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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei17 – 171Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAMBy similarity
Binding sitei146 – 1461Substrate
Binding sitei251 – 2511Pyridoxal phosphateBy similarity
Binding sitei280 – 2801SubstrateBy similarity
Binding sitei315 – 3151Substrate; via carbonyl oxygen
Binding sitei410 – 4101Substrate

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448L-Lysine--8-amino-7-oxononanoate transaminasePRO_0000120361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei280 – 2801N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP53555.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 129Combined sources
Helixi20 – 256Combined sources
Beta strandi29 – 357Combined sources
Beta strandi37 – 404Combined sources
Beta strandi45 – 484Combined sources
Helixi51 – 544Combined sources
Helixi63 – 7311Combined sources
Beta strandi82 – 865Combined sources
Helixi87 – 9913Combined sources
Beta strandi104 – 1129Combined sources
Helixi113 – 13018Combined sources
Beta strandi138 – 1436Combined sources
Helixi151 – 1555Combined sources
Turni160 – 1623Combined sources
Beta strandi163 – 1664Combined sources
Helixi167 – 1693Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi184 – 1863Combined sources
Helixi189 – 20719Combined sources
Helixi208 – 2103Combined sources
Beta strandi211 – 22212Combined sources
Turni223 – 2253Combined sources
Helixi233 – 24311Combined sources
Beta strandi247 – 2515Combined sources
Turni253 – 2608Combined sources
Beta strandi261 – 2644Combined sources
Helixi265 – 2695Combined sources
Beta strandi274 – 2785Combined sources
Helixi280 – 2834Combined sources
Beta strandi290 – 2956Combined sources
Helixi296 – 3005Combined sources
Helixi306 – 3083Combined sources
Turni317 – 3204Combined sources
Helixi322 – 33716Combined sources
Helixi340 – 35819Combined sources
Beta strandi364 – 3707Combined sources
Beta strandi373 – 3786Combined sources
Turni382 – 3854Combined sources
Helixi390 – 3923Combined sources
Helixi394 – 40411Combined sources
Beta strandi415 – 4184Combined sources
Helixi426 – 44419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DODX-ray1.90A/B1-448[»]
3DRDX-ray2.17A/B1-448[»]
3DU4X-ray2.20A/B1-448[»]
ProteinModelPortaliP53555.
SMRiP53555. Positions 1-448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 1142Pyridoxal phosphate binding

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3DODX-ray1.90A/B1-448[»]
3DRDX-ray2.17A/B1-448[»]
3DU4X-ray2.20A/B1-448[»]
ProteinModelPortaliP53555.
SMRiP53555. Positions 1-448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53555. 1 interaction.
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: September 7, 2016
This is version 125 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.