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Q64VX4

- BIOAB_BACFR

UniProt

Q64VX4 - BIOAB_BACFR

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Protein

Biotin biosynthesis bifunctional protein BioAB

Gene

bioB

Organism
Bacteroides fragilis (strain YCH46)
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

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).By similarity
Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine (By similarity).By similarity
Pyridoxal phosphate.By 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

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:BF1603
OrganismiBacteroides fragilis (strain YCH46)
Taxonomic identifieri295405 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000002197: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 748748Biotin biosynthesis bifunctional protein BioABPRO_0000381228Add
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

STRINGi295405.BF1603.

Structurei

3D structure databases

ProteinModelPortaliQ64VX4.
SMRiQ64VX4. Positions 321-740.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni428 – 4292Pyridoxal phosphate binding
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

eggNOGiCOG0161.
HOGENOMiHOG000032982.
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.

Q64VX4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTIEEIKNQV LQGTAISREQ AGWLALYPRK EELYDAAHDI TTACASQEFD
60 70 80 90 100
MCSIINARSG RCPENCKWCA QSSHYKTKAD VYDLVSAEEC LRQAKYNEAQ
110 120 130 140 150
GVNRFSLVTS GRKPSPKNMK ELCVAVRRMR RHSSIRLCAS LGLLDEEELQ
160 170 180 190 200
ALYDAGVTRY HCNLETAPSH FDSLCTTHTQ EQKLKTLYAA 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 LEHLLEKHAD 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):83,163
Last modified:October 25, 2004 - v1
Checksum:iEBEAA61DCA8BBD73
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006841 Genomic DNA. Translation: BAD48352.1.
RefSeqiWP_011202495.1. NC_006347.1.
YP_098886.1. NC_006347.1.

Genome annotation databases

EnsemblBacteriaiBAD48352; BAD48352; BF1603.
GeneIDi3082802.
KEGGibfr:BF1603.
PATRICi21048885. VBIBacFra17906_1560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006841 Genomic DNA. Translation: BAD48352.1 .
RefSeqi WP_011202495.1. NC_006347.1.
YP_098886.1. NC_006347.1.

3D structure databases

ProteinModelPortali Q64VX4.
SMRi Q64VX4. Positions 321-740.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 295405.BF1603.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD48352 ; BAD48352 ; BF1603 .
GeneIDi 3082802.
KEGGi bfr:BF1603.
PATRICi 21048885. VBIBacFra17906_1560.

Phylogenomic databases

eggNOGi COG0161.
HOGENOMi HOG000032982.
KOi K00833.
OMAi KWCAQSS.
OrthoDBi EOG6QVRHN.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00160 .
UPA00078 ; UER00162 .

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. "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
    Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
    Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: YCH46.

Entry informationi

Entry nameiBIOAB_BACFR
AccessioniPrimary (citable) accession number: Q64VX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 25, 2004
Last modified: October 29, 2014
This is version 67 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