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A7FVS6

- BIOB_CLOB1

UniProt

A7FVS6 - BIOB_CLOB1

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Protein

Biotin synthase

Gene

bioB

Organism
Clostridium botulinum (strain ATCC 19397 / Type A)
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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi106 – 1061Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi138 – 1381Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi198 – 1981Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi268 – 2681Iron-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

BioCyciCBOT441770:GH1E-2177-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:CLB_2200
OrganismiClostridium botulinum (strain ATCC 19397 / Type A)
Taxonomic identifieri441770 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000006379: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Biotin synthasePRO_0000381309Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi441770.CLB_2200.

Structurei

3D structure databases

ProteinModelPortaliA7FVS6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiIDLMWEA.
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.

A7FVS6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNIIKYKKK ILNGDLLTKE EVEELLEEDI TDLAATANEI RESLCGNKFD
60 70 80 90 100
LCTIINGKSG RCQENCKYCA QSAHFDTDII EYNILNSDRI INSAISNYNK
110 120 130 140 150
GVHRFSVVTS GRALNNNEVD TLCKTYSKLK ETCSIRLCAS HGLLKYEDLK
160 170 180 190 200
RLKDSGVTRY HNNLETSRKF FTKICTTHKY DDKIETIKNA KKAGIEICSG
210 220 230 240 250
GIIGLGETME DRIDMAFTLR ELSVESVPVN ILNPIKGTPL ENQEILSYEE
260 270 280 290 300
IIKTLALFRF ILPTVQIRLA GGRTIISDKG KKALESGVNG AISGDMLTTL
310
GIETSEDIKM IKNLGFEV
Length:318
Mass (Da):35,506
Last modified:September 11, 2007 - v1
Checksum:i04A5868F15F62E4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000726 Genomic DNA. Translation: ABS34058.1.
RefSeqiYP_001384513.1. NC_009697.1.

Genome annotation databases

EnsemblBacteriaiABS34058; ABS34058; CLB_2200.
GeneIDi5397839.
KEGGicba:CLB_2200.
PATRICi19358976. VBICloBot110701_2123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000726 Genomic DNA. Translation: ABS34058.1 .
RefSeqi YP_001384513.1. NC_009697.1.

3D structure databases

ProteinModelPortali A7FVS6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 441770.CLB_2200.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS34058 ; ABS34058 ; CLB_2200 .
GeneIDi 5397839.
KEGGi cba:CLB_2200.
PATRICi 19358976. VBICloBot110701_2123.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci CBOT441770:GH1E-2177-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. "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
    Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
    PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19397 / Type A.

Entry informationi

Entry nameiBIOB_CLOB1
AccessioniPrimary (citable) accession number: A7FVS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 11, 2007
Last modified: November 26, 2014
This is version 51 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