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Q6FAP9

- BIOB_ACIAD

UniProt

Q6FAP9 - BIOB_ACIAD

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Protein

Biotin synthase

Gene

bioB

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
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 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

BioCyciASP62977:GJVV-1935-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:ACIAD2045
OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Taxonomic identifieri62977 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
ProteomesiUP000000430: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Biotin synthasePRO_0000381167Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi62977.ACIAD2045.

Structurei

3D structure databases

ProteinModelPortaliQ6FAP9.
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.

Q6FAP9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLRNDWTRD EIQALYDQPF LDLVFQAQQV HREHFSANTI QVSTLLSIKT
60 70 80 90 100
GKCPEDCKYC SQSAHYDSKL EAEKRIAVDK VISEAKAAKD SGSSRFCMGA
110 120 130 140 150
AWRNPHERDM PYVLEMVREV KALGLETCMT LGMLNQSQAE RLSDAGLDYY
160 170 180 190 200
NHNLDTSREY YNNIISTRTF DDRLNTLDHV RSAGMKVCSG GIVGLGEQKQ
210 220 230 240 250
DRIGLLHELA TLPIHPESVP INMLVPIEGT PLADVEKLDV TEWIRTIAVA
260 270 280 290 300
RIIMPYSYIR LSAGRESLSD SDQALAFMAG ANSLFSGDKL LTTPNAGEGK
310 320
DQVLFAKLGL VAEKPKVSVR AMAVDAMSA
Length:329
Mass (Da):36,505
Last modified:July 28, 2009 - v2
Checksum:iD4BB94F2C0665E23
GO

Sequence cautioni

The sequence CAG68864.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR543861 Genomic DNA. Translation: CAG68864.1. Different initiation.
RefSeqiWP_011182406.1. NC_005966.1.
YP_046686.1. NC_005966.1.

Genome annotation databases

EnsemblBacteriaiCAG68864; CAG68864; ACIAD2045.
GeneIDi2879177.
KEGGiaci:ACIAD2045.
PATRICi20741796. VBIAciSp98416_1843.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR543861 Genomic DNA. Translation: CAG68864.1 . Different initiation.
RefSeqi WP_011182406.1. NC_005966.1.
YP_046686.1. NC_005966.1.

3D structure databases

ProteinModelPortali Q6FAP9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 62977.ACIAD2045.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAG68864 ; CAG68864 ; ACIAD2045 .
GeneIDi 2879177.
KEGGi aci:ACIAD2045.
PATRICi 20741796. VBIAciSp98416_1843.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci ASP62977:GJVV-1935-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. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
    Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
    Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33305 / BD413 / ADP1.

Entry informationi

Entry nameiBIOB_ACIAD
AccessioniPrimary (citable) accession number: Q6FAP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 28, 2009
Last modified: November 26, 2014
This is version 81 of the entry and version 2 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