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Protein

Biotin synthase

Gene

bioB

Organism
Persephonella marina (strain DSM 14350 / EX-H1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.UniRule annotation

Catalytic activityi

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.UniRule annotation

Pathway: biotin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes biotin from 7,8-diaminononanoate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. ATP-dependent dethiobiotin synthetase BioD (bioD)
  2. Biotin synthase (bioB)
This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes biotin from 7,8-diaminononanoate, the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi110 – 1101Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi142 – 1421Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi202 – 2021Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi272 – 2721Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciPMAR123214:GIZP-1354-MONOMER.
UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
Ordered Locus Names:PERMA_1355
OrganismiPersephonella marina (strain DSM 14350 / EX-H1)
Taxonomic identifieri123214 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesHydrogenothermaceaePersephonella
ProteomesiUP000001366 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Biotin synthasePRO_0000381524Add
BLAST

Proteomic databases

PRIDEiC0QR28.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi123214.PERMA_1355.

Structurei

3D structure databases

ProteinModelPortaliC0QR28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Biotin synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiYNINIQV.
OrthoDBiEOG622PMP.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

C0QR28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDFIKGLAE RVLEGEKLSK EDGLKILSIP DEYLDLLVQE ASKVREAVFG
60 70 80 90 100
DEVEFCSLIN AKNGACSEDC SFCAQSSKYP TPINAYGLVP KKELVEGAQK
110 120 130 140 150
AVSIKANRYC IVTSGKRATK EEVEQIADAV REITENLPVR VCVSIGTVDE
160 170 180 190 200
EDLKLLKDSG VDRVNHNLET SERHFKNIVT THSYKERLET IKTVQKVGLS
210 220 230 240 250
TCTGGIFGIG ETDEDIVDLA SVYRELNVNS IPMNFLIPIP GTPLEGNKQL
260 270 280 290 300
TPQRCLKIIS LFKLFNPQAE LRLCGGREIN LREYHDTAME IANCVMAGGY
310 320 330
LTRAGRAPGK DEEMVRRLGR KLITGRDLFS KYKTAV
Length:336
Mass (Da):37,308
Last modified:May 5, 2009 - v1
Checksum:i8ADF65010B4CE95A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001230 Genomic DNA. Translation: ACO03951.1.
RefSeqiWP_012676190.1. NC_012440.1.
YP_002731124.1. NC_012440.1.

Genome annotation databases

EnsemblBacteriaiACO03951; ACO03951; PERMA_1355.
KEGGipmx:PERMA_1355.
PATRICi22916167. VBIPerMar119911_1373.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001230 Genomic DNA. Translation: ACO03951.1.
RefSeqiWP_012676190.1. NC_012440.1.
YP_002731124.1. NC_012440.1.

3D structure databases

ProteinModelPortaliC0QR28.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi123214.PERMA_1355.

Proteomic databases

PRIDEiC0QR28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACO03951; ACO03951; PERMA_1355.
KEGGipmx:PERMA_1355.
PATRICi22916167. VBIPerMar119911_1373.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiYNINIQV.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciPMAR123214:GIZP-1354-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 14350 / EX-H1.

Entry informationi

Entry nameiBIOB_PERMH
AccessioniPrimary (citable) accession number: C0QR28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: May 27, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.