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
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
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 bindingi63 – 631Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi67 – 671Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi139 – 1391Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi199 – 1991Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi269 – 2691Iron-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

BioCyciPTHE370438:GCGQ-539-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:PTH_0521
OrganismiPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Taxonomic identifieri370438 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum
ProteomesiUP000006556 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Biotin synthasePRO_0000381523Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi370438.PTH_0521.

Structurei

3D structure databases

ProteinModelPortaliA5D4Y6.
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.

A5D4Y6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNELVKKIK SGLEITFEEA LALGGLDEDR LNELFLAALQ VNRHFHGNRV
60 70 80 90 100
DLCSIVNARS GRCSEDCAFC AQSGHYRTEA PVYPLLSKEE ILERAREMEL
110 120 130 140 150
RGARRFALVT SGRGISESDF EKVLDIYQML KEKTGLGLCA SLGIIGYDKA
160 170 180 190 200
VRLKEAGVGM YHHNLETCRS YFPHICTTHS FDERVETVKA AKEAGLEVCS
210 220 230 240 250
GGIIGLGESW RHRVEMAFHL KELGVASVPI NILTPVKGTP LWGRPLLEPV
260 270 280 290 300
EVLRTAAMFR LVLPGALIRL CGGREAALRD LQPLALLAGV NALMVGNYLT
310 320
TSGRRVEDDL QMVADLKLSV M
Length:321
Mass (Da):35,453
Last modified:June 12, 2007 - v1
Checksum:iF280BD8D6C62A033
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009389 Genomic DNA. Translation: BAF58702.1.
RefSeqiYP_001211071.1. NC_009454.1.

Genome annotation databases

EnsemblBacteriaiBAF58702; BAF58702; PTH_0521.
KEGGipth:PTH_0521.
PATRICi22907920. VBIPelThe8413_0582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009389 Genomic DNA. Translation: BAF58702.1.
RefSeqiYP_001211071.1. NC_009454.1.

3D structure databases

ProteinModelPortaliA5D4Y6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi370438.PTH_0521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF58702; BAF58702; PTH_0521.
KEGGipth:PTH_0521.
PATRICi22907920. VBIPelThe8413_0582.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciPTHE370438:GCGQ-539-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 genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
    Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
    Genome Res. 18:442-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13744 / JCM 10971 / SI.

Entry informationi

Entry nameiBIOB_PELTS
AccessioniPrimary (citable) accession number: A5D4Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 12, 2007
Last modified: April 1, 2015
This is version 57 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.