Skip Header

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

Q8DL38

- BIOB_THEEB

UniProt

Q8DL38 - BIOB_THEEB

(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
Thermosynechococcus elongatus (strain BP-1)
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 bindingi94 – 941Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi98 – 981Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi101 – 1011Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi138 – 1381Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi170 – 1701Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi230 – 2301Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi300 – 3001Iron-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

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:tll0661
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Biotin synthasePRO_0000381683Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi197221.tll0661.

Structurei

3D structure databases

ProteinModelPortaliQ8DL38.
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.

Q8DL38-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNSISASAIV LWKNTPLPFV VKSYPMSTLT TDWQHLANLA LADECLSRDQ
60 70 80 90 100
ARAVLQAPDT ELLNQLAAAY RVRYHYWGNR VRLHYLLNAQ SGLCPEDCHY
110 120 130 140 150
CSQSKISTAE IEKYPLLSQE KILAAADRAA HLKAGTFCMV ISGRSPSEKV
160 170 180 190 200
FEQVLAAIRA VKERYPLKIC ACLGLLTPEQ TARLAAAGVD RVNHNLNTSE
210 220 230 240 250
NFYSEICTTH TFRDRDQTLA NIQAAGITTC SGGILGMGES DDDVIDLALF
260 270 280 290 300
LRQRQVTSVP VNFLIPIPGT PLGEQHTLNP RHCLRILVLF RFLLPRQEIR
310 320 330 340 350
IAGGREVHLR SLQPLGLYAA NSMFIGDYLT TPGQAPHQDW QMIADAGFVL
360
EDPEGRAIAP
Length:360
Mass (Da):39,878
Last modified:March 1, 2003 - v1
Checksum:iAA370F3D3E6694B1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC08212.1.
RefSeqiNP_681450.1. NC_004113.1.
WP_011056508.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08212; BAC08212; BAC08212.
GeneIDi1012044.
KEGGitel:tll0661.
PATRICi23926598. VBITheElo119873_0700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000039 Genomic DNA. Translation: BAC08212.1 .
RefSeqi NP_681450.1. NC_004113.1.
WP_011056508.1. NC_004113.1.

3D structure databases

ProteinModelPortali Q8DL38.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 197221.tll0661.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC08212 ; BAC08212 ; BAC08212 .
GeneIDi 1012044.
KEGGi tel:tll0661.
PATRICi 23926598. VBITheElo119873_0700.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiBIOB_THEEB
AccessioniPrimary (citable) accession number: Q8DL38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2003
Last modified: October 1, 2014
This is version 79 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, Reference proteome

Documents

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

External Data

Dasty 3