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Protein

Kynureninase

Gene

kynU

Organism
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei110 – 1101Pyridoxal phosphateUniRule annotation
Binding sitei222 – 2221Pyridoxal phosphateUniRule annotation
Binding sitei225 – 2251Pyridoxal phosphateUniRule annotation
Binding sitei247 – 2471Pyridoxal phosphateUniRule annotation
Binding sitei278 – 2781Pyridoxal phosphateUniRule annotation
Binding sitei306 – 3061Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciSTRO369723:GI49-3575-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:Strop_3530
OrganismiSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Taxonomic identifieri369723 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora
ProteomesiUP000000235: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429KynureninasePRO_0000357011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi369723.Strop_3530.

Structurei

3D structure databases

ProteinModelPortaliA4XAL2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 1404Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
OMAiWLPYHEL.
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.

A4XAL2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MREEELIQEE KAANRLDTAD PGHRHLFHVP PADGGRYQQA AYLAGNSLGL
60 70 80 90 100
QPRATRDELF ADLEAWRRLG VEGHLAADRP WLPYHELLTA PTARLVGARP
110 120 130 140 150
AEVVVMNSLT VNLHLLMVSF YRPTGVRTRI VIEDSAFPSD SYAVRSQARF
160 170 180 190 200
HGLDPDSTVV RLAPRPGEDT LRTADVRDLL AAEGDTIALV LLGGVNYLTG
210 220 230 240 250
ELMEIPEITA AGRAAGAVVG WDLAHAAGNV PLALHDWDVD FAAWCSYKYL
260 270 280 290 300
NSGPGGLSGV FVHERHLADP TLPRFEGWWS TEAATRFEMS PVARPPATAE
310 320 330 340 350
AWQVSNPPIL AMGPVRTSLE VFDSVGMTAL RERSVRLTGY LEWLLDQVTP
360 370 380 390 400
GRPLAVVTPR DPDRRGAQLS VRIGTGSAAE LAKRLRLEHG VVADAREPDV
410 420
VRFAPVPLYS TYHDCWRVAD ALAATVEVH
Length:429
Mass (Da):46,976
Last modified:May 29, 2007 - v1
Checksum:i49393A089963E960
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000667 Genomic DNA. Translation: ABP55961.1.
RefSeqiYP_001160339.1. NC_009380.1.

Genome annotation databases

EnsemblBacteriaiABP55961; ABP55961; Strop_3530.
GeneIDi5060004.
KEGGistp:Strop_3530.
PATRICi23446224. VBISalTro43511_3644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000667 Genomic DNA. Translation: ABP55961.1.
RefSeqiYP_001160339.1. NC_009380.1.

3D structure databases

ProteinModelPortaliA4XAL2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi369723.Strop_3530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP55961; ABP55961; Strop_3530.
GeneIDi5060004.
KEGGistp:Strop_3530.
PATRICi23446224. VBISalTro43511_3644.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
OMAiWLPYHEL.
OrthoDBiEOG6N67XP.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.
BioCyciSTRO369723:GI49-3575-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. "Complete sequence of Salinispora tropica CNB-440."
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Entry informationi

Entry nameiKYNU_SALTO
AccessioniPrimary (citable) accession number: A4XAL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 29, 2007
Last modified: January 7, 2015
This is version 60 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.