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
Acinetobacter calcoaceticus
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 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

UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
OrganismiAcinetobacter calcoaceticus
Taxonomic identifieri471 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Biotin synthasePRO_0000381175Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ93GG2.
SMRiQ93GG2. Positions 4-314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

Q93GG2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLRNDWTRD EIQALYDQPF LDLVFEAQSV HRQHFQANTI QVSTLLSIKT
60 70 80 90 100
GKCPEDCKYC SQSAHYDSKL EAEKRIAVDK VISEAQAAKE SGSSRFCMGA
110 120 130 140 150
AWRNPHERDM PYVLEMVREV KALGLETCMT LGMLNQSQAE RLKDAGLDYY
160 170 180 190 200
NHNLDTSREY YSHIISTRTF DDRLNTLDHV RHAGMKVCSG GIVGLGESRN
210 220 230 240 250
DRIGLLQELA TMPVHPESVP INMLVPIEGT PLAEVEKLDV TEWIRTIAVA
260 270 280 290 300
RIIMPHSYIR LSAGRESLSD SDQALAFMAG ANSLFSGEKL LTTPNAGEGK
310 320
DQILFAKLGL TAEKAKPTVA ELSVDAMSA
Length:329
Mass (Da):36,549
Last modified:December 1, 2001 - v1
Checksum:i448D5EA79B0A79E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239257 Genomic DNA. Translation: AAK96892.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239257 Genomic DNA. Translation: AAK96892.1.

3D structure databases

ProteinModelPortaliQ93GG2.
SMRiQ93GG2. Positions 4-314.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

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. "Genetic characterization of Acinetobacter calcoaceticus RAG-1 transposon mutants."
    Blank W.A., Kaplan D.L.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 31012 / RAG-1.

Entry informationi

Entry nameiBIOB_ACICA
AccessioniPrimary (citable) accession number: Q93GG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 1, 2001
Last modified: March 4, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.