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Q1C947

- BIOB_YERPA

UniProt

Q1C947 - BIOB_YERPA

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Protein

Biotin synthase

Gene

bioB

Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
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

BioCyciYPES360102:GHZU-1097-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:YPA_1058
OrganismiYersinia pestis bv. Antiqua (strain Antiqua)
Taxonomic identifieri360102 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001971: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Biotin synthasePRO_0000381721Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi360102.YPA_1058.

Structurei

3D structure databases

ProteinModelPortaliQ1C947.
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.

Q1C947-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATYHHWTVG QALALFDKPL LELLFEAQQV HRQHFDPRQV QVSTLLSIKT
60 70 80 90 100
GACPEDCKYC PQSSRYKTGL ESERLMQVEQ VLESAKKAKA AGSTRFCMGA
110 120 130 140 150
AWKNPHERDM PYLAKMVEGV KALGMETCMT LGSLSKQQAH RLADAGLDYY
160 170 180 190 200
NHNLDTSPEF YGSIITTRSY QERLDTLNEV RDAGIKVCSG GIVGLGETVR
210 220 230 240 250
DRAGLLVQLA NLPKPPESVP INMLVKVKGT PLENNAEVDA FEFIRTIAVA
260 270 280 290 300
RIMMPSSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPDEDK
310 320 330 340
DLQLFRKLGL NPQQTATSHG DREQQQALTE QLLHGDTAQF YNAAV
Length:345
Mass (Da):38,378
Last modified:July 11, 2006 - v1
Checksum:i5E947F85B26780A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000308 Genomic DNA. Translation: ABG13025.1.
RefSeqiYP_650970.1. NC_008150.1.

Genome annotation databases

EnsemblBacteriaiABG13025; ABG13025; YPA_1058.
GeneIDi4119828.
KEGGiypa:YPA_1058.
PATRICi18581247. VBIYerPes1796_1448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000308 Genomic DNA. Translation: ABG13025.1 .
RefSeqi YP_650970.1. NC_008150.1.

3D structure databases

ProteinModelPortali Q1C947.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360102.YPA_1058.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG13025 ; ABG13025 ; YPA_1058 .
GeneIDi 4119828.
KEGGi ypa:YPA_1058.
PATRICi 18581247. VBIYerPes1796_1448.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci YPES360102:GHZU-1097-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 Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
    Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
    J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Antiqua.

Entry informationi

Entry nameiBIOB_YERPA
AccessioniPrimary (citable) accession number: Q1C947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 11, 2006
Last modified: November 26, 2014
This is version 64 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