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B4S0P9 (BIOB_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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 namesRecommended name:
Biotin synthase

EC=2.8.1.6
Gene names
Name:bioB
Ordered Locus Names:MADE_1007255
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length374 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 – 374374Biotin synthase HAMAP-Rule MF_01694
PRO_0000381194

Sites

Metal binding641Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding681Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding711Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1081Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1391Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1991Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2711Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S0P9 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 949F05B2DF1C24D2

FASTA37441,999
        10         20         30         40         50         60 
MTLAYAPTAQ TITIRNDWTK AEVEALFAMP FNDLLFNAQV VHRQHFNPNE VQVSTLLSIK 

        70         80         90        100        110        120 
TGACPEDCKY CPQSARYDTG LEKERLLEIE KVIQRAKEAK QVGSTRFCMG AAWRNPRDRD 

       130        140        150        160        170        180 
MPYILKMVEE VKSLGLETCM TLGMLTRDQA VALKQAGLDY YNHNLDTSPE YYGDIITTRT 

       190        200        210        220        230        240 
YEDRLNTLEN VRAAGMNVCS GGIVGMGETV SDRASMLVQL ANLPEQPQSV PINMLVKVKG 

       250        260        270        280        290        300 
TPLDSVEDLD YFEFIRTIAV ARIMMPKSHV RLSAGREAMN EQMQAMCFMA GANSIFYGCK 

       310        320        330        340        350        360 
LLTTSNPDTH EDVMLFKKLG INTERTRDYS DEAHQQVLEE EIAQQQEQAE GSNDLFIDAT 

       370 
KPKVAAKQQH ATEA 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEA97593.1.
RefSeqYP_004426591.1. NC_011138.3.

3D structure databases

ProteinModelPortalB4S0P9.
SMRB4S0P9. Positions 15-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314275.MADE_02211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA97593; AEA97593; MADE_1007255.
GeneID10556793.
KEGGamc:MADE_1007255.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
KOK01012.
OMARIMMPAS.

Enzyme and pathway databases

BioCycAMAC314275:GHA7-1469-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_ALTMD
AccessionPrimary (citable) accession number: B4S0P9
Secondary accession number(s): F2G6Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 46 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