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
Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
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: 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)DescriptionActionsGraphical viewLength
Metal bindingi16Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi20Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi23Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi60Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi95Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi153Iron-sulfur 2 (2Fe-2S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processBiotin biosynthesis
Ligand2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

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:C8J_1582
OrganismiCampylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
Taxonomic identifieri407148 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003812841 – 278Biotin synthaseAdd BLAST278

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA8FNZ2.
SMRiA8FNZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000239958.
KOiK01012.
OMAiADRFCMG.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB. 1 hit.
InterProiView protein in InterPro
IPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
PANTHERiPTHR22976. PTHR22976. 1 hit.
PfamiView protein in Pfam
PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SFLDiSFLDG01278. biotin_synthase_like. 1 hit.
SFLDS00029. Radical_SAM. 1 hit.
SMARTiView protein in SMART
SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

A8FNZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIMLCAISN IASGNCSEDC KYCTQSAHVK TDIQKYRRKE LSQIVLEAKM
60 70 80 90 100
AKKNEALGFC LVTAGLGLDD EKLEYVCEAA KAVQKEVPNL LLIACNGMAS
110 120 130 140 150
VEQLKELKKA GIFSYNHNLE TSKEFFPQIC TTHTWESRFQ TNLNAKEAGL
160 170 180 190 200
MLCCGGIYGM GESEEDRLSF RKSLQELQPF STPINFFIAN ENLKLQVPRL
210 220 230 240 250
SADEALKIVR DTKEALPQSV VMVAGGREVV LQERQYEIFQ AGAGAIVIGD
260 270
YLTTKGEEPS QDIIKLKEMG FTFASECH
Length:278
Mass (Da):30,928
Last modified:November 13, 2007 - v1
Checksum:i2B00338F88CA3F10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000814 Genomic DNA. Translation: ABV53179.1.
RefSeqiWP_002866830.1. NC_009839.1.

Genome annotation databases

EnsemblBacteriaiABV53179; ABV53179; C8J_1582.
KEGGicju:C8J_1582.

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 one 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.

Entry informationi

Entry nameiBIOB_CAMJ8
AccessioniPrimary (citable) accession number: A8FNZ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 13, 2007
Last modified: June 7, 2017
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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