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Protein

Biotin synthase

Gene

bioB

Organism
Ehrlichia ruminantium (strain Welgevonden)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi59 – 591Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi99 – 991Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi130 – 1301Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi190 – 1901Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi262 – 2621Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. biotin synthase activity Source: UniProtKB-HAMAP
  4. iron ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciERUM254945:GJ2L-714-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:Erum6500, ERWE_CDS_06820
OrganismiEhrlichia ruminantium (strain Welgevonden)
Taxonomic identifieri254945 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia
ProteomesiUP000001021: Chromosome, UP000006739: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Biotin synthasePRO_0000381377Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi254945.Erum6500.

Structurei

3D structure databases

ProteinModelPortaliQ5HAN0.
SMRiQ5HAN0. Positions 6-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
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.

Q5HAN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCTSIRHDWQ LPEVLELFNL PFNDLILNAH LIHRKFFNSN EIQIAGLLNI
60 70 80 90 100
KTGGCPENCK YCSQSAHYKT QLKKEDLLNI ETIKEAIKKA KVNGIDRFCF
110 120 130 140 150
AAAWRQIRDR DIEYICNIIS LIKSENLESC ASLGMVTLEQ AKKLKTAGLD
160 170 180 190 200
FYNHNIDTSR DFYYNVTTTR SYDDRLSSLN NISEAEINIC SGGILGLGES
210 220 230 240 250
IEDRAKMLLT LANLKKHPKS VPINRLVPIK GTPFENNPKI SNIDFIRTIA
260 270 280 290 300
VARILMPESY VRLAAGRESM SHEMQALCLF AGANSLFYGE KLLTTPNADC
310 320
NDDKNLLSKL GVKTKQAVFF DS
Length:322
Mass (Da):36,318
Last modified:February 15, 2005 - v1
Checksum:iF8CB0E1BDCFB4541
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR767821 Genomic DNA. Translation: CAH58382.1.
CR925678 Genomic DNA. Translation: CAI27176.1.
RefSeqiWP_011155330.1. NC_006832.1.
YP_180514.1. NC_005295.2.
YP_197558.1. NC_006832.1.

Genome annotation databases

EnsemblBacteriaiCAH58382; CAH58382; Erum6500.
CAI27176; CAI27176; ERWE_CDS_06820.
GeneIDi3233288.
3260991.
KEGGieru:Erum6500.
erw:ERWE_CDS_06820.
PATRICi20581228. VBIEhrRum92411_0721.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR767821 Genomic DNA. Translation: CAH58382.1.
CR925678 Genomic DNA. Translation: CAI27176.1.
RefSeqiWP_011155330.1. NC_006832.1.
YP_180514.1. NC_005295.2.
YP_197558.1. NC_006832.1.

3D structure databases

ProteinModelPortaliQ5HAN0.
SMRiQ5HAN0. Positions 6-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi254945.Erum6500.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH58382; CAH58382; Erum6500.
CAI27176; CAI27176; ERWE_CDS_06820.
GeneIDi3233288.
3260991.
KEGGieru:Erum6500.
erw:ERWE_CDS_06820.
PATRICi20581228. VBIEhrRum92411_0721.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciERUM254945:GJ2L-714-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: Welgevonden.
  2. "Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
    Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
    J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Welgevonden.

Entry informationi

Entry nameiBIOB_EHRRW
AccessioniPrimary (citable) accession number: Q5HAN0
Secondary accession number(s): Q5FD99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 15, 2005
Last modified: March 4, 2015
This is version 81 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

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.