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Q5LN74

- BIOB_RUEPO

UniProt

Q5LN74 - BIOB_RUEPO

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Protein

Biotin synthase

Gene

bioB

Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
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 bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi59 – 591Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi100 – 1001Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi132 – 1321Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi192 – 1921Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi264 – 2641Iron-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:SPO3338
OrganismiRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Taxonomic identifieri246200 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
ProteomesiUP000001023: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Biotin synthasePRO_0000381637Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi246200.SPO3338.

Structurei

3D structure databases

ProteinModelPortaliQ5LN74.
SMRiQ5LN74. Positions 6-313.
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.

Q5LN74-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEAIRSDWS VDEVEALLRL PLLDLVGRAN GVHRAHHAPD DIQKASLLSI
60 70 80 90 100
KTGGCPEDCA YCPQSAHHRE VELTREKLMN PDHVVSLARR AQRAGAERFC
110 120 130 140 150
MGAAWRQVRD GAEFDNVLAM VRGVRALGME ACVTLGMLRP HQAQRLAEAG
160 170 180 190 200
LTAYNHNLDT SPEFYGQIIG TRTYQDRLDT LAYCRDAGIE LCCGGIIGMG
210 220 230 240 250
ESLRDRAAML QVLANFAPHP ESVPINALIP IEGTPLAHRE RVGIFDLVRM
260 270 280 290 300
VATARIIMPL TRVRLSAGRS DFSAAEQALC FLAGANSVFY GDVLLTAPNA
310
GTGADAELFA ALGALETA
Length:318
Mass (Da):34,397
Last modified:February 1, 2005 - v1
Checksum:iA46B7BDC2ED068ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000031 Genomic DNA. Translation: AAV96565.1.
RefSeqiYP_168534.1. NC_003911.12.

Genome annotation databases

EnsemblBacteriaiAAV96565; AAV96565; SPO3338.
GeneIDi3195697.
KEGGisil:SPO3338.
PATRICi23380127. VBIRuePom114501_3400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000031 Genomic DNA. Translation: AAV96565.1 .
RefSeqi YP_168534.1. NC_003911.12.

3D structure databases

ProteinModelPortali Q5LN74.
SMRi Q5LN74. Positions 6-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246200.SPO3338.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV96565 ; AAV96565 ; SPO3338 .
GeneIDi 3195697.
KEGGi sil:SPO3338.
PATRICi 23380127. VBIRuePom114501_3400.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239957.
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: ATCC 700808 / DSM 15171 / DSS-3.

Entry informationi

Entry nameiBIOB_RUEPO
AccessioniPrimary (citable) accession number: Q5LN74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 1, 2005
Last modified: November 26, 2014
This is version 69 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