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Protein

Biotin synthase

Gene

bioB

Organism
Prochlorococcus marinus (strain MIT 9515)
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 bindingi61Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi65Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi68Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi105Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi137Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi197Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi269Iron-sulfur 2 (2Fe-2S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

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:P9515_11841
OrganismiProchlorococcus marinus (strain MIT 9515)
Taxonomic identifieri167542 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001589 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003815411 – 335Biotin synthaseAdd BLAST335

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi167542.P9515_11841.

Structurei

3D structure databases

ProteinModelPortaliA2BX80.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QSQ. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239957.
KOiK01012.
OMAiPFDFIRM.
OrthoDBiPOG091H01DF.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB. 1 hit.
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.

A2BX80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINSDNQKFS KIRFDWARDE ILEILNYPLV DLMWEAQIIH RRFNEYKVQL
60 70 80 90 100
ASLFSVKTGG CEENCSYCSQ SIYSSSQIKS HPQFEVEAVL NRAKTAKKEG
110 120 130 140 150
ADRFCMGWAW REIRDGKPFN SMLEMVKGVK ELGMEACVTA GMLTDEQALR
160 170 180 190 200
LADAGLTAYN HNLDTSPEYY KNIITTRTYQ DRLETIKRVR NAGINVCCGG
210 220 230 240 250
IIGLGENNGD RASLLEVLSN MNPHPESVPI NSLVAIEGTG LEEKKEIDSI
260 270 280 290 300
EMIRMIATAR ILMPKSKIRL SAGREKLTKE AQIICFQCGA NSIFYGDELL
310 320 330
TTSNPSFQDD RKLLKDVGVL FNKDFEYCDK TVSTV
Length:335
Mass (Da):37,831
Last modified:February 20, 2007 - v1
Checksum:i380F819F0C8C33E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM72391.1.
RefSeqiWP_011820491.1. NC_008817.1.

Genome annotation databases

EnsemblBacteriaiABM72391; ABM72391; P9515_11841.
KEGGipmc:P9515_11841.
PATRICi23015984. VBIProMar113831_1214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM72391.1.
RefSeqiWP_011820491.1. NC_008817.1.

3D structure databases

ProteinModelPortaliA2BX80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167542.P9515_11841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM72391; ABM72391; P9515_11841.
KEGGipmc:P9515_11841.
PATRICi23015984. VBIProMar113831_1214.

Phylogenomic databases

eggNOGiENOG4107QSQ. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239957.
KOiK01012.
OMAiPFDFIRM.
OrthoDBiPOG091H01DF.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB. 1 hit.
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...

Entry informationi

Entry nameiBIOB_PROM5
AccessioniPrimary (citable) accession number: A2BX80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 20, 2007
Last modified: November 2, 2016
This is version 67 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

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.