Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-Lysine--8-amino-7-oxononanoate transaminase

Gene

bioK

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the alpha-amino group from L-lysine to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine as an amino donor in the biosynthesis of DAPA.1 Publication

Catalytic activityi

L-lysine + 8-amino-7-oxononanoate = (S)-2-amino-6-oxohexanoate + 7,8-diaminononanoate.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Enzyme regulationi

Inhibited by 7-keto-8-aminopelargonic acid at concentrations above 80 µM.1 Publication

pH dependencei

Optimum pH is 8.6.1 Publication

Pathwayi: biotin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route).
Proteins known to be involved in this subpathway in this organism are:
  1. L-Lysine--8-amino-7-oxononanoate transaminase (bioK)
This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route), the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei17Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAMBy similarity1
Binding sitei146Substrate1
Binding sitei251Pyridoxal phosphateBy similarity1
Binding sitei280SubstrateBy similarity1
Binding sitei315Substrate; via carbonyl oxygen1
Binding sitei410Substrate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciBSUB:BSU30230-MONOMER.
MetaCyc:BSU30230-MONOMER.
BRENDAi2.6.1.105. 658.
UniPathwayiUPA00078; UER00160.

Names & Taxonomyi

Protein namesi
Recommended name:
L-Lysine--8-amino-7-oxononanoate transaminase (EC:2.6.1.105)
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
L-Lysine--8-amino-7-oxononanoate aminotransferase
Gene namesi
Name:bioK
Synonyms:bioA
Ordered Locus Names:BSU30230
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001203611 – 448L-Lysine--8-amino-7-oxononanoate transaminaseAdd BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei280N6-(pyridoxal phosphate)lysine1

Proteomic databases

PaxDbiP53555.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP53555. 1 interactor.
MINTiMINT-8366234.
STRINGi224308.Bsubs1_010100016466.

Structurei

Secondary structure

1448
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 12Combined sources9
Helixi20 – 25Combined sources6
Beta strandi29 – 35Combined sources7
Beta strandi37 – 40Combined sources4
Beta strandi45 – 48Combined sources4
Helixi51 – 54Combined sources4
Helixi63 – 73Combined sources11
Beta strandi82 – 86Combined sources5
Helixi87 – 99Combined sources13
Beta strandi104 – 112Combined sources9
Helixi113 – 130Combined sources18
Beta strandi138 – 143Combined sources6
Helixi151 – 155Combined sources5
Turni160 – 162Combined sources3
Beta strandi163 – 166Combined sources4
Helixi167 – 169Combined sources3
Beta strandi174 – 177Combined sources4
Beta strandi184 – 186Combined sources3
Helixi189 – 207Combined sources19
Helixi208 – 210Combined sources3
Beta strandi211 – 222Combined sources12
Turni223 – 225Combined sources3
Helixi233 – 243Combined sources11
Beta strandi247 – 251Combined sources5
Turni253 – 260Combined sources8
Beta strandi261 – 264Combined sources4
Helixi265 – 269Combined sources5
Beta strandi274 – 278Combined sources5
Helixi280 – 283Combined sources4
Beta strandi290 – 295Combined sources6
Helixi296 – 300Combined sources5
Helixi306 – 308Combined sources3
Turni317 – 320Combined sources4
Helixi322 – 337Combined sources16
Helixi340 – 358Combined sources19
Beta strandi364 – 370Combined sources7
Beta strandi373 – 378Combined sources6
Turni382 – 385Combined sources4
Helixi390 – 392Combined sources3
Helixi394 – 404Combined sources11
Beta strandi415 – 418Combined sources4
Helixi426 – 444Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DODX-ray1.90A/B1-448[»]
3DRDX-ray2.17A/B1-448[»]
3DU4X-ray2.20A/B1-448[»]
ProteinModelPortaliP53555.
SMRiP53555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 114Pyridoxal phosphate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108JPX. Bacteria.
COG0161. LUCA.
HOGENOMiHOG000020209.
InParanoidiP53555.
KOiK19563.
OMAiMAFEYCK.
PhylomeDBiP53555.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00834. BioA. 1 hit.
InterProiIPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00508. bioA. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHDLIEKSK KHLWLPFTQM KDYDENPLII ESGTGIKVKD INGKEYYDGF
60 70 80 90 100
SSVWLNVHGH RKKELDDAIK KQLGKIAHST LLGMTNVPAT QLAETLIDIS
110 120 130 140 150
PKKLTRVFYS DSGAEAMEIA LKMAFQYWKN IGKPEKQKFI AMKNGYHGDT
160 170 180 190 200
IGAVSVGSIE LFHHVYGPLM FESYKAPIPY VYRSESGDPD ECRDQCLREL
210 220 230 240 250
AQLLEEHHEE IAALSIESMV QGASGMIVMP EGYLAGVREL CTTYDVLMIV
260 270 280 290 300
DEVATGFGRT GKMFACEHEN VQPDLMAAGK GITGGYLPIA VTFATEDIYK
310 320 330 340 350
AFYDDYENLK TFFHGHSYTG NQLGCAVALE NLALFESENI VEQVAEKSKK
360 370 380 390 400
LHFLLQDLHA LPHVGDIRQL GFMCGAELVR SKETKEPYPA DRRIGYKVSL
410 420 430 440
KMRELGMLTR PLGDVIAFLP PLASTAEELS EMVAIMKQAI HEVTSLED
Length:448
Mass (Da):50,112
Last modified:October 1, 1996 - v1
Checksum:i38F104A93A74AA24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51868 Genomic DNA. Translation: AAB17458.1.
AF008220 Genomic DNA. Translation: AAC00262.1.
AL009126 Genomic DNA. Translation: CAB15001.1.
PIRiC69594.
RefSeqiNP_390901.1. NC_000964.3.
WP_004398913.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB15001; CAB15001; BSU30230.
GeneIDi936286.
KEGGibsu:BSU30230.
PATRICi18977948. VBIBacSub10457_3162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51868 Genomic DNA. Translation: AAB17458.1.
AF008220 Genomic DNA. Translation: AAC00262.1.
AL009126 Genomic DNA. Translation: CAB15001.1.
PIRiC69594.
RefSeqiNP_390901.1. NC_000964.3.
WP_004398913.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DODX-ray1.90A/B1-448[»]
3DRDX-ray2.17A/B1-448[»]
3DU4X-ray2.20A/B1-448[»]
ProteinModelPortaliP53555.
SMRiP53555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53555. 1 interactor.
MINTiMINT-8366234.
STRINGi224308.Bsubs1_010100016466.

Proteomic databases

PaxDbiP53555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15001; CAB15001; BSU30230.
GeneIDi936286.
KEGGibsu:BSU30230.
PATRICi18977948. VBIBacSub10457_3162.

Phylogenomic databases

eggNOGiENOG4108JPX. Bacteria.
COG0161. LUCA.
HOGENOMiHOG000020209.
InParanoidiP53555.
KOiK19563.
OMAiMAFEYCK.
PhylomeDBiP53555.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00160.
BioCyciBSUB:BSU30230-MONOMER.
MetaCyc:BSU30230-MONOMER.
BRENDAi2.6.1.105. 658.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00834. BioA. 1 hit.
InterProiIPR005814. Aminotrans_3.
IPR005815. BioA.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00508. bioA. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBIOK_BACSU
AccessioniPrimary (citable) accession number: P53555
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 127 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.