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A0KB05

- BIOB_BURCH

UniProt

A0KB05 - BIOB_BURCH

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Protein

Biotin synthase

Gene

bioB

Organism
Burkholderia cenocepacia (strain HI2424)
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 bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi114 – 1141Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi145 – 1451Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi205 – 2051Iron-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

BioCyciBCEN331272:GHR7-3005-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:Bcen2424_2934
OrganismiBurkholderia cenocepacia (strain HI2424)
Taxonomic identifieri331272 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000000776: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Biotin synthasePRO_0000381261Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi331272.Bcen2424_2934.

Structurei

3D structure databases

ProteinModelPortaliA0KB05.
SMRiA0KB05. Positions 23-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
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.

A0KB05-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTQAQTAAVQ PAAIPVAAPA SQRWRVADVV ALFELPFNDL MFRAQQVHRE
60 70 80 90 100
HFDANAVQLS TLLSIKTGGC EEDCGYCSQS SHHDTGLKAE KLMDVDTVLD
110 120 130 140 150
AARAAKANGA SRFCMGAAWR NPKERHMPAL TEMVRGVKEL GLETCMTLGM
160 170 180 190 200
LEDEQAQQLA DAGLDYYNHN LDTSPEFYGQ VISTRTYQDR LDTLDRVRDA
210 220 230 240 250
GINVCCGGII GMGESRRERA GLISQLANLN PYPESVPINN LVAIEGTPLE
260 270 280 290 300
GTAPLDPFEF VRTIAVARIT MPKAVVRLSA GREQLDDAMQ AMCFLAGANS
310 320 330
MFYGDQLLTT SNPQTQRDRA LFERLGIRAS QADALSDNA
Length:339
Mass (Da):37,014
Last modified:December 12, 2006 - v1
Checksum:i1CB08D807073166F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000458 Genomic DNA. Translation: ABK09682.1.
RefSeqiYP_836575.1. NC_008542.1.

Genome annotation databases

EnsemblBacteriaiABK09682; ABK09682; Bcen2424_2934.
GeneIDi4448466.
KEGGibch:Bcen2424_2934.
PATRICi19063349. VBIBurCen15205_3009.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000458 Genomic DNA. Translation: ABK09682.1 .
RefSeqi YP_836575.1. NC_008542.1.

3D structure databases

ProteinModelPortali A0KB05.
SMRi A0KB05. Positions 23-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331272.Bcen2424_2934.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK09682 ; ABK09682 ; Bcen2424_2934 .
GeneIDi 4448466.
KEGGi bch:Bcen2424_2934.
PATRICi 19063349. VBIBurCen15205_3009.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239957.
KOi K01012.
OMAi DETQALC.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci BCEN331272:GHR7-3005-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. "Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.
    , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HI2424.

Entry informationi

Entry nameiBIOB_BURCH
AccessioniPrimary (citable) accession number: A0KB05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 12, 2006
Last modified: November 26, 2014
This is version 54 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