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Q5LEY1

- BIOAB_BACFN

UniProt

Q5LEY1 - BIOAB_BACFN

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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

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

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.By similarity
  • pyridoxal 5'-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
Complete GO annotation...

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

        10         20         30         40         50
MTIEEIKNQV LQGTAISREQ AEWLALYPRK EELYDAAHDI TTACASQEFD
60 70 80 90 100
MCSIINARSG RCPENCKWCA QSSHYKTKAD VYDLVSADEC LRQAKYNEAQ
110 120 130 140 150
GVNRFSLVTS GRKPSPKNMK ELCVAARRMR RHSSIRLCAS LGLLDEEELQ
160 170 180 190 200
ALYDAGVTRY HCNLETAPSH FDSLCTTHTQ EQKLKTLHAA RRVGMDLCCG
210 220 230 240 250
GIIGMGETVE QRIEFAFTLR DLNIQSIPIN LLQPIPGTPL EHQSPLSEEE
260 270 280 290 300
ILTTVALFRF INPAAYLRFA GGRSQLTPEA VRKSLYIGIN SAIVGDLLTT
310 320 330 340 350
LGSKVSDDKE MILSEGYHFA DSQFDREHLW HPYTSTSNPL PVYKVKRADG
360 370 380 390 400
ATITLESGQT LIEGMSSWWC AVHGYNHPIL NQAVQDQLSR MSHVMFGGLT
410 420 430 440 450
HDPAIELGKL LLPLVPPSMQ KIFYADSGSV AVEVALKMAV QYWYAAGKPE
460 470 480 490 500
KNNFVTIRNG YHGDTWNAMS VCDPVTGMHS IFGSALPIRH FLPAPSSRFG
510 520 530 540 550
DEWNPEDIRP LEYLLEKHAD ELAAFILEPI VQGAGGMRFY HPEYLKEAAR
560 570 580 590 600
LCHRYGVLLI FDEIATGFGR TGKLFAWEHA GVEPDIMCIG KALTGGYMTL
610 620 630 640 650
SAVLTTNEVA DCISNHAPGA FMHGPTFMGN PLACAVACAS VRLLLTSGWQ
660 670 680 690 700
ENVKRIEAQL NRELAPAREL PQVADVRVLG AIGVIEMKEP VNMAYLQRRF
710 720 730 740
VEEGIWLRPF GKLIYVMPPF IITPEQLTKL TEGMIRIISN GLPGSQTK
Length:748
Mass (Da):83,164
Last modified:June 21, 2005 - v1
Checksum:i611586B40A861A51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 66 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