Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A3PH74 (BIOB_RHOS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Rsph17029_0574
OrganismRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) [Complete proteome] [HAMAP]
Taxonomic identifier349101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length328 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 – 328328Biotin synthase HAMAP-Rule MF_01694
PRO_0000381586

Sites

Metal binding561Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding601Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding631Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1001Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1311Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1911Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2641Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PH74 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 401CE37238D785E0

FASTA32835,442
        10         20         30         40         50         60 
MIRPALRTDW TVEEARAIHA LPFPELMHRA QTLHRAHFDP TAIETASLLS IKTGGCPEDC 

        70         80         90        100        110        120 
GYCSQSAHHD TGVKATKLMA EEEVLAAARR AKAAGAQRFC MGAAWRSPKD RDMDQLCDMV 

       130        140        150        160        170        180 
RGVADLGLET CMTLGMLSPG QVARLKAAGL DFYNHNIDTS PAYYAQIAST RTMEDRLETV 

       190        200        210        220        230        240 
EQVRRGGIKV CCGGILGMGE AEEDRIALLV TLATLPAHPD SVPVNLWNEI EGVPVQGRAR 

       250        260        270        280        290        300 
AVDPFALVRI VALARILMPA SVVRLSAGRT EMSDELQALC FLAGANSIFV GDQLLTTGNP 

       310        320 
AAWKDRDLLS RLGLHIAPAR ARPPVAAD 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17029 / ATH 2.4.9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000577 Genomic DNA. Translation: ABN75690.1.
RefSeqYP_001042462.1. NC_009049.1.

3D structure databases

ProteinModelPortalA3PH74.
SMRA3PH74. Positions 7-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349101.Rsph17029_0574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN75690; ABN75690; Rsph17029_0574.
GeneID4897552.
KEGGrsh:Rsph17029_0574.
PATRIC23168791. VBIRhoSph114483_0712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMATCENTLR.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycRSPH349101:GHC8-587-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_RHOS1
AccessionPrimary (citable) accession number: A3PH74
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 3, 2007
Last modified: May 14, 2014
This is version 50 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