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Protein

Biotin synthase

Gene

bioB

Organism
Helicobacter hepaticus (strain ATCC 51449 / 3B1)
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 bindingi21Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi25Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi28Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi65Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi100Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi225Iron-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

BioCyciHHEP235279:GHUA-1771-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:HH_1731
OrganismiHelicobacter hepaticus (strain ATCC 51449 / 3B1)
Taxonomic identifieri235279 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000002495 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003814231 – 283Biotin synthaseAdd BLAST283

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi235279.HH1731.

Structurei

3D structure databases

ProteinModelPortaliQ7VFE6.
SMRiQ7VFE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CZF. Bacteria.
COG0502. LUCA.
KOiK01012.
OMAiADRFCMG.
OrthoDBiPOG091H01DF.

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.

Q7VFE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKISNEIFL CSICNVSSGD CPEDCKYCTQ SAHYGTQIQR YKNKSIDKIV
60 70 80 90 100
QEAKTLREYG ALGFCLVTAG RSLESQKCEY IAKAASAIKK ADLGLHIIAC
110 120 130 140 150
CGSADVDSLK YLKTNGVDSY NHNLETSKEF FPHICTTHTW KERFETCENT
160 170 180 190 200
LKAELGLLSG GIFGLGESWG DRIELLKHLQ ILSPHTSPLN FYIANESLPL
210 220 230 240 250
PMQTLSPQEA LECVTLAREY LPNTRLMIAG GREAVFGDNQ KPLFEAGING
260 270 280
VVLGDYLTTD GKAPKDDVAM IESYGYVAAT NCH
Length:283
Mass (Da):31,166
Last modified:October 1, 2003 - v1
Checksum:i84B9F5289D27EA69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017125 Genomic DNA. Translation: AAP78328.1.
RefSeqiWP_011116570.1. NC_004917.1.

Genome annotation databases

EnsemblBacteriaiAAP78328; AAP78328; HH_1731.
KEGGihhe:HH_1731.

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_HELHP
AccessioniPrimary (citable) accession number: Q7VFE6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 1, 2003
Last modified: June 7, 2017
This is version 97 of the entry and version 1 of the sequence. See 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