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A7FKM9

- BIOB_YERP3

UniProt

A7FKM9 - BIOB_YERP3

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Protein

Biotin synthase

Gene

bioB

Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
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 bindingi53 – 531Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi57 – 571Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi60 – 601Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi97 – 971Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi128 – 1281Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi188 – 1881Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi260 – 2601Iron-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

BioCyciYPSE349747:GH71-2907-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:YpsIP31758_2844
OrganismiYersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Taxonomic identifieri349747 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000002412: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Biotin synthasePRO_0000381720Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi349747.YpsIP31758_2844.

Structurei

3D structure databases

ProteinModelPortaliA7FKM9.
SMRiA7FKM9. Positions 7-315.
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.

A7FKM9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATYHHWTVG QALALFDKPL LELLFEAQQV HRQHFDPRQV QVSTLLSIKT
60 70 80 90 100
GACPEDCKYC PQSSRYKTGL ESERLMQVEQ VLESAKKAKA AGSTRFCMGA
110 120 130 140 150
AWKNPHERDM PYLVKMVEGV KALGMETCMT LGSLSKQQAH RLADAGLDYY
160 170 180 190 200
NHNLDTSPEF YGSIITTRSY QERLDTLNEV RDAGIKVCSG GIVGLGETVR
210 220 230 240 250
DRAGLLVQLA NLPKPPESVP INMLVKVKGT PLENNAEVDA FEFIRTIAVA
260 270 280 290 300
RIMMPSSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPDEDN
310 320 330 340
DLQLFRKLGL NPQQTATSHG DREQQQALTE QLLHGDTAQF YNAAV
Length:345
Mass (Da):38,392
Last modified:September 11, 2007 - v1
Checksum:i9972DAE5716FA434
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000720 Genomic DNA. Translation: ABS47575.1.
RefSeqiYP_001401807.1. NC_009708.1.

Genome annotation databases

EnsemblBacteriaiABS47575; ABS47575; YpsIP31758_2844.
GeneIDi5387493.
KEGGiypi:YpsIP31758_2844.
PATRICi18634731. VBIYerPse15693_3299.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000720 Genomic DNA. Translation: ABS47575.1 .
RefSeqi YP_001401807.1. NC_009708.1.

3D structure databases

ProteinModelPortali A7FKM9.
SMRi A7FKM9. Positions 7-315.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349747.YpsIP31758_2844.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS47575 ; ABS47575 ; YpsIP31758_2844 .
GeneIDi 5387493.
KEGGi ypi:YpsIP31758_2844.
PATRICi 18634731. VBIYerPse15693_3299.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci YPSE349747:GH71-2907-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 complete genome sequence of Yersinia pseudotuberculosis IP31758, the causative agent of Far East scarlet-like fever."
    Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., Fayolle C., Lindler L.E., Carniel E., Ravel J.
    PLoS Genet. 3:1508-1523(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IP 31758.

Entry informationi

Entry nameiBIOB_YERP3
AccessioniPrimary (citable) accession number: A7FKM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 11, 2007
Last modified: November 26, 2014
This is version 53 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