Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B7JLW9

- BIOB_BACC0

UniProt

B7JLW9 - BIOB_BACC0

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Biotin synthase

Gene

bioB

Organism
Bacillus cereus (strain AH820)
Status
Reviewed - 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 = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation
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 bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi75 – 751Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi78 – 781Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi115 – 1151Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi147 – 1471Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi207 – 2071Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi277 – 2771Iron-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

BioCyciBCER405535:GHSL-4151-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:BCAH820_4138
OrganismiBacillus cereus (strain AH820)
Taxonomic identifieri405535 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001363: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Biotin synthasePRO_0000381218Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi405535.BCAH820_4138.

Structurei

3D structure databases

ProteinModelPortaliB7JLW9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiDETQALC.
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.

B7JLW9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKQVQTKRDW KKLAYDVVEE KMITKEDAIA ILEADDTEVL EIMNAAYIIR
60 70 80 90 100
HHYFGKKVKL NMIINTKSGL CPEDCGYCSQ SIISEAPIDK YAWLTQEKIV
110 120 130 140 150
EGAHEAIRRK AGTYCIVASG RRPTDKEVNH VIGAVKEIRE TTDLKICCCL
160 170 180 190 200
GFLNEDQAGR LAEAGVHRYN HNLNTHANNY ESICSTHTYD DRVDTVQKAK
210 220 230 240 250
QAGISPCSGA IFGMGETIEE RAEIAFELQR IDADSIPCNF LVAVKGTPLE
260 270 280 290 300
GQKELTPVEC LKVLAMMRFV NPTKEIRISG GREINLRSVQ PIGLFAANSI
310 320 330
FVGDYLTTAG QEPTADWGMI EDLGFEIEEC AL
Length:332
Mass (Da):36,996
Last modified:February 10, 2009 - v1
Checksum:i5C4BB89751C3CB96
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001283 Genomic DNA. Translation: ACK92404.1.
RefSeqiYP_002453088.1. NC_011773.1.

Genome annotation databases

EnsemblBacteriaiACK92404; ACK92404; BCAH820_4138.
GeneIDi7191650.
KEGGibcu:BCAH820_4138.
PATRICi18845244. VBIBacCer122868_4130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001283 Genomic DNA. Translation: ACK92404.1 .
RefSeqi YP_002453088.1. NC_011773.1.

3D structure databases

ProteinModelPortali B7JLW9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 405535.BCAH820_4138.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACK92404 ; ACK92404 ; BCAH820_4138 .
GeneIDi 7191650.
KEGGi bcu:BCAH820_4138.
PATRICi 18845244. VBIBacCer122868_4130.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239958.
KOi K01012.
OMAi DETQALC.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci BCER405535:GHSL-4151-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01694. BioB.
InterProi IPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view ]
Pfami PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF001619. Biotin_synth. 1 hit.
SMARTi SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00433. bioB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Bacillus cereus AH820."
    Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AH820.

Entry informationi

Entry nameiBIOB_BACC0
AccessioniPrimary (citable) accession number: B7JLW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: October 1, 2014
This is version 40 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

External Data

Dasty 3