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Protein

Kynureninase

Gene

kynU

Organism
Bacillus clausii (strain KSM-K16)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

Pathway: 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.

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei105 – 1051Pyridoxal phosphateUniRule annotation
Binding sitei213 – 2131Pyridoxal phosphateUniRule annotation
Binding sitei216 – 2161Pyridoxal phosphateUniRule annotation
Binding sitei238 – 2381Pyridoxal phosphateUniRule annotation
Binding sitei267 – 2671Pyridoxal phosphateUniRule annotation
Binding sitei295 – 2951Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBCLA66692:GHMP-681-MONOMER.
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 annotation
Ordered Locus Names:ABC0651
OrganismiBacillus clausii (strain KSM-K16)
Taxonomic identifieri66692 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001168 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427KynureninasePRO_0000356993Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi66692.ABC0651.

Structurei

3D structure databases

ProteinModelPortaliQ5WKB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 1354Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
OMAiRFWQPLS.
OrthoDBiEOG6N67XP.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5WKB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPCFDSVYTK EYAQQLDAVD PLARFRNEFY IDEDSIYLDG NSLGLLSTRA
60 70 80 90 100
EQSLLDVLDS WKQYGIDGWT KGKHPWFYLS ESLGEKMASL VGAKAEEVIV
110 120 130 140 150
TGSTTTNLHQ LVSSFFRPEG KKTKILADEL NFPSDIYALK SQLHLQGFDP
160 170 180 190 200
EEHLIQVKSD NGHLLNEEDI IAEMKEDIAL IVLPSVLYRS GQILDMERLT
210 220 230 240 250
TAAHQRNILI GFDLCHSIGA IPHQLRKWDV DFAFWCTYKH VNGGPGSVAA
260 270 280 290 300
LFVNEKHFGR RPGLAGWFSS NKQKQFDMEH TLTPAEHAGA FQIGTPHIFS
310 320 330 340 350
IAPLIGSLAI FAEAGIEQIR KKSLKLTDYM MTLIEHELSD YQFTIQNPRD
360 370 380 390 400
ERRGAHLYIE HDEAARICKA LKEENVIPDF RSPKGIRLAP VALYNTFKEV
410 420
WNTIQVLKFI MKEERYKKFK NERDVVA
Length:427
Mass (Da):48,667
Last modified:November 23, 2004 - v1
Checksum:i19F67CEC50D893AC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD63190.1.
RefSeqiWP_011245506.1. NC_006582.1.
YP_174151.1. NC_006582.1.

Genome annotation databases

EnsemblBacteriaiBAD63190; BAD63190; ABC0651.
KEGGibcl:ABC0651.
PATRICi18920560. VBIBacCla58185_0685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD63190.1.
RefSeqiWP_011245506.1. NC_006582.1.
YP_174151.1. NC_006582.1.

3D structure databases

ProteinModelPortaliQ5WKB5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi66692.ABC0651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD63190; BAD63190; ABC0651.
KEGGibcl:ABC0651.
PATRICi18920560. VBIBacCla58185_0685.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
OMAiRFWQPLS.
OrthoDBiEOG6N67XP.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
BioCyciBCLA66692:GHMP-681-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
    Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KSM-K16.

Entry informationi

Entry nameiKYNU_BACSK
AccessioniPrimary (citable) accession number: Q5WKB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 23, 2004
Last modified: May 27, 2015
This is version 73 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, 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

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 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.