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E6SRG2 (BIOAB_BACT6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 19. 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:Bache_2094
OrganismBacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108) [Complete proteome] [HAMAP]
Taxonomic identifier693979 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides ›

Protein attributes

Sequence length744 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 + 2 S-adenosyl-L-methionine = biotin + 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 By similarity. HAMAP-Rule MF_00834

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 – 744744Biotin biosynthesis bifunctional protein BioAB HAMAP-Rule MF_00834
PRO_0000411134

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 site71017-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
E6SRG2 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 6D94D64153D41FC0

FASTA74482,983
        10         20         30         40         50         60 
MTVNELKEQV LEGNFISREE AEWLAAQSDK EALYEAAHEI TRTLASEEFD MCSIINAKSG 

        70         80         90        100        110        120 
RCPENCKWCA QSSHYKTKAD VYDLVDKEEC LRHAKYNEEQ GVARFSLVTS GRKPSGKNME 

       130        140        150        160        170        180 
KLCEAARHMR RHSSIQLCAS LGLLNEEEML ALHDAGITRY HCNLETAPSY FSNLCSTHTQ 

       190        200        210        220        230        240 
AEKIRTLKAA RNAGMDICSG GIIGMGESME QRIEFAFTLK DMEVQSIPIN LLSPIPGTPL 

       250        260        270        280        290        300 
ERQEPLNEEE ILTTIALFRF INPRAFLRFA GGRSQLSTEA VRKALHIGIN SAIVGDLLTT 

       310        320        330        340        350        360 
IGSKVSEDKT LIEEAGYRFS DSQFDREHLW HPYTSTTDPL PVYKVEQAEG ATITLESGQT 

       370        380        390        400        410        420 
LIEGMSSWWC AIHGYNNPVL NHAATEQIGK MSHVMFGGLT HEPAIELGKL LLPLVPPSMQ 

       430        440        450        460        470        480 
KIFYADSGSV AVEVALKMAV QYWYGKGKEK KNNFVTIRSG YHGDTWNAMS VCDPVTGMHS 

       490        500        510        520        530        540 
LFGSSLPIRY FAPQPRSRYD GDWDAGDSME LQNIIEQHHE ELAALILEPI VQGAGGMWFY 

       550        560        570        580        590        600 
HPQYLREAAR LCKQYGLLLI FDEIATGFGR TGKLFAWEHA GTEPDIMCIG KALTGGYMTL 

       610        620        630        640        650        660 
SAVLTTNEVA DAISNHSPGV FMHGPTFMGN PLACAVACAS VRLLTSPVYD WQGKVNRISM 

       670        680        690        700        710        720 
QLREELAPAR QLPQVKDVRI LGAIGVIEVT ENVDMAWMQR RFVEEGIWVR PFGKLVYLMP 

       730        740 
PFIIEPEQLT KLTSGLIKII KEML

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002352 Genomic DNA. Translation: ADV44065.1.
RefSeqYP_004161651.1. NC_014933.1.

3D structure databases

ProteinModelPortalE6SRG2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV44065; ADV44065; Bache_2094.
GeneID10140872.
KEGGbhl:Bache_2094.
PATRIC45174812. VBIBacHel147569_2204.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000138865.
KOK00833.

Enzyme and pathway databases

BioCycBHEL693979:GHID-2149-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. Fused.
MF_01694. BioB. Fused.
InterProIPR013785. Aldolase_TIM.
IPR005814. Aminotrans_3.
IPR005815. BioA.
IPR010722. Biotin/thiamin_synth-assoc.
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.
PTHR11986:SF8. PTHR11986:SF8. 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. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00508. bioA. 1 hit.
TIGR00433. bioB. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBIOAB_BACT6
AccessionPrimary (citable) accession number: E6SRG2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: March 8, 2011
Last modified: May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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