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Protein

Biotin synthase

Gene

bioB

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi98 – 981Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi130 – 1301Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi190 – 1901Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi262 – 2621Iron-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

BioCyciSELO269084:GCDQ-1123-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:syc1098_d
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Biotin synthasePRO_0000381676Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi269084.syc1098_d.

Structurei

3D structure databases

ProteinModelPortaliQ5N332.
SMRiQ5N332. Positions 5-316.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
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.

Q5N332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAIRHDWTL EEIEDLLNTP LLELVHRAQT VHRDYQPANA IQLATLLSVK
60 70 80 90 100
TGGCSENCAY CPQSAHYNTE VDPQSTLPIE TVLEQAERAK AAGASRFCMG
110 120 130 140 150
WAWREIRDGA QFDAMLEMVQ GVRQLGLEAC VTAGMLSDRQ AERLAEAGLT
160 170 180 190 200
AYNHNLDTSP EFYGEIISTR TYADRLATLE RVRQAGISVC CGGIIGMGEG
210 220 230 240 250
QRDRAGLLQV LATLNPHPES VPINALVPVE GTPLGDRDRL DPLDLVRMCA
260 270 280 290 300
VARILMPKAR VRLSAGRTAL SREAQVLCFL AGANSIFYGD TLLTTANPVC
310 320
EADRQLLADI GAEALEVVTA
Length:320
Mass (Da):34,816
Last modified:February 1, 2005 - v1
Checksum:iC2D5AD8892F576C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD79288.1.
RefSeqiYP_171808.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD79288; BAD79288; syc1098_d.
KEGGisyc:syc1098_d.
PATRICi32488024. VBISynElo117686_1271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008231 Genomic DNA. Translation: BAD79288.1.
RefSeqiYP_171808.1. NC_006576.1.

3D structure databases

ProteinModelPortaliQ5N332.
SMRiQ5N332. Positions 5-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269084.syc1098_d.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD79288; BAD79288; syc1098_d.
KEGGisyc:syc1098_d.
PATRICi32488024. VBISynElo117686_1271.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciSELO269084:GCDQ-1123-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
    Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
    Photosyn. Res. 93:55-67(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.

Entry informationi

Entry nameiBIOB_SYNP6
AccessioniPrimary (citable) accession number: Q5N332
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 1, 2005
Last modified: April 1, 2015
This is version 72 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

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 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.