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B0SLQ3

- BIOB_LEPBP

UniProt

B0SLQ3 - BIOB_LEPBP

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Protein

Biotin synthase

Gene

bioB

Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
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 bindingi64 – 641Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi68 – 681Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi108 – 1081Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi140 – 1401Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi200 – 2001Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi269 – 2691Iron-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

BioCyciLBIF456481:GCM0-818-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:LEPBI_I0828
OrganismiLeptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Taxonomic identifieri456481 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000001847: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Biotin synthasePRO_0000381445Add
BLAST

Proteomic databases

PRIDEiB0SLQ3.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi456481.LEPBI_I0828.

Structurei

3D structure databases

ProteinModelPortaliB0SLQ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiTCENTLR.
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.

B0SLQ3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIAEVQEKTI SSSPSIISEE EALQILKGEV PLLPVVAKAS EERFRHFGNR
60 70 80 90 100
VRIHILDNIK NGYCPEDCGY CAQRKGGESG IQEYSLKSPE EIWEDAKKAK
110 120 130 140 150
ENGAYRFCMV TSGRGPTDKA VDKLAETISK INGELGMKVC LSAGILDGKK
160 170 180 190 200
AKTLKDAGLD RYNHNLNTSE SKYNEICSTH TFKDRLTTLE AAKEAEIGLC
210 220 230 240 250
SGIIVGMGEE LKDIVQVAFE LKRLGVISIP VNFFIPIKGH AIQKSTLTPE
260 270 280 290 300
FCVRVLSVFR LVNPDSEIRV GAGREGHLGF LQSMALYVAN SLFAEGYLNV
310 320 330 340 350
KGSEMEQTMN LIRDCNMVPE FTEGIPEGWE DYDSKFLYDE KNFPELYKHK

K
Length:351
Mass (Da):39,131
Last modified:April 8, 2008 - v1
Checksum:i04CFBD924BF2B1B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000786 Genomic DNA. Translation: ABZ96955.1.
RefSeqiYP_001838231.1. NC_010602.1.

Genome annotation databases

EnsemblBacteriaiABZ96955; ABZ96955; LEPBI_I0828.
GeneIDi6221101.
KEGGilbi:LEPBI_I0828.
PATRICi22348380. VBILepBif123590_0838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000786 Genomic DNA. Translation: ABZ96955.1 .
RefSeqi YP_001838231.1. NC_010602.1.

3D structure databases

ProteinModelPortali B0SLQ3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 456481.LEPBI_I0828.

Proteomic databases

PRIDEi B0SLQ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABZ96955 ; ABZ96955 ; LEPBI_I0828 .
GeneIDi 6221101.
KEGGi lbi:LEPBI_I0828.
PATRICi 22348380. VBILepBif123590_0838.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239958.
KOi K01012.
OMAi TCENTLR.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci LBIF456481:GCM0-818-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. "Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
    Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A.
    , Davies J.K., Medigue C., Adler B.
    PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Patoc 1 / ATCC 23582 / Paris.

Entry informationi

Entry nameiBIOB_LEPBP
AccessioniPrimary (citable) accession number: B0SLQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: November 26, 2014
This is version 48 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