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A9NCS0

- BIOB_COXBR

UniProt

A9NCS0 - BIOB_COXBR

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Protein

Biotin synthase

Gene

bioB

Organism
Coxiella burnetii (strain RSA 331 / Henzerling II)
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 bindingi52 – 521Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi56 – 561Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi59 – 591Iron-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

BioCyciCBUR360115:GI0X-940-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:COXBURSA331_A0933
OrganismiCoxiella burnetii (strain RSA 331 / Henzerling II)
Taxonomic identifieri360115 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000008557: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Biotin synthasePRO_0000381334Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi360115.COXBURSA331_A0933.

Structurei

3D structure databases

ProteinModelPortaliA9NCS0.
SMRiA9NCS0. Positions 4-310.
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.

A9NCS0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKGRNWNQAS VAKLFELPFF ELLYKAYETH RSHFDVRDME LCTLSSIKTG
60 70 80 90 100
TCPEDCAYCP QSGHYKTDVE REKLINLEAV LEQAKVAKEN GARRFCMGAA
110 120 130 140 150
WRSPPKRELP KVLEMIKSVK ALGLETCVTL GMLDQEQALQ LKEAGLDFYN
160 170 180 190 200
HNLDTSPEFY KKIITTRTYQ DRMETLKNVR NAGINVCCGG ILGMGESRAD
210 220 230 240 250
RIQLLLELYQ LPEPPTSIPI NQLIPIKGTP LENTKAIDPF EFIKTIAITR
260 270 280 290 300
LLFPTSVIRL SAGREAMSDE LQAWCFMAGA NSIFYGDKLL TAKNPGQNRD
310 320
VNLLKKLGLK VPVLTEEYAC Y
Length:321
Mass (Da):36,252
Last modified:February 5, 2008 - v1
Checksum:iFDC79146CEC713D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000890 Genomic DNA. Translation: ABX77241.1.
RefSeqiYP_001596710.1. NC_010117.1.

Genome annotation databases

EnsemblBacteriaiABX77241; ABX77241; COXBURSA331_A0933.
GeneIDi5792907.
KEGGicbs:COXBURSA331_A0933.
PATRICi17926121. VBICoxBur33747_0939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000890 Genomic DNA. Translation: ABX77241.1 .
RefSeqi YP_001596710.1. NC_010117.1.

3D structure databases

ProteinModelPortali A9NCS0.
SMRi A9NCS0. Positions 4-310.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360115.COXBURSA331_A0933.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX77241 ; ABX77241 ; COXBURSA331_A0933 .
GeneIDi 5792907.
KEGGi cbs:COXBURSA331_A0933.
PATRICi 17926121. VBICoxBur33747_0939.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci CBUR360115:GI0X-940-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. "Genome sequencing of phylogenetically and phenotypically diverse Coxiella burnetii isolates."
    Seshadri R., Samuel J.E.
    Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RSA 331 / Henzerling II.

Entry informationi

Entry nameiBIOB_COXBR
AccessioniPrimary (citable) accession number: A9NCS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 49 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