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B4RLI6

- BIOB_NEIG2

UniProt

B4RLI6 - BIOB_NEIG2

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Protein

Biotin synthase

Gene

bioB

Organism
Neisseria gonorrhoeae (strain NCCP11945)
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 bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi76 – 761Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi113 – 1131Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi144 – 1441Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi204 – 2041Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi276 – 2761Iron-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

BioCyciNGON521006:GJ73-1018-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:NGK_0996
OrganismiNeisseria gonorrhoeae (strain NCCP11945)
Taxonomic identifieri521006 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000002564: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Biotin synthasePRO_0000381494Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi521006.NGK_0996.

Structurei

3D structure databases

ProteinModelPortaliB4RLI6.
SMRiB4RLI6. Positions 23-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
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.

B4RLI6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVSPVALRR KTECKPHPTA RYWKKCDVEA LFGLPFLELV YQAAEVHRQN
60 70 80 90 100
FNPREIQLST LLSIKTGGCP EDCAYCPQSA HHNTNLGKEQ MMDVDEIVEK
110 120 130 140 150
AKIAKSRGAS RFCMGAAWRG PKPKDVETVS AIIKAVKGLG METCGTFGML
160 170 180 190 200
EEGMAEDLKE AGLDYYNHNL DTDPDRYNDI IHTRRHEDRM DTLGKVRNAG
210 220 230 240 250
LKVCCGGIVG MNETRAERAG LIASLANLDP QPESVPINRL VKVEGTPLAD
260 270 280 290 300
AEDLDWTEFV RTVSVARITM PQSYVRLSAG RSNMPEAMQA MCFMAGANSI
310 320 330 340 350
FYGDKLLTTG NPDEDGDRIL MEKLNLYPLQ FEPEGEVAEV EKASGIKADY
Length:350
Mass (Da):38,781
Last modified:July 28, 2009 - v2
Checksum:iCAD3FC7352529499
GO

Sequence cautioni

The sequence ACF29673.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001050 Genomic DNA. Translation: ACF29673.1. Different initiation.
RefSeqiYP_002001621.1. NC_011035.1.

Genome annotation databases

EnsemblBacteriaiACF29673; ACF29673; NGK_0996.
GeneIDi6448834.
KEGGingk:NGK_0996.
PATRICi20340432. VBINeiGon87511_1083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001050 Genomic DNA. Translation: ACF29673.1 . Different initiation.
RefSeqi YP_002001621.1. NC_011035.1.

3D structure databases

ProteinModelPortali B4RLI6.
SMRi B4RLI6. Positions 23-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 521006.NGK_0996.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF29673 ; ACF29673 ; NGK_0996 .
GeneIDi 6448834.
KEGGi ngk:NGK_0996.
PATRICi 20340432. VBINeiGon87511_1083.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci NGON521006:GJ73-1018-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. "Complete genome sequence of Neisseria gonorrhoeae NCCP11945."
    Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.
    J. Bacteriol. 190:6035-6036(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCCP11945.

Entry informationi

Entry nameiBIOB_NEIG2
AccessioniPrimary (citable) accession number: B4RLI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 28, 2009
Last modified: November 26, 2014
This is version 44 of the entry and version 2 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