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Protein

Biotin synthase

Gene

bioB

Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi)
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 bindingi50 – 501Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi54 – 541Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi57 – 571Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi94 – 941Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi125 – 1251Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi185 – 1851Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi257 – 2571Iron-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

BioCyciRFEL315456:GKEK-541-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:RF_0527
OrganismiRickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi)
Taxonomic identifieri315456 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
ProteomesiUP000008548 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Biotin synthasePRO_0000381590Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi315456.RF_0527.

Structurei

3D structure databases

ProteinModelPortaliQ4UM45.
SMRiQ4UM45. Positions 2-308.
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.

Q4UM45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKWTFDEAK EIFSFSFMEL VYQAQTIHRA NFDPNKIQIS SLLSIKTGSC
60 70 80 90 100
PENCKFCPQS SHYKTYVKKE PLMQIEDVIT AAKRAKAAGS TRFCMGAAWR
110 120 130 140 150
GPRDEDLKLV CEMIKEVKKL GLETCVTLGL LKEHQAVTLK EAGLDFYNHN
160 170 180 190 200
IDTSEEFYNK IITTRTFQDR LDTLRYVRAS GMKVCCGGIL GMGETNDDRI
210 220 230 240 250
NMILTLANLE EPAESVTINK LIKIPGTPLE NVQDIDPFDF VRVIALARIM
260 270 280 290 300
IPKSYIRLSA GREQMSDELQ ALCIMAGVYS IFYGEKILTS ANPMPERDND

LFQKLGIIH
Length:309
Mass (Da):34,987
Last modified:July 5, 2005 - v1
Checksum:i5E7BCC700C4B475B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000053 Genomic DNA. Translation: AAY61378.1.
RefSeqiWP_011270859.1. NC_007109.1.
YP_246543.1. NC_007109.1.

Genome annotation databases

EnsemblBacteriaiAAY61378; AAY61378; RF_0527.
KEGGirfe:RF_0527.
PATRICi17891578. VBIRicFel64634_0622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000053 Genomic DNA. Translation: AAY61378.1.
RefSeqiWP_011270859.1. NC_007109.1.
YP_246543.1. NC_007109.1.

3D structure databases

ProteinModelPortaliQ4UM45.
SMRiQ4UM45. Positions 2-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi315456.RF_0527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAY61378; AAY61378; RF_0527.
KEGGirfe:RF_0527.
PATRICi17891578. VBIRicFel64634_0622.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciRFEL315456:GKEK-541-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. "The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite."
    Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D.
    PLoS Biol. 3:1-12(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-1525 / URRWXCal2.

Entry informationi

Entry nameiBIOB_RICFE
AccessioniPrimary (citable) accession number: Q4UM45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 5, 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. Rickettsia felis (Rickettsia azadi)
    Rickettsia felis (strain URRWXCal2): entries and gene names
  3. 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.