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Q8A7T2 (BIOAB_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BT_1442
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides ›

Protein attributes

Sequence length741 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.

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.

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 caution

The sequence AAO76549.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 741741Biotin biosynthesis bifunctional protein BioAB HAMAP-Rule MF_00834
PRO_0000381234

Regions

Region428 – 4292Pyridoxal phosphate binding HAMAP-Rule MF_00834
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
Q8A7T2 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 6FA1F6EE5879C1DD

FASTA74182,116
        10         20         30         40         50         60 
MTLQEIKDQV LAGFDISSAQ ATWLANMADS EALYAAAHEI TITCASHEFD MCSIINAKSG 

        70         80         90        100        110        120 
RCPENCKWCA QSSHYKTQAE IYDLLPAEEC LRQAKYNESQ DVNRFSLVTS GRKPSPKQIS 

       130        140        150        160        170        180 
QLCDAARLMR KHSSIQLCAS LGLLNEEELR ALHTAGITRY HCNLETAPSY FPTLCSTHTQ 

       190        200        210        220        230        240 
EQKLATLDAA RRVGMDICCG GIIGMGETME QRIEFAFTLA ELNVQSIPIN LLSPIPGTPL 

       250        260        270        280        290        300 
ENEKALSEEE ILRTIALFRF INPTAFLRFA GGRSQLTPEA MRKALFVGIN SAIVGDLLTT 

       310        320        330        340        350        360 
LGSKVSDDKK MILEEGYHFA DSQFDREHLW HPYTSTTDPL PVYKVKRADG ATITLEDGRT 

       370        380        390        400        410        420 
LIEGMSSWWC AVHGYNHPVL NQAAKDQLDK MSHVMFGGLT HDPAIELGKL LLPLVPPSMQ 

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

       490        500        510        520        530        540 
LFGSSLPVRY FVPAPSSRFD GEWNPDEIIP LRETIEKHSK ELAALILEPI VQGAGGMWFY 

       550        560        570        580        590        600 
HPQYLREAEK LCKEHDILLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL 

       610        620        630        640        650        660 
SAVLASNQIA DTISNHAPKA FMHGPTFMGN PLACAVACAS VRLLLDSGWA ENVKRIEAQL 

       670        680        690        700        710        720 
KEELAPARKF PQVADVRILG AIGVIQTERS VSMAYMQRRF VEEGIWVRPF GKLVYLMPPF 

       730        740 
IISPEQLSKL TSGVLKIVRE M

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References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015928 Genomic DNA. Translation: AAO76549.1. Different initiation.
RefSeqNP_810355.1. NC_004663.1.

3D structure databases

HSSPHSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ProteinModelPortalQ8A7T2.
ModBaseSearch...

Protein-protein interaction databases

STRING226186.BT_1442.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO76549; AAO76549; BT_1442.
GeneID1076134.
KEGGbth:BT_1442.
PATRIC21057749. VBIBacThe70966_1474.

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000138865.
KOK00833.
OMACPENCKW.
ProtClustDBCLSK377747.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-1471-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_BACTN
AccessionPrimary (citable) accession number: Q8A7T2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 28, 2009
Last modified: May 1, 2013
This is version 71 of the entry and version 2 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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