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

Kynureninase

Gene

kynU

Organism
Geobacillus sp. PA-3
Status
Unreviewed-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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation
L-kynurenine + H2O = anthranilate + 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 functionHydrolaseUniRule annotationImported
Biological processPyridine nucleotide biosynthesisUniRule annotation
LigandPyridoxal phosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00253; 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 annotationImported
ORF Names:GEPA3_3274Imported
OrganismiGeobacillus sp. PA-3Imported
Taxonomic identifieri1699078 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
Proteomesi
  • UP000050486 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini87 – 376Aminotran_5InterPro annotationAdd BLAST290

Region

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

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

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.

A0A0Q1EFB6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSTALEPTL EFARKLDQED PLRHFRDEFY LPPNSIYMDG NSLGLLSKRA
60 70 80 90 100
EKTLFTILQD WKLLGIDGWT KGTYPWFDLS EKIGVMLAPL VGASPEEVIA
110 120 130 140 150
TGSTTVNLHQ LVSTFYQPEG KRTKILADEL TFPSDIYALQ SQLRIHGYDP
160 170 180 190 200
STHLIRVKSR DGRFLEEEDI IAAMSEDVAL VVLPTVLYRS GQILDIQLLT
210 220 230 240 250
DEAHKRGILI GFDACHSIGA IPHSFSEWGV DFAFWCNYKY MNGGPGCVAG
260 270 280 290 300
LYVHRKHFGS APGLAGWFGS KKDKQFDMEH TFTPSLTAGA YQIGTPHLLS
310 320 330 340 350
LAPLIGSLEI FQEAGIERIR QKSLQLTNYF MYLIEQELSH FGFIIGNPKD
360 370 380 390 400
DVRRGGHISL EHEEAARICK SLKENGVIPD FRAPNIIRLA PIALYTSYEE
410 420
VWNVVQIMKK IMQEKQYKKF SNEREVVA
Length:428
Mass (Da):48,361
Last modified:January 20, 2016 - v1
Checksum:i792664FAE283EFA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LIDX01000135 Genomic DNA Translation: KQB91745.1

Genome annotation databases

EnsemblBacteriaiKQB91745; KQB91745; GEPA3_3274
PATRICifig|1699078.3.peg.1386

Similar proteinsi

Entry informationi

Entry nameiA0A0Q1EFB6_9BACI
AccessioniPrimary (citable) accession number: A0A0Q1EFB6
Entry historyiIntegrated into UniProtKB/TrEMBL: January 20, 2016
Last sequence update: January 20, 2016
Last modified: March 28, 2018
This is version 13 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health