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P70712

- KYNU_RAT

UniProt

P70712 - KYNU_RAT

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Protein

Kynureninase

Gene

Kynu

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.1 PublicationUniRule annotation

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.1 PublicationUniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.1 PublicationUniRule annotation

Cofactori

Pyridoxal phosphate.

Enzyme regulationi

Inhibited by o-methylbenzoylalanine (OMBA).1 Publication

Kineticsi

  1. KM=440 µM for L-kynurenine1 Publication
  2. KM=32 µM for DL-3-hydroxykynurenine1 Publication

pH dependencei

Optimum pH is about 9.0 with L-kynurenine as substrate, and about 8.5 with DL-3-hydroxykynurenine as substrate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei137 – 1371Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei138 – 1381Pyridoxal phosphateUniRule annotation
Binding sitei221 – 2211Pyridoxal phosphateUniRule annotation
Binding sitei250 – 2501Pyridoxal phosphateUniRule annotation
Binding sitei253 – 2531Pyridoxal phosphateUniRule annotation
Binding sitei275 – 2751Pyridoxal phosphateUniRule annotation
Binding sitei305 – 3051Pyridoxal phosphateUniRule annotation
Binding sitei333 – 3331Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. kynureninase activity Source: RGD
  2. pyridoxal phosphate binding Source: RGD

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. response to interferon-gamma Source: Ensembl
  6. response to vitamin B6 Source: Ensembl
  7. tryptophan catabolic process to acetyl-CoA Source: RGD
  8. tryptophan catabolic process to kynurenine Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15007.
ReactomeiREACT_222206. Tryptophan catabolism.
SABIO-RKP70712.
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:Kynu
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi71061. Kynu.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464KynureninasePRO_0000218659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 PublicationUniRule annotation
Modified residuei276 – 2761N6-(pyridoxal phosphate)lysineUniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP70712.

Expressioni

Tissue specificityi

High levels in liver and kidney. Also detected in heart, retina, ovary. Lung, testis and brain.1 Publication

Inductioni

Inhibited by thiol reagents and heavy metal ions.

Gene expression databases

GenevestigatoriP70712.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP70712.
SMRiP70712. Positions 6-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 1684Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
GeneTreeiENSGT00390000008033.
HOGENOMiHOG000242438.
HOVERGENiHBG001170.
InParanoidiP70712.
KOiK01556.
OMAiGWYGGDK.
OrthoDBiEOG7D2FDV.
PhylomeDBiP70712.

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.

P70712-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEPSPLELPV DAVRRIATEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK
60 70 80 90 100
MRDLPSIDLS LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY
110 120 130 140 150
GHEVGKRPWI IGDESIVSLM KDIVGAHEKE IALMNALTVN LHLLLLSFFK
160 170 180 190 200
PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMI KPREGEETLR
210 220 230 240 250
MEDILEVIEK EGDSIAVVLF SGLHFYTGQL FNIPAITQAG HAKGCFVGFD
260 270 280 290 300
LAHAVGNVEL HLHDWDVDFA CWCSYKYLNS GAGGLAGAFI HEKHAHTIKP
310 320 330 340 350
ALVGWFGHEL STRFNMDNKL QLIPGVNGFR ISNPPILLVC SLHASLEIFQ
360 370 380 390 400
QATMTALRRK SILLTGYLEY LLKHYHGGND TENKRPVVNI ITPSRAEERG
410 420 430 440 450
CQLTLTFSIS KKGVFKELEK RGVVCDKREP EGIRVAPVPL YNSFHDVYKF
460
IRLLTAILDS TERN
Length:464
Mass (Da):52,470
Last modified:November 9, 2004 - v2
Checksum:i1490A74EFF7287AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181T → A in AAC53206. (PubMed:9180257)Curated
Sequence conflicti26 – 261D → N AA sequence (PubMed:7578221)Curated
Sequence conflicti118 – 1181S → T in AAC53206. (PubMed:9180257)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U68168 mRNA. Translation: AAC53206.1.
BC078762 mRNA. Translation: AAH78762.1.
PIRiPS0370.
S59898.
T48675.
RefSeqiNP_446354.1. NM_053902.2.
UniGeneiRn.10575.

Genome annotation databases

EnsembliENSRNOT00000043533; ENSRNOP00000050947; ENSRNOG00000029993.
GeneIDi116682.
KEGGirno:116682.
UCSCiRGD:71061. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U68168 mRNA. Translation: AAC53206.1 .
BC078762 mRNA. Translation: AAH78762.1 .
PIRi PS0370.
S59898.
T48675.
RefSeqi NP_446354.1. NM_053902.2.
UniGenei Rn.10575.

3D structure databases

ProteinModelPortali P70712.
SMRi P70712. Positions 6-460.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P70712.
ChEMBLi CHEMBL2969.

Proteomic databases

PRIDEi P70712.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000043533 ; ENSRNOP00000050947 ; ENSRNOG00000029993 .
GeneIDi 116682.
KEGGi rno:116682.
UCSCi RGD:71061. rat.

Organism-specific databases

CTDi 8942.
RGDi 71061. Kynu.

Phylogenomic databases

eggNOGi COG3844.
GeneTreei ENSGT00390000008033.
HOGENOMi HOG000242438.
HOVERGENi HBG001170.
InParanoidi P70712.
KOi K01556.
OMAi GWYGGDK.
OrthoDBi EOG7D2FDV.
PhylomeDBi P70712.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .
BioCyci MetaCyc:MONOMER-15007.
Reactomei REACT_222206. Tryptophan catabolism.
SABIO-RK P70712.

Miscellaneous databases

NextBioi 619528.
PROi P70712.

Gene expression databases

Genevestigatori P70712.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_01970. Kynureninase.
InterProi IPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR14084. PTHR14084. 1 hit.
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF038800. KYNU. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01814. kynureninase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT MET-1.
    Strain: Wistar.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-117, PARTIAL PROTEIN SEQUENCE.
    Tissue: Kidney and Liver.
  5. Matsui Lee I.S., Okuno E., Kido R.
    Submitted (JUN-1992) to the PIR data bank
    Cited for: PROTEIN SEQUENCE OF 83-116 AND 273-319.
    Tissue: Liver.

Entry informationi

Entry nameiKYNU_RAT
AccessioniPrimary (citable) accession number: P70712
Secondary accession number(s): Q68G25, Q7M0D0, Q9QW90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 9, 2004
Last modified: October 29, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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