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A9HRF2

- BIOB_GLUDA

UniProt

A9HRF2 - BIOB_GLUDA

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Protein

Biotin synthase

Gene

bioB

Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
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 bindingi51 – 511Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi96 – 961Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi127 – 1271Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi187 – 1871Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi259 – 2591Iron-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

BioCyciGDIA272568:GJPS-3000-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:GDI2953, Gdia_3396
OrganismiGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Taxonomic identifieri272568 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter
ProteomesiUP000000736: Chromosome, UP000001176: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Biotin synthasePRO_0000381409Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272568.GDI_2953.

Structurei

3D structure databases

ProteinModelPortaliA9HRF2.
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.

A9HRF2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRTDWTRDEI AALIALPFPE LMFRAQSVHR ARFDPTEIQI STLLSIKTGG
60 70 80 90 100
CPEDCAYCPQ SAKHEDGGVK ASRLMAVEAV LKEARAARDA GAARFCMGAA
110 120 130 140 150
WRSPKDHDLE TVCAMVEGVK SLGMETCVTL GMLDDRQAHR LREAGLDYYN
160 170 180 190 200
HNLDTSPEHY GSIISTRTYQ ERLDTLAHVR DAGINVCCGG IVGMGENDDD
210 220 230 240 250
RAGLIASLAS LPRHPESVPI NLLVRVAGTP LAGADPVDPI DFVRIIAAAR
260 270 280 290 300
IAMPASRVRL AAGREDMTDE AQTLCFLAGA NSIFYGEKLL TTPNPEASRD
310
ARLLARLGMH TSLAQA
Length:316
Mass (Da):34,213
Last modified:September 1, 2009 - v2
Checksum:i56B554525102199E
GO

Sequence cautioni

The sequence ACI53122.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAP56896.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM889285 Genomic DNA. Translation: CAP56896.1. Different initiation.
CP001189 Genomic DNA. Translation: ACI53122.1. Different initiation.
RefSeqiYP_001603186.1. NC_010125.1.
YP_002277737.1. NC_011365.1.

Genome annotation databases

EnsemblBacteriaiACI53122; ACI53122; Gdia_3396.
CAP56896; CAP56896; GDI2953.
GeneIDi5791775.
6976842.
KEGGigdi:GDI_2953.
gdj:Gdia_3396.
PATRICi22055230. VBIGluDia203729_3377.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM889285 Genomic DNA. Translation: CAP56896.1 . Different initiation.
CP001189 Genomic DNA. Translation: ACI53122.1 . Different initiation.
RefSeqi YP_001603186.1. NC_010125.1.
YP_002277737.1. NC_011365.1.

3D structure databases

ProteinModelPortali A9HRF2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272568.GDI_2953.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACI53122 ; ACI53122 ; Gdia_3396 .
CAP56896 ; CAP56896 ; GDI2953 .
GeneIDi 5791775.
6976842.
KEGGi gdi:GDI_2953.
gdj:Gdia_3396.
PATRICi 22055230. VBIGluDia203729_3377.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci GDIA272568:GJPS-3000-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 the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5."
    Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A., Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.
    , Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O., Baldani J.I., Ferreira P.C.
    BMC Genomics 10:450-450(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49037 / DSM 5601 / PAl5.
  2. "Two genome sequences of the same bacterial strain, Gluconacetobacter diazotrophicus PAl 5, suggest a new standard in genome sequence submission."
    Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.
    Stand. Genomic Sci. 2:309-317(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49037 / DSM 5601 / PAl5.

Entry informationi

Entry nameiBIOB_GLUDA
AccessioniPrimary (citable) accession number: A9HRF2
Secondary accession number(s): B5ZM22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: November 26, 2014
This is version 48 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, 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