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Protein

Biotin synthase

Gene

bioB

Organism
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
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 bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi76 – 761Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi113 – 1131Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi144 – 1441Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi204 – 2041Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi282 – 2821Iron-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

BioCyciNARO279238:GHBU-728-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:Saro_0719
OrganismiNovosphingobium aromaticivorans (strain DSM 12444 / F199)
Taxonomic identifieri279238 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium
ProteomesiUP000009134 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Biotin synthasePRO_0000381511Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi279238.Saro_0719.

Structurei

3D structure databases

ProteinModelPortaliQ2GAF7.
SMRiQ2GAF7. Positions 20-336.
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.

Q2GAF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQETALLERE SAGTGNAPVR TDWTREEIAA LFDLPFTELL FRAAEVHRAH
60 70 80 90 100
HRAGEVQLCT LLSIKTGGCP EDCGYCSQSV KADSGVEATK LMEVQKVLQS
110 120 130 140 150
AAQAKDNGSK RFCMGAAWRN PKDRDMPAII SMIKGVREMG METCMTLGML
160 170 180 190 200
TPSQAAQLAD AGLDYYNHNI DTSPERYEEV ITTRTFADRL QTLDNVRNAG
210 220 230 240 250
INVCSGGIVG MGETRADRVG FVHALATLEQ HPESVPVNAL VPIKGTVLGD
260 270 280 290 300
MLADTPLAKI DDIEFVRTVA VARITMPLSM VRLSAGRESM SEATQALCFM
310 320 330 340 350
AGANSIFTGD KLLTAANAGD DADAAMFKRL GLKPMEGEEP MRAMKSVGGC

SGGCAA
Length:356
Mass (Da):38,170
Last modified:March 21, 2006 - v1
Checksum:iA6C552ABAD311F9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD25166.1.
RefSeqiWP_011444380.1. NC_007794.1.
YP_496000.1. NC_007794.1.

Genome annotation databases

EnsemblBacteriaiABD25166; ABD25166; Saro_0719.
KEGGinar:Saro_0719.
PATRICi22784058. VBINovAro50627_0738.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD25166.1.
RefSeqiWP_011444380.1. NC_007794.1.
YP_496000.1. NC_007794.1.

3D structure databases

ProteinModelPortaliQ2GAF7.
SMRiQ2GAF7. Positions 20-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279238.Saro_0719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD25166; ABD25166; Saro_0719.
KEGGinar:Saro_0719.
PATRICi22784058. VBINovAro50627_0738.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciNARO279238:GHBU-728-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 12444 / F199.

Entry informationi

Entry nameiBIOB_NOVAD
AccessioniPrimary (citable) accession number: Q2GAF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 21, 2006
Last modified: April 1, 2015
This is version 67 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

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.