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Q3YRG6

- BIOB_EHRCJ

UniProt

Q3YRG6 - BIOB_EHRCJ

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Protein

Biotin synthase

Gene

bioB

Organism
Ehrlichia canis (strain Jake)
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 bindingi57 – 571Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi64 – 641Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi101 – 1011Iron-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

BioCyciECAN269484:GI02-690-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:Ecaj_0657
OrganismiEhrlichia canis (strain Jake)
Taxonomic identifieri269484 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia
ProteomesiUP000000435: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Biotin synthasePRO_0000381374Add
BLAST

Proteomic databases

PRIDEiQ3YRG6.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi269484.Ecaj_0657.

Structurei

3D structure databases

ProteinModelPortaliQ3YRG6.
SMRiQ3YRG6. Positions 8-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiRIMMPAS.
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.

Q3YRG6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTFTPTRND WQLDEILELF HTAFNDLILQ SHLLHRQFFS NNEVQISSLL
60 70 80 90 100
NIKTGGCPEN CKYCSQSAHY KTDLKKESLL DIESIKKAIQ TAKKNGADRF
110 120 130 140 150
CFAAAWRQVR DRDLEYICDI IDLIKSENLE SCASLGMVTL EQAKKLKNAG
160 170 180 190 200
LDFYNHNIDT SRDFYPNVTT TRSYDDRLTS LNNIHEAGIN ICSGGILGLG
210 220 230 240 250
ESVEDRAKML LTLANLKEHP LSVPINRLVP IKGTPFENNA KIDNIDFIKT
260 270 280 290 300
IAVARILMPK SYIRLAAGRM SMSEEMQALC LFAGANSIFY GEKLLTTPNA
310 320
DCNDDRNLLS KLGAKTKEPV FFNS
Length:324
Mass (Da):36,442
Last modified:September 27, 2005 - v1
Checksum:i7824C0FF36C2614B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000107 Genomic DNA. Translation: AAZ68689.1.
RefSeqiYP_303287.1. NC_007354.1.

Genome annotation databases

EnsemblBacteriaiAAZ68689; AAZ68689; Ecaj_0657.
GeneIDi3618143.
KEGGiecn:Ecaj_0657.
PATRICi20574918. VBIEhrCan118076_0707.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000107 Genomic DNA. Translation: AAZ68689.1 .
RefSeqi YP_303287.1. NC_007354.1.

3D structure databases

ProteinModelPortali Q3YRG6.
SMRi Q3YRG6. Positions 8-318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269484.Ecaj_0657.

Proteomic databases

PRIDEi Q3YRG6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ68689 ; AAZ68689 ; Ecaj_0657 .
GeneIDi 3618143.
KEGGi ecn:Ecaj_0657.
PATRICi 20574918. VBIEhrCan118076_0707.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239957.
KOi K01012.
OMAi RIMMPAS.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci ECAN269484:GI02-690-MONOMER.

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. "The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies."
    Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.
    J. Bacteriol. 188:4015-4023(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Jake.

Entry informationi

Entry nameiBIOB_EHRCJ
AccessioniPrimary (citable) accession number: Q3YRG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 27, 2005
Last modified: November 26, 2014
This is version 71 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