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Q5LEY1

- BIOAB_BACFN

UniProt

Q5LEY1 - BIOAB_BACFN

Protein

Biotin biosynthesis bifunctional protein BioAB

Gene

bioB

Organism
Bacteroides fragilis (strain ATCC 25285 / NCTC 9343)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    Catalyzes two activities which are involved in the biotine biosynthesis: the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism, and the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA).By similarity

    Catalytic activityi

    Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.
    S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate.

    Cofactori

    Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.By similarity
    Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine By similarity.By similarity
    Pyridoxal phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
    Metal bindingi106 – 1061Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi138 – 1381Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi198 – 1981Iron-sulfur 2 (2Fe-2S)By similarity
    Metal bindingi268 – 2681Iron-sulfur 2 (2Fe-2S)By similarity
    Sitei333 – 3331Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAMBy similarity
    Binding sitei368 – 36817-keto-8-aminopelargonic acidBy similarity
    Binding sitei461 – 46117-keto-8-aminopelargonic acidBy similarity
    Binding sitei562 – 5621Pyridoxal phosphateBy similarity
    Binding sitei591 – 59117-keto-8-aminopelargonic acidBy similarity
    Binding sitei624 – 62417-keto-8-aminopelargonic acid; via carbonyl oxygenBy similarity
    Binding sitei708 – 70817-keto-8-aminopelargonic acidBy similarity

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. adenosylmethionine-8-amino-7-oxononanoate transaminase activity Source: UniProtKB-EC
    4. biotin synthase activity Source: UniProtKB-EC
    5. metal ion binding Source: UniProtKB-KW
    6. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. biotin biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Biotin biosynthesis

    Keywords - Ligandi

    2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciBFRA272559:GKF0-1552-MONOMER.
    UniPathwayiUPA00078; UER00160.
    UPA00078; UER00162.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin biosynthesis bifunctional protein BioAB
    Including the following 2 domains:
    Biotin synthase BioB (EC:2.8.1.6)
    Adenosylmethionine-8-amino-7-oxononanoate aminotransferase BioA (EC:2.6.1.62)
    Alternative name(s):
    7,8-diamino-pelargonic acid aminotransferase
    Short name:
    DAPA AT
    Short name:
    DAPA aminotransferase
    7,8-diaminononanoate synthase
    Short name:
    DANS
    Diaminopelargonic acid synthase
    Gene namesi
    Name:bioB
    Ordered Locus Names:BF1617
    OrganismiBacteroides fragilis (strain ATCC 25285 / NCTC 9343)
    Taxonomic identifieri272559 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    ProteomesiUP000006731: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 748748Biotin biosynthesis bifunctional protein BioABPRO_0000381227Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei591 – 5911N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi272559.BF1617.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5LEY1.
    SMRiQ5LEY1. Positions 321-740.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni428 – 4292Pyridoxal phosphate bindingBy similarity
    Regioni625 – 6262Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the radical SAM superfamily. Biotin synthase family.Curated
    In the C-terminal section; belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000291940.
    KOiK00833.
    OMAiKWCAQSS.
    OrthoDBiEOG6QVRHN.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPiMF_00834. BioA.
    MF_01694. BioB.
    InterProiIPR013785. Aldolase_TIM.
    IPR005814. Aminotrans_3.
    IPR010722. BATS_dom.
    IPR005815. BioA.
    IPR002684. Biotin_synth/BioAB.
    IPR006638. Elp3/MiaB/NifB.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR007197. rSAM.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    PF06968. BATS. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view]
    SMARTiSM00876. BATS. 1 hit.
    SM00729. Elp3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00508. bioA. 1 hit.
    TIGR00433. bioB. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5LEY1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTIEEIKNQV LQGTAISREQ AEWLALYPRK EELYDAAHDI TTACASQEFD    50
    MCSIINARSG RCPENCKWCA QSSHYKTKAD VYDLVSADEC LRQAKYNEAQ 100
    GVNRFSLVTS GRKPSPKNMK ELCVAARRMR RHSSIRLCAS LGLLDEEELQ 150
    ALYDAGVTRY HCNLETAPSH FDSLCTTHTQ EQKLKTLHAA RRVGMDLCCG 200
    GIIGMGETVE QRIEFAFTLR DLNIQSIPIN LLQPIPGTPL EHQSPLSEEE 250
    ILTTVALFRF INPAAYLRFA GGRSQLTPEA VRKSLYIGIN SAIVGDLLTT 300
    LGSKVSDDKE MILSEGYHFA DSQFDREHLW HPYTSTSNPL PVYKVKRADG 350
    ATITLESGQT LIEGMSSWWC AVHGYNHPIL NQAVQDQLSR MSHVMFGGLT 400
    HDPAIELGKL LLPLVPPSMQ KIFYADSGSV AVEVALKMAV QYWYAAGKPE 450
    KNNFVTIRNG YHGDTWNAMS VCDPVTGMHS IFGSALPIRH FLPAPSSRFG 500
    DEWNPEDIRP LEYLLEKHAD ELAAFILEPI VQGAGGMRFY HPEYLKEAAR 550
    LCHRYGVLLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL 600
    SAVLTTNEVA DCISNHAPGA FMHGPTFMGN PLACAVACAS VRLLLTSGWQ 650
    ENVKRIEAQL NRELAPAREL PQVADVRVLG AIGVIEMKEP VNMAYLQRRF 700
    VEEGIWLRPF GKLIYVMPPF IITPEQLTKL TEGMIRIISN GLPGSQTK 748
    Length:748
    Mass (Da):83,164
    Last modified:June 21, 2005 - v1
    Checksum:i611586B40A861A51
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR626927 Genomic DNA. Translation: CAH07318.1.
    RefSeqiWP_010992602.1. NC_003228.3.
    YP_211257.1. NC_003228.3.

    Genome annotation databases

    EnsemblBacteriaiCAH07318; CAH07318; BF9343_1537.
    GeneIDi3289161.
    KEGGibfs:BF1617.
    PATRICi21039656. VBIBacFra29119_1576.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR626927 Genomic DNA. Translation: CAH07318.1 .
    RefSeqi WP_010992602.1. NC_003228.3.
    YP_211257.1. NC_003228.3.

    3D structure databases

    ProteinModelPortali Q5LEY1.
    SMRi Q5LEY1. Positions 321-740.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272559.BF1617.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH07318 ; CAH07318 ; BF9343_1537 .
    GeneIDi 3289161.
    KEGGi bfs:BF1617.
    PATRICi 21039656. VBIBacFra29119_1576.

    Phylogenomic databases

    eggNOGi COG0502.
    HOGENOMi HOG000291940.
    KOi K00833.
    OMAi KWCAQSS.
    OrthoDBi EOG6QVRHN.

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00160 .
    UPA00078 ; UER00162 .
    BioCyci BFRA272559:GKF0-1552-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPi MF_00834. BioA.
    MF_01694. BioB.
    InterProi IPR013785. Aldolase_TIM.
    IPR005814. Aminotrans_3.
    IPR010722. BATS_dom.
    IPR005815. BioA.
    IPR002684. Biotin_synth/BioAB.
    IPR006638. Elp3/MiaB/NifB.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR007197. rSAM.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    PF06968. BATS. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    SMARTi SM00876. BATS. 1 hit.
    SM00729. Elp3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR00508. bioA. 1 hit.
    TIGR00433. bioB. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 25285 / NCTC 9343.

    Entry informationi

    Entry nameiBIOAB_BACFN
    AccessioniPrimary (citable) accession number: Q5LEY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 65 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, Multifunctional enzyme, 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