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Q5QZ16 (BIOB_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:IL1324
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length345 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 – 345345Biotin synthase HAMAP-Rule MF_01694
PRO_0000381432

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 binding1291Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1891Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2611Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QZ16 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 53147BA8366F50E7

FASTA34538,619
        10         20         30         40         50         60 
MPQIRNDWTI EEVQNLLQMP LNDLVFEAQT VHRQHFNPNE VQVSTLLSIK TGACPEDCKY 

        70         80         90        100        110        120 
CPQSAHYHTG LDRERLMAVE SVLAEAQAAK EKGASRFCMG AAWRNPKDRD MPYVIEMIKG 

       130        140        150        160        170        180 
VKALGLESCM TLGMLSNEQA KMLQQAGLDY YNHNLDTSPE FYGDIITTRT YQDRLNTLNN 

       190        200        210        220        230        240 
VRDAGMKVCA GGIVGMGESV TDRASLLVQL ANLPKHPESV PINMLVKVEG TPFAKLEDLD 

       250        260        270        280        290        300 
NFEFVRTVAV ARILMPASHV RLSAGREDMN DEMQALCFLA GANSIFYGEK LLTTANPEAD 

       310        320        330        340 
ADLRLFERLG IKPEQRDGYD DEVHTAVIED AIKEQQNPVR YYDAS 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV82164.1.
RefSeqYP_155713.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QZ16.
SMRQ5QZ16. Positions 5-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL1324.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV82164; AAV82164; IL1324.
GeneID3173798.
KEGGilo:IL1324.
PATRIC22140723. VBIIdiLoi21852_1325.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMARIMMPAS.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycILOI283942:GI0U-1333-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_IDILO
AccessionPrimary (citable) accession number: Q5QZ16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 65 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