Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Biotin synthase

Gene

bioB

Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Status
Reviewed-Annotation score: 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 + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.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 bindingi83 – 831Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi87 – 871Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi90 – 901Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi129 – 1291Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi160 – 1601Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi220 – 2201Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi296 – 2961Iron-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

BioCyciPARC259536:GI3A-1905-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:Psyc_1861
OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
Taxonomic identifieri259536 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000000546: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Biotin synthasePRO_0000381568Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi259536.Psyc_1861.

Structurei

3D structure databases

ProteinModelPortaliQ4FQJ9.
SMRiQ4FQJ9. Positions 36-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
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.

Q4FQJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALLNITEP NNNTNTKNDH FLASLTTDAT QSTASKYSRE QIAQLFDLPL
60 70 80 90 100
MDLLLQAQTI HRQNFTANEV QISTLLSIKT GNCPEDCGYC SQSGHHRDKT
110 120 130 140 150
ELVAEKRIEV SKVIAAAKRA KATGSSRFCM GAAWKHPSAK DMPYVVELVK
160 170 180 190 200
EVKALGLETC MTLGMLDTDQ AAQLANAGLD YYNHNLDTSR SYYEQVVSTR
210 220 230 240 250
SYDERLDTIA NVRNSGINVC SGNIVGMGES RDDRIDWVHE LLKMPKAPES
260 270 280 290 300
IPVNLLVPIQ GTPIGDKVLA EGQLSVLEWI RTIAVTRICC PSSYVRLSAG
310 320 330 340 350
RESLSDAEQA LAFMAGANSF FYGDKLLTTG NASQSGDDRL MRELGLTKQF
360 370
SAPRLPKQVP VLDAMSGHQS QVILASLS
Length:378
Mass (Da):41,377
Last modified:August 30, 2005 - v1
Checksum:i85114A8448C5911B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000082 Genomic DNA. Translation: AAZ19709.1.
RefSeqiYP_265143.1. NC_007204.1.

Genome annotation databases

EnsemblBacteriaiAAZ19709; AAZ19709; Psyc_1861.
GeneIDi3515830.
KEGGipar:Psyc_1861.
PATRICi23058591. VBIPsyArc98534_2201.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000082 Genomic DNA. Translation: AAZ19709.1.
RefSeqiYP_265143.1. NC_007204.1.

3D structure databases

ProteinModelPortaliQ4FQJ9.
SMRiQ4FQJ9. Positions 36-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi259536.Psyc_1861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ19709; AAZ19709; Psyc_1861.
GeneIDi3515830.
KEGGipar:Psyc_1861.
PATRICi23058591. VBIPsyArc98534_2201.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciPARC259536:GI3A-1905-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
    Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
    Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17307 / 273-4.

Entry informationi

Entry nameiBIOB_PSYA2
AccessioniPrimary (citable) accession number: Q4FQJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: August 30, 2005
Last modified: March 4, 2015
This is version 70 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.