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B1Y502 (BIOB_LEPCP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

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_0000381446

Sites

Metal binding741Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding781Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding811Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1181Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1491Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2091Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2811Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B1Y502 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 1551BA337F91B5BE

FASTA34537,438
        10         20         30         40         50         60 
MTTATISLST LQASRPSVAA RADAAARWRV ADVEALYALP FMDLLFQAQQ VHRAHFDANE 

        70         80         90        100        110        120 
VQLSTLLSIK TGGCAEDCGY CPQSAHFDTA VEASKLMPID EVLDAANAAK AQGATRFCMG 

       130        140        150        160        170        180 
AAWRSPKERD MERVTEMVRE VRALGLETCM TLGMLDGEQA RELKDAGLDY YNHNLDSAPD 

       190        200        210        220        230        240 
FYGQVISTRT YQDRLDTLGN VRDAGINVCC GGIVGMGESR TQRAGLIAQL ANLSPYPESV 

       250        260        270        280        290        300 
PINNLVPVPG TPLADAEPID PFEFVRTIAV ARITMPTTMV RLSAGREQMD EALQALCFAA 

       310        320        330        340 
GANSIFYGDK LLTTSNPQAA RDRALFERLG LRVQGERPAV RTSDN 

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001013 Genomic DNA. Translation: ACB35898.1.
RefSeqYP_001792663.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y502.
SMRB1Y502. Positions 27-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395495.Lcho_3644.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB35898; ACB35898; Lcho_3644.
GeneID6162681.
KEGGlch:Lcho_3644.
PATRIC22397719. VBILepCho83238_3680.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2314514.

Enzyme and pathway databases

BioCycLCHO395495:GHYL-3692-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_LEPCP
AccessionPrimary (citable) accession number: B1Y502
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 43 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