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Q1LTL8

- BIOB_BAUCH

UniProt

Q1LTL8 - BIOB_BAUCH

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Protein

Biotin synthase

Gene

bioB

Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
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

BioCyciBCIC374463:GI6Q-246-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:BCI_0246
OrganismiBaumannia cicadellinicola subsp. Homalodisca coagulata
Taxonomic identifieri374463 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia
ProteomesiUP000002427: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Biotin synthasePRO_0000381236Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi374463.BCI_0246.

Structurei

3D structure databases

ProteinModelPortaliQ1LTL8.
SMRiQ1LTL8. Positions 6-314.
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.

Q1LTL8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQVTQRWNRE QAISLFNKPF FDLLFQAQQV HRKYFRLGQV QISTLLSIKT
60 70 80 90 100
GNCAEDCKYC PQSSHYETKL DNEPLVQLPQ VLAAAKKASD AGSTRFCIGA
110 120 130 140 150
AWKKIHDRDM PLLEQIVTGV KAIGLETCMT LGILKPQQAQ RLAKAGLDFY
160 170 180 190 200
NHNLDTSPEF YHSIVTTRSY QDRLNTIENV RKAGIKICSG GIIGLGETIS
210 220 230 240 250
DRAGLLVELA NLPEPPSSVP INMLVKVRGT PMFDNKDVDP FDLIRMIAVT
260 270 280 290 300
RIMMPTSYVR LSAGREQMNE QTQAICFMAG ANSIFYGRKL LTSSNPTEDS
310 320 330 340
DKRLFRKLGM QIEKHTTIKN SNWKKKKLLL HDNQQHDNTI SS
Length:342
Mass (Da):38,592
Last modified:May 30, 2006 - v1
Checksum:i2D7DB29C8EB19CE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000238 Genomic DNA. Translation: ABF14204.1.
RefSeqiYP_588696.1. NC_007984.1.

Genome annotation databases

EnsemblBacteriaiABF14204; ABF14204; BCI_0246.
GeneIDi4056501.
KEGGibci:BCI_0246.
PATRICi21073993. VBIBauCic75062_0232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000238 Genomic DNA. Translation: ABF14204.1 .
RefSeqi YP_588696.1. NC_007984.1.

3D structure databases

ProteinModelPortali Q1LTL8.
SMRi Q1LTL8. Positions 6-314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 374463.BCI_0246.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF14204 ; ABF14204 ; BCI_0246 .
GeneIDi 4056501.
KEGGi bci:BCI_0246.
PATRICi 21073993. VBIBauCic75062_0232.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci BCIC374463:GI6Q-246-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. "Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
    Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
    PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiBIOB_BAUCH
AccessioniPrimary (citable) accession number: Q1LTL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 30, 2006
Last modified: November 26, 2014
This is version 61 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