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Q5F8G2 (BIOB_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:NGO0813
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length350 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 – 350350Biotin synthase HAMAP-Rule MF_01694
PRO_0000381493

Sites

Metal binding691Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding761Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1131Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1441Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2041Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2761Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5F8G2 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: CAD3FC7352529499

FASTA35038,781
        10         20         30         40         50         60 
MTVSPVALRR KTECKPHPTA RYWKKCDVEA LFGLPFLELV YQAAEVHRQN FNPREIQLST 

        70         80         90        100        110        120 
LLSIKTGGCP EDCAYCPQSA HHNTNLGKEQ MMDVDEIVEK AKIAKSRGAS RFCMGAAWRG 

       130        140        150        160        170        180 
PKPKDVETVS AIIKAVKGLG METCGTFGML EEGMAEDLKE AGLDYYNHNL DTDPDRYNDI 

       190        200        210        220        230        240 
IHTRRHEDRM DTLGKVRNAG LKVCCGGIVG MNETRAERAG LIASLANLDP QPESVPINRL 

       250        260        270        280        290        300 
VKVEGTPLAD AEDLDWTEFV RTVSVARITM PQSYVRLSAG RSNMPEAMQA MCFMAGANSI 

       310        320        330        340        350 
FYGDKLLTTG NPDEDGDRIL MEKLNLYPLQ FEPEGEVAEV EKASGIKADY 

« Hide

References

[1]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004969 Genomic DNA. Translation: AAW89525.1.
RefSeqYP_207937.1. NC_002946.2.

3D structure databases

ProteinModelPortalQ5F8G2.
SMRQ5F8G2. Positions 23-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242231.NGO0813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW89525; AAW89525; NGO0813.
GeneID3281938.
KEGGngo:NGO0813.
PATRIC20334782. VBINeiGon24812_0961.

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2300453.

Enzyme and pathway databases

BioCycNGON242231:GI2G-767-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_NEIG1
AccessionPrimary (citable) accession number: Q5F8G2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 15, 2005
Last modified: February 19, 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