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B9MJH4

- BIOB_ACIET

UniProt

B9MJH4 - BIOB_ACIET

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Protein

Biotin synthase

Gene

bioB

Organism
Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY))
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 bindingi78 – 781Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi82 – 821Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi85 – 851Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi122 – 1221Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi153 – 1531Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi213 – 2131Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi285 – 2851Iron-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

BioCyciAEBR535289:GHOO-1886-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:Dtpsy_1855
OrganismiAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY))
Taxonomic identifieri535289 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax
ProteomesiUP000000450: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Biotin synthasePRO_0000381354Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi535289.Dtpsy_1855.

Structurei

3D structure databases

ProteinModelPortaliB9MJH4.
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.

B9MJH4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSATTAPHT TQTLQFHPRV AESVATQRGE GWSIQAVQEL LDLPFMELLW
60 70 80 90 100
RAQATHRAHW PQGDIELATL LSVKTGGCPE NCGYCPQSAE FDTGVKAEKL
110 120 130 140 150
MSVQEVTQAA QAAKDAGATR FCMGAAWRAP KDRDIEKMSE LITAVKDLGL
160 170 180 190 200
QTCATLGMLQ SHQALALKDA GLDYYNHNLD TAPEYYSDVV STRQYQDRLD
210 220 230 240 250
TLRHVRDAGI NVCCGGIVGM GEAPVHRAGL IAQLANLNPY PESVPINSLV
260 270 280 290 300
RVAGTPLANS EPVDPLDFVR VIAVARITMP KARVRLSAGR QQLGDAVQAL
310 320 330 340 350
CFLAGANSIF YGDKLLVTSN PDVEADTQLL AKLGLKGTPN QTTTETACGA
Length:350
Mass (Da):37,658
Last modified:March 24, 2009 - v1
Checksum:i344F8A60A311D866
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001392 Genomic DNA. Translation: ACM33312.1.
RefSeqiYP_002553312.1. NC_011992.1.

Genome annotation databases

EnsemblBacteriaiACM33312; ACM33312; Dtpsy_1855.
GeneIDi7382216.
KEGGidia:Dtpsy_1855.
PATRICi21780821. VBIDiaSp55748_1897.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001392 Genomic DNA. Translation: ACM33312.1 .
RefSeqi YP_002553312.1. NC_011992.1.

3D structure databases

ProteinModelPortali B9MJH4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 535289.Dtpsy_1855.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM33312 ; ACM33312 ; Dtpsy_1855 .
GeneIDi 7382216.
KEGGi dia:Dtpsy_1855.
PATRICi 21780821. VBIDiaSp55748_1897.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci AEBR535289:GHOO-1886-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TPSY.

Entry informationi

Entry nameiBIOB_ACIET
AccessioniPrimary (citable) accession number: B9MJH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: November 26, 2014
This is version 42 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