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Protein

Biotin synthase

Gene

bioB

Organism
Prochlorococcus marinus (strain MIT 9215)
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

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:P9215_12291
OrganismiProchlorococcus marinus (strain MIT 9215)
Taxonomic identifieri93060 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000002014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003815381 – 335Biotin synthaseAdd BLAST335

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi93060.P9215_12291.

Structurei

3D structure databases

ProteinModelPortaliA8G5G3.
SMRiA8G5G3.
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.
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.
PTHR22976:SF32. PTHR22976:SF32. 1 hit.
PfamiView protein in Pfam
PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SFLDiSFLDF00272. biotin_synthase. 1 hit.
SFLDG01278. biotin_synthase_like. 1 hit.
SMARTiView protein in SMART
SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

A8G5G3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANSNNQLLK EIRFDWNKEE ILEILNMPLI DLMWESQTIH RKFNKYDIQL
60 70 80 90 100
ASLFSVKTGG CEENCSYCSQ SIYSASEIKS HPQFQVEEVL ARAQIAKKEG
110 120 130 140 150
ADRFCMGWAW REIRDGKSFN AMLEMVSGVR DLGMEACVTA GMLTEEQAAR
160 170 180 190 200
LADAGLTAYN HNLDTSPEHY KNIITTRTYQ DRLDTIKRVR NAGINVCCGG
210 220 230 240 250
IIGLGETNGD RASLLKVLSN MNPHPESVPI NSLVAIEGTG LEDNQEIDSI
260 270 280 290 300
EMIRMIATAR ILMPKSKIRL SAGREKLSKE AQILCFQCGA NSIFYGDELL
310 320 330
TTSNPSFQSD RKLLKEVGVS FNKDFETREK TLSSL
Length:335
Mass (Da):37,581
Last modified:November 13, 2007 - v1
Checksum:i6B7FB559E82B4D97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000825 Genomic DNA. Translation: ABV50844.1.
RefSeqiWP_002808166.1. NC_009840.1.

Genome annotation databases

EnsemblBacteriaiABV50844; ABV50844; P9215_12291.
KEGGipmh:P9215_12291.

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_PROM2
AccessioniPrimary (citable) accession number: A8G5G3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 13, 2007
Last modified: June 7, 2017
This is version 66 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

Documents

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