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E6SRG2

- BIOAB_BACT6

UniProt

E6SRG2 - BIOAB_BACT6

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Protein

Biotin biosynthesis bifunctional protein BioAB

Gene

bioB

Organism
Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108)
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 sitei710 – 71017-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

BioCyciBHEL693979:GHID-2149-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:Bache_2094
OrganismiBacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108)
Taxonomic identifieri693979 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000008630: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 744744Biotin biosynthesis bifunctional protein BioABPRO_0000411134Add
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

ProteinModelPortaliE6SRG2.
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

HOGENOMiHOG000138865.
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.

E6SRG2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVNELKEQV LEGNFISREE AEWLAAQSDK EALYEAAHEI TRTLASEEFD
60 70 80 90 100
MCSIINAKSG RCPENCKWCA QSSHYKTKAD VYDLVDKEEC LRHAKYNEEQ
110 120 130 140 150
GVARFSLVTS GRKPSGKNME KLCEAARHMR RHSSIQLCAS LGLLNEEEML
160 170 180 190 200
ALHDAGITRY HCNLETAPSY FSNLCSTHTQ AEKIRTLKAA RNAGMDICSG
210 220 230 240 250
GIIGMGESME QRIEFAFTLK DMEVQSIPIN LLSPIPGTPL ERQEPLNEEE
260 270 280 290 300
ILTTIALFRF INPRAFLRFA GGRSQLSTEA VRKALHIGIN SAIVGDLLTT
310 320 330 340 350
IGSKVSEDKT LIEEAGYRFS DSQFDREHLW HPYTSTTDPL PVYKVEQAEG
360 370 380 390 400
ATITLESGQT LIEGMSSWWC AIHGYNNPVL NHAATEQIGK MSHVMFGGLT
410 420 430 440 450
HEPAIELGKL LLPLVPPSMQ KIFYADSGSV AVEVALKMAV QYWYGKGKEK
460 470 480 490 500
KNNFVTIRSG YHGDTWNAMS VCDPVTGMHS LFGSSLPIRY FAPQPRSRYD
510 520 530 540 550
GDWDAGDSME LQNIIEQHHE ELAALILEPI VQGAGGMWFY HPQYLREAAR
560 570 580 590 600
LCKQYGLLLI FDEIATGFGR TGKLFAWEHA GTEPDIMCIG KALTGGYMTL
610 620 630 640 650
SAVLTTNEVA DAISNHSPGV FMHGPTFMGN PLACAVACAS VRLLTSPVYD
660 670 680 690 700
WQGKVNRISM QLREELAPAR QLPQVKDVRI LGAIGVIEVT ENVDMAWMQR
710 720 730 740
RFVEEGIWVR PFGKLVYLMP PFIIEPEQLT KLTSGLIKII KEML
Length:744
Mass (Da):82,983
Last modified:March 8, 2011 - v1
Checksum:i6D94D64153D41FC0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002352 Genomic DNA. Translation: ADV44065.1.
RefSeqiYP_004161651.1. NC_014933.1.

Genome annotation databases

EnsemblBacteriaiADV44065; ADV44065; Bache_2094.
GeneIDi10140872.
KEGGibhl:Bache_2094.
PATRICi45174812. VBIBacHel147569_2204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002352 Genomic DNA. Translation: ADV44065.1 .
RefSeqi YP_004161651.1. NC_014933.1.

3D structure databases

ProteinModelPortali E6SRG2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADV44065 ; ADV44065 ; Bache_2094 .
GeneIDi 10140872.
KEGGi bhl:Bache_2094.
PATRICi 45174812. VBIBacHel147569_2204.

Phylogenomic databases

HOGENOMi HOG000138865.
KOi K00833.
OMAi KWCAQSS.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00160 .
UPA00078 ; UER00162 .
BioCyci BHEL693979:GHID-2149-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 35417 / DSM 20613 / JCM 6297 / P 36-108.

Entry informationi

Entry nameiBIOAB_BACT6
AccessioniPrimary (citable) accession number: E6SRG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: March 8, 2011
Last modified: October 29, 2014
This is version 27 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