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Q5LEY1 (BIOAB_BACFN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biotin biosynthesis bifunctional protein BioAB

Including the following 2 domains:

  1. Biotin synthase BioB
    EC=2.8.1.6
  2. 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 names
Name:bioB
Ordered Locus Names:BF1617
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length748 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00834

Catalytic activity

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_00834

S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate. HAMAP-Rule MF_00834

Cofactor

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

Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine By similarity.

Pyridoxal phosphate.

Pathway

Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. HAMAP-Rule MF_00834

Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. HAMAP-Rule MF_00834

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00834

Sequence similarities

In the N-terminal section; belongs to the radical SAM superfamily. Biotin synthase family.

In the C-terminal section; belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 748748Biotin biosynthesis bifunctional protein BioAB HAMAP-Rule MF_00834
PRO_0000381227

Regions

Region428 – 4292Pyridoxal phosphate binding By similarity
Region625 – 6262Pyridoxal phosphate binding By similarity

Sites

Metal binding621Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding661Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding691Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1061Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1381Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1981Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2681Iron-sulfur 2 (2Fe-2S) By similarity
Binding site36817-keto-8-aminopelargonic acid By similarity
Binding site46117-keto-8-aminopelargonic acid By similarity
Binding site5621Pyridoxal phosphate By similarity
Binding site59117-keto-8-aminopelargonic acid By similarity
Binding site62417-keto-8-aminopelargonic acid; via carbonyl oxygen By similarity
Binding site70817-keto-8-aminopelargonic acid By similarity
Site3331Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM By similarity

Amino acid modifications

Modified residue5911N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LEY1 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 611586B40A861A51

FASTA74883,164
        10         20         30         40         50         60 
MTIEEIKNQV LQGTAISREQ AEWLALYPRK EELYDAAHDI TTACASQEFD MCSIINARSG 

        70         80         90        100        110        120 
RCPENCKWCA QSSHYKTKAD VYDLVSADEC LRQAKYNEAQ GVNRFSLVTS GRKPSPKNMK 

       130        140        150        160        170        180 
ELCVAARRMR RHSSIRLCAS LGLLDEEELQ ALYDAGVTRY HCNLETAPSH FDSLCTTHTQ 

       190        200        210        220        230        240 
EQKLKTLHAA RRVGMDLCCG GIIGMGETVE QRIEFAFTLR DLNIQSIPIN LLQPIPGTPL 

       250        260        270        280        290        300 
EHQSPLSEEE ILTTVALFRF INPAAYLRFA GGRSQLTPEA VRKSLYIGIN SAIVGDLLTT 

       310        320        330        340        350        360 
LGSKVSDDKE MILSEGYHFA DSQFDREHLW HPYTSTSNPL PVYKVKRADG ATITLESGQT 

       370        380        390        400        410        420 
LIEGMSSWWC AVHGYNHPIL NQAVQDQLSR MSHVMFGGLT HDPAIELGKL LLPLVPPSMQ 

       430        440        450        460        470        480 
KIFYADSGSV AVEVALKMAV QYWYAAGKPE KNNFVTIRNG YHGDTWNAMS VCDPVTGMHS 

       490        500        510        520        530        540 
IFGSALPIRH FLPAPSSRFG DEWNPEDIRP LEYLLEKHAD ELAAFILEPI VQGAGGMRFY 

       550        560        570        580        590        600 
HPEYLKEAAR LCHRYGVLLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL 

       610        620        630        640        650        660 
SAVLTTNEVA DCISNHAPGA FMHGPTFMGN PLACAVACAS VRLLLTSGWQ ENVKRIEAQL 

       670        680        690        700        710        720 
NRELAPAREL PQVADVRVLG AIGVIEMKEP VNMAYLQRRF VEEGIWLRPF GKLIYVMPPF 

       730        740 
IITPEQLTKL TEGMIRIISN GLPGSQTK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR626927 Genomic DNA. Translation: CAH07318.1.
RefSeqYP_211257.1. NC_003228.3.

3D structure databases

ProteinModelPortalQ5LEY1.
SMRQ5LEY1. Positions 321-740.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272559.BF1617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH07318; CAH07318; BF9343_1537.
GeneID3289161.
KEGGbfs:BF1617.
PATRIC21039656. VBIBacFra29119_1576.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000291940.
KOK00833.
OMAKWCAQSS.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycBFRA272559:GKF0-1552-MONOMER.
UniPathwayUPA00078; UER00160.
UPA00078; UER00162.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00834. BioA.
MF_01694. BioB.
InterProIPR013785. 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]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00508. bioA. 1 hit.
TIGR00433. bioB. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBIOAB_BACFN
AccessionPrimary (citable) accession number: Q5LEY1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 21, 2005
Last modified: June 11, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways