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B2RH08 (BIOB_PORG3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:PGN_0134
OrganismPorphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257) [Complete proteome] [HAMAP]
Taxonomic identifier431947 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length330 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 caution

The sequence BAG32653.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Biotin synthase HAMAP-Rule MF_01694
PRO_0000381532

Sites

Metal binding611Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding651Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding681Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1051Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1371Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1971Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2671Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2RH08 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 843537B62FD8FA5A

FASTA33036,649
        10         20         30         40         50         60 
MIQTIENRLI NGGEPTFEEA LLLASSADKE ALYETAHRIT RHFMGDKFDT CSIINAKSGN 

        70         80         90        100        110        120 
CPEDCKWCAQ SRHYATSIEK YGLLSATVCA EQAAYNRRQG IGRFSLVASG RTASMNEIRQ 

       130        140        150        160        170        180 
MAESFRTIKQ RTDIKCCASL GLLSEEKLQI LFDNGVTTYH CNMETAPSFF PSLCSTHTQE 

       190        200        210        220        230        240 
EKLATIRAAR RVGMRVCSGG IIGMGETMEQ RIEFAFFLHS INVYSIPINI LQPIPGTPLE 

       250        260        270        280        290        300 
KTPPLSEEEY LTTVALFRLI NPRAFLRFSG GRAQLSPAVQ RKAIYIGINA AITGDLLTTT 

       310        320        330 
GSKAAEDMQL ARECGFQVTN DTDWEVSYDH 

« Hide

References

[1]"Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis."
Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., Nakayama K.
DNA Res. 15:215-225(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33277 / DSM 20709 / JCM 12257.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009380 Genomic DNA. Translation: BAG32653.1. Different initiation.
RefSeqYP_001928250.1. NC_010729.1.

3D structure databases

ProteinModelPortalB2RH08.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING431947.PGN_0134.

Protocols and materials databases

DNASU6330269.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG32653; BAG32653; PGN_0134.
GeneID6330269.
KEGGpgn:PGN_0134.
PATRIC22973179. VBIPorGin26334_0128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycPGIN431947:GC9J-140-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_PORG3
AccessionPrimary (citable) accession number: B2RH08
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 48 of the entry and version 2 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