Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Biotin synthase

Gene

bioB

Organism
Propionibacterium acnes (strain KPA171202 / DSM 16379)
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 = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.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 bindingi59 – 591Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi63 – 631Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi103 – 1031Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi136 – 1361Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi196 – 1961Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi267 – 2671Iron-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

BioCyciPACN267747:GHO9-1432-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:PPA1407
OrganismiPropionibacterium acnes (strain KPA171202 / DSM 16379)
Taxonomic identifieri267747 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium
ProteomesiUP000000603: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358Biotin synthasePRO_0000381535Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267747.PPA1407.

Structurei

3D structure databases

ProteinModelPortaliQ6A7V7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
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.

Q6A7V7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTERGLRGES ITREEALEIL RSSDDELMSI IAAAGKVRRH FFDNRVRLNY
60 70 80 90 100
LVNLKSGLCP EDCSYCSQRL GSRAEIMKYS WADPQKVHDA VEAGIAGGAR
110 120 130 140 150
RVCMVASGHG PSRRDVERVN GMVRSLKADH PDVEVCVCLG FVDDEKAASI
160 170 180 190 200
KEAGADAYNH NANTARSHYG KICSTHSYED RMDTVEVLKR NGLSPCSGVI
210 220 230 240 250
AGMGETDEEF VDVIFDLRKH GVDSVPVNFL LPFEGTPLAG GAQHITPQWC
260 270 280 290 300
LKRLAMVRFA HPDSEVRAAA GREQHIRTMQ PLALEVVNSI FLGDYLTSEG
310 320 330 340 350
AAGAADLQMI EDGGFIPEGA DGQPMVHTDV NSHHSANLPV NAVPIRHRGI

GTEVPANA
Length:358
Mass (Da):38,940
Last modified:July 28, 2009 - v2
Checksum:iBD661CA1E0BF2183
GO

Sequence cautioni

The sequence AAT83158.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT83158.1. Different initiation.
RefSeqiYP_056116.1. NC_006085.1.

Genome annotation databases

EnsemblBacteriaiAAT83158; AAT83158; PPA1407.
GeneIDi2930948.
KEGGipac:PPA1407.
PATRICi23037585. VBIProAcn64440_1452.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT83158.1. Different initiation.
RefSeqiYP_056116.1. NC_006085.1.

3D structure databases

ProteinModelPortaliQ6A7V7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi267747.PPA1407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT83158; AAT83158; PPA1407.
GeneIDi2930948.
KEGGipac:PPA1407.
PATRICi23037585. VBIProAcn64440_1452.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciPACN267747:GHO9-1432-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. "The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
    Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
    Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KPA171202 / DSM 16379.

Entry informationi

Entry nameiBIOB_PROAC
AccessioniPrimary (citable) accession number: Q6A7V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 28, 2009
Last modified: January 7, 2015
This is version 80 of the entry and version 2 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.