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Q5PA14 (BIOB_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:AM969
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length324 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 – 324324Biotin synthase HAMAP-Rule MF_01694
PRO_0000381199

Sites

Metal binding521Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding561Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding591Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding961Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1271Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1871Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2591Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PA14 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 264C5DEC6C28DAAA

FASTA32436,039
        10         20         30         40         50         60 
MIRNNWTLEE ALELFRMPFS DLILKAHSVH VQNFRNNEVQ VAALMNIKTG SCPENCRYCA 

        70         80         90        100        110        120 
QSAHYNTGLE KKSLSTVEEV KTAAKRAKEI GADRFCFAAA WRNLHDRDLE KICQFVEAIK 

       130        140        150        160        170        180 
SEGLESCASL GMLKLDQAQK LKESGLDFYN HNVDTSREFY HNVVTTRTYE ERLETVRNVQ 

       190        200        210        220        230        240 
QAGIKVCCGG ILGMGESTED RASMLVTLAN LEQHPLSVPI NRLVPIEGTP MEGNPKIDNI 

       250        260        270        280        290        300 
DFVRTIAVAR IMMPASYVRL AAGRGEMSEE MQALCMLAGA NSIFCGEKLL TTPNARPEDD 

       310        320 
QRLFSQLGIT PSRAACTTSD AQLA 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86866.1.
RefSeqYP_154121.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PA14.
SMRQ5PA14. Positions 3-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234826.AM969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV86866; AAV86866; AM969.
GeneID3171351.
KEGGama:AM969.
PATRIC20947867. VBIAnaMar46146_0846.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMARIMMPAS.
OrthoDBEOG622PMP.

Enzyme and pathway databases

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_ANAMM
AccessionPrimary (citable) accession number: Q5PA14
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 67 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