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Protein

Kynureninase

Gene

kynU

Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.UniRule annotation

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase (kynU)
This subpathway is part of the pathway L-kynurenine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Kynureninase (kynU)
  3. no protein annotated in this organism
This subpathway is part of the pathway NAD(+) 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 quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei104Pyridoxal phosphate; via amide nitrogenUniRule annotation1
Binding sitei105Pyridoxal phosphateUniRule annotation1
Binding sitei213Pyridoxal phosphateUniRule annotation1
Binding sitei216Pyridoxal phosphateUniRule annotation1
Binding sitei238Pyridoxal phosphateUniRule annotation1
Binding sitei267Pyridoxal phosphateUniRule annotation1
Binding sitei295Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processPyridine nucleotide biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciBTHU281309:G1G14-2603-MONOMER
UniPathwayi
UPA00253;UER00329

UPA00334;UER00455

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:kynUUniRule annotation
Ordered Locus Names:BT9727_2523
OrganismiBacillus thuringiensis subsp. konkukian (strain 97-27)
Taxonomic identifieri281309 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001301 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003569921 – 428KynureninaseAdd BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei239N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6HHX7
SMRiQ6HHX7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 135Pyridoxal phosphate bindingUniRule annotation4

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000242438
KOiK01556
OMAiVCSLHAS

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_01970 Kynureninase, 1 hit
InterProiView protein in InterPro
IPR000192 Aminotrans_V_dom
IPR010111 Kynureninase
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR14084 PTHR14084, 1 hit
PfamiView protein in Pfam
PF00266 Aminotran_5, 1 hit
PIRSFiPIRSF038800 KYNU, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01814 kynureninase, 1 hit

Sequencei

Sequence statusi: Complete.

Q6HHX7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA
60 70 80 90 100
EKSLLTLLDS WKEYGIDGWT EGEHPWFFLS EKLGELTAPL IGALPEESIV
110 120 130 140 150
TGSTTTNIHQ VIATFYEPKG IRTKILADEL TFPSDIYALQ SQIRLKGLDP
160 170 180 190 200
DEHLVRVKSR DGRTLSEDDI IQAMTDDIAL ILLPSVLYRS GQILDMKRLT
210 220 230 240 250
AEAHERGIHI GFDLCHSIGS IPHHFKEWDV DFAIWCNYKY LNAGPGGVAG
260 270 280 290 300
LYVNKKHFNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHILS
310 320 330 340 350
TAPLIGSLEI FKDAGIERLR EKSLHITRYM LNLIDHELKD FGFAIGNPLE
360 370 380 390 400
DEKRGGHIYL EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE
410 420
VWQSVMILKK IMKDEEYKQF ENKREVVA
Length:428
Mass (Da):48,659
Last modified:July 19, 2004 - v1
Checksum:iDB3E0D0AE1A3FC91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017355 Genomic DNA Translation: AAT60051.1
RefSeqiWP_000276276.1, NC_005957.1
YP_036849.1, NC_005957.1

Genome annotation databases

EnsemblBacteriaiAAT60051; AAT60051; BT9727_2523
GeneIDi2855106
KEGGibtk:BT9727_2523
PATRICifig|281309.8.peg.2671

Similar proteinsi

Entry informationi

Entry nameiKYNU_BACHK
AccessioniPrimary (citable) accession number: Q6HHX7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 19, 2004
Last modified: February 28, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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