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Q2NB65

- BIOB_ERYLH

UniProt

Q2NB65 - BIOB_ERYLH

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Protein

Biotin synthase

Gene

bioB

Organism
Erythrobacter litoralis (strain HTCC2594)
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 bindingi54 – 541Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi98 – 981Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi129 – 1291Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi189 – 1891Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi267 – 2671Iron-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

BioCyciELIT314225:GHLE-1005-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:ELI_04920
OrganismiErythrobacter litoralis (strain HTCC2594)
Taxonomic identifieri314225 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter
ProteomesiUP000008808: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Biotin synthasePRO_0000381382Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi314225.ELI_04920.

Structurei

3D structure databases

ProteinModelPortaliQ2NB65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiDETQALC.
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.

Q2NB65-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTPIRTNWSR DEIAALFEQP FTELLFQAAT VHRAYHPPEQ VQLCTLLSIK
60 70 80 90 100
TGGCPEDCGY CSQSVKADSG VEATKLMDVQ RVLQSAAQAK DAGSQRFCMG
110 120 130 140 150
AAWRNPKDRD MPAIVEIVKG VRDMGLETCM TLGMLTPKQA DMLKDAGLDY
160 170 180 190 200
YNHNVDTGPE YYERVISTRN YQDRLDTLQN VRDAGINVCS GGIVGMGETR
210 220 230 240 250
EDRVGFVHTL ATLERHPESV PVNALVPVKG TVLGDMLADT PLAKIDDIEF
260 270 280 290 300
VRTVAVARIT MPLSMVRLSA GRESMSEATQ ALCFMAGANS IFTGDKLLTA
310 320 330 340
ANAGDDKDAA LFDKLGLTAL QGEEPLRRAK DEAGKAAIPA E
Length:341
Mass (Da):37,045
Last modified:February 7, 2006 - v1
Checksum:iF81B8CC13D4B7AF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000157 Genomic DNA. Translation: ABC63076.1.
RefSeqiWP_011413912.1. NC_007722.1.
YP_457873.1. NC_007722.1.

Genome annotation databases

EnsemblBacteriaiABC63076; ABC63076; ELI_04920.
GeneIDi3870147.
KEGGieli:ELI_04920.
PATRICi21859078. VBIEryLit102657_0974.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000157 Genomic DNA. Translation: ABC63076.1 .
RefSeqi WP_011413912.1. NC_007722.1.
YP_457873.1. NC_007722.1.

3D structure databases

ProteinModelPortali Q2NB65.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 314225.ELI_04920.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC63076 ; ABC63076 ; ELI_04920 .
GeneIDi 3870147.
KEGGi eli:ELI_04920.
PATRICi 21859078. VBIEryLit102657_0974.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci ELIT314225:GHLE-1005-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 Erythrobacter litoralis HTCC2594."
    Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
    J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HTCC2594.

Entry informationi

Entry nameiBIOB_ERYLH
AccessioniPrimary (citable) accession number: Q2NB65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 7, 2006
Last modified: November 26, 2014
This is version 69 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