVRM VATARILMPL SRVRLSAGRE QLGDEAQILC FLAGADSIFY 

       310        320        330 
GDTLLTTSNP AIQADRELLS KAGVQVNWSL HE 

« 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 9211.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000878 Genomic DNA. Translation: ABX09024.1.
RefSeqYP_001550978.1. NC_009976.1.

3D structure databases

ProteinModelPortalA9BB12.
SMRA9BB12. Positions 17-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93059.P9211_10931.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX09024; ABX09024; P9211_10931.
GeneID5731333.
KEGGpmj:P9211_10931.
PATRIC22987760. VBIProMar136502_1156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2391410.

Enzyme and pathway databases

BioCycPMAR93059:GHJV-1119-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_PROM4
AccessionPrimary (citable) accession number: A9BB12
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 45 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