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P0A507

- BIOB_MYCBO

UniProt

P0A507 - BIOB_MYCBO

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Protein

Biotin synthase

Gene

bioB

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
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 bindingi85 – 851Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi89 – 891Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi92 – 921Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi128 – 1281Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi161 – 1611Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi220 – 2201Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi290 – 2901Iron-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:Mb1615
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001419: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Biotin synthasePRO_0000185558Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi233413.Mb1615.

Structurei

3D structure databases

ProteinModelPortaliP0A507.
SMRiP0A507. Positions 45-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiETHHNID.
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.

P0A507-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTQAATRPTN DAGQDGGNNS DILVVARQQV LQRGEGLNQD QVLAVLQLPD
60 70 80 90 100
DRLEELLALA HEVRMRWCGP EVEVEGIISL KTGGCPEDCH FCSQSGLFAS
110 120 130 140 150
PVRSAWLDIP SLVEAAKQTA KSGATEFCIV AAVRGPDERL MAQVAAGIEA
160 170 180 190 200
IRNEVEINIA CSLGMLTAEQ VDQLAARGVH RYNHNLETAR SFFANVVTTH
210 220 230 240 250
TWEERWQTLS MVRDAGMEVC CGGILGMGET LQQRAEFAAE LAELGPDEVP
260 270 280 290 300
LNFLNPRPGT PFADLEVMPV GDALKAVAAF RLALPRTMLR FAGGREITLG
310 320 330 340
DLGAKRGILG GINAVIVGNY LTTLGRPAEA DLELLDELQM PLKALNASL
Length:349
Mass (Da):37,550
Last modified:March 15, 2005 - v1
Checksum:iF3B0A5821B3F14A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041819 Genomic DNA. Translation: AAB96962.1.
BX248333 Genomic DNA. Translation: CDO42864.1.
RefSeqiNP_855268.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCAD96283; CAD96283; Mb1615.
GeneIDi1092504.
KEGGimbo:Mb1615.
PATRICi18005233. VBIMycBov88188_1764.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041819 Genomic DNA. Translation: AAB96962.1 .
BX248333 Genomic DNA. Translation: CDO42864.1 .
RefSeqi NP_855268.1. NC_002945.3.

3D structure databases

ProteinModelPortali P0A507.
SMRi P0A507. Positions 45-340.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 233413.Mb1615.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD96283 ; CAD96283 ; Mb1615 .
GeneIDi 1092504.
KEGGi mbo:Mb1615.
PATRICi 18005233. VBIMycBov88188_1764.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239958.
KOi K01012.
OMAi ETHHNID.
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

« Hide 'large scale' publications
  1. "Cloning, sequencing, and identification of Mycobacterium bovis BCG biotin biosynthetic genes by complementing two Mycobacterium smegmatis biotin mutants."
    Yu S., Jacobs W.R. Jr.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BCG / Pasteur.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-935 / AF2122/97.

Entry informationi

Entry nameiBIOB_MYCBO
AccessioniPrimary (citable) accession number: P0A507
Secondary accession number(s): O06601, X2BIA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 26, 2014
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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3