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E1WTS4

- BIOAB_BACF6

UniProt

E1WTS4 - BIOAB_BACF6

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Protein

Biotin biosynthesis bifunctional protein BioAB

Gene

bioB

Organism
Bacteroides fragilis (strain 638R)
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'-phosphateBy similarity

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

BioCyciBFRA862962:GHND-1547-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:BF638R_1618
OrganismiBacteroides fragilis (strain 638R)
Taxonomic identifieri862962 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000008560: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 748748Biotin biosynthesis bifunctional protein BioABPRO_0000411133Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliE1WTS4.
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

KOiK00833.
OMAiKWCAQSS.

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.

E1WTS4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTIEEIKNQV LQGTAISREQ AEWLALYPRK EELYDAAHDI TTACASQEFD
60 70 80 90 100
MCSIINARSG RCPENCKWCA QSSHYKTKAD VYDLVSAEEC 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 LEHLLEKHTD ELAAFILEPI VQGAGGMRFY HPEYLREAAR
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):83,211
Last modified:November 30, 2010 - v1
Checksum:i12363C6F57D0DC52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FQ312004 Genomic DNA. Translation: CBW22147.1.
RefSeqiYP_005110691.1. NC_016776.1.

Genome annotation databases

EnsemblBacteriaiCBW22147; CBW22147; BF638R_1618.
GeneIDi11702631.
KEGGibfg:BF638R_1618.
PATRICi42746108. VBIBacFra167533_1624.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FQ312004 Genomic DNA. Translation: CBW22147.1 .
RefSeqi YP_005110691.1. NC_016776.1.

3D structure databases

ProteinModelPortali E1WTS4.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CBW22147 ; CBW22147 ; BF638R_1618 .
GeneIDi 11702631.
KEGGi bfg:BF638R_1618.
PATRICi 42746108. VBIBacFra167533_1624.

Phylogenomic databases

KOi K00833.
OMAi KWCAQSS.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00160 .
UPA00078 ; UER00162 .
BioCyci BFRA862962:GHND-1547-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. "Twenty-eight divergent polysaccharide loci specifying within- and amongst-strain capsule diversity in three strains of Bacteroides fragilis."
    Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M., Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A., Barron A., Clark L., Bentley S.D., Parkhill J.
    Microbiology 156:3255-3269(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 638R.

Entry informationi

Entry nameiBIOAB_BACF6
AccessioniPrimary (citable) accession number: E1WTS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: November 30, 2010
Last modified: November 26, 2014
This is version 30 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3