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Protein

Biotin synthase

Gene

bioB

Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
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 bindingi56 – 561Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi60 – 601Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi63 – 631Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi100 – 1001Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi131 – 1311Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi191 – 1911Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi263 – 2631Iron-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

BioCyciPHAL326442:GJIU-1642-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:PSHAa1609
OrganismiPseudoalteromonas haloplanktis (strain TAC 125)
Taxonomic identifieri326442 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas
ProteomesiUP000006843 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Biotin synthasePRO_0000381558Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi326442.PSHAa1609.

Structurei

3D structure databases

ProteinModelPortaliQ3IGS6.
SMRiQ3IGS6. Positions 7-316.
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.

Q3IGS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELAPVRHNW THSEVKAIFE MPFNDLLFKA ASVHRANFNP NEVQISTLLS
60 70 80 90 100
IKTGACPEDC KYCPQSGHYR TDLERERLIE VEKVVEQARL AKQKGATRFC
110 120 130 140 150
MGAAWSDPKD RDMPYISQMV KEVKELGLET CMTLGMLNNE KAHELRNAGL
160 170 180 190 200
DYYNHNLDTS PEYYEQIIST RTFQDRLDTI GNVRDAGMKV CSGGIVGMGE
210 220 230 240 250
QAADRYGLLM QLANLDQQPE SVPINMLVKV KGTPLENVDD LDHFEFIRTI
260 270 280 290 300
ATARIMMPHS YVRLSAGRNA MNEQMQSMCF FAGANSIFYG DKLLTTENPD
310 320 330 340
ADADMALIKK LGMNPETRHD YSDEAVAASL SSQVADKATS KLFYEA
Length:346
Mass (Da):38,900
Last modified:November 8, 2005 - v1
Checksum:i1F1432B73015C7EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR954246 Genomic DNA. Translation: CAI86682.1.
RefSeqiWP_011328287.1. NC_007481.1.
YP_340125.1. NC_007481.1.

Genome annotation databases

EnsemblBacteriaiCAI86682; CAI86682; PSHAa1609.
GeneIDi3708753.
KEGGipha:PSHAa1609.
PATRICi32296783. VBIPseHal105694_1556.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR954246 Genomic DNA. Translation: CAI86682.1.
RefSeqiWP_011328287.1. NC_007481.1.
YP_340125.1. NC_007481.1.

3D structure databases

ProteinModelPortaliQ3IGS6.
SMRiQ3IGS6. Positions 7-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326442.PSHAa1609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI86682; CAI86682; PSHAa1609.
GeneIDi3708753.
KEGGipha:PSHAa1609.
PATRICi32296783. VBIPseHal105694_1556.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciPHAL326442:GJIU-1642-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TAC 125.

Entry informationi

Entry nameiBIOB_PSEHT
AccessioniPrimary (citable) accession number: Q3IGS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 8, 2005
Last modified: April 29, 2015
This is version 75 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.