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Q08415 (KAT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynurenine--oxoglutarate transaminase 1, mitochondrial
Short name=Kynurenine--oxoglutarate transaminase I
EC=2.6.1.7
Alternative name(s):
Cysteine-S-conjugate beta-lyase
EC=4.4.1.13
Glutamine transaminase K
Short name=GTK
Glutamine--phenylpyruvate transaminase
EC=2.6.1.64
Kynurenine aminotransferase I
Short name=KATI
Gene names
Name:Ccbl1
Synonyms:Kat
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond By similarity.

Catalytic activity

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. Ref.5 Ref.6

L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. Ref.5 Ref.6

RS-CH(2)-CH(NH3+)COO- + H2O = RSH + NH3 + pyruvate. Ref.5 Ref.6

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Inhibited by aminooxyacetate (in vitro). Ref.6

Pathway

Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2.

Subunit structure

Homodimer. Ref.5

Subcellular location

Isoform 2: Cytoplasm.

Isoform 1: Mitochondrion matrix.

Tissue specificity

Detected in kidney. Ref.1

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=17 µM for L-kynurenine (with 2-oxoglutarate as cosubstrate) Ref.6

KM=910 µM for L-kynurenine (with pyruvate as cosubstrate)

KM=150 µM for 2-oxoglutarate

KM=160 µM for pyruvate

pH dependence:

Optimum pH is 9-9.5.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08415-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q08415-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 457429Kynurenine--oxoglutarate transaminase 1, mitochondrial
PRO_0000001221

Sites

Binding site701Substrate; via amide nitrogen By similarity
Binding site2191Substrate By similarity
Binding site4321Substrate By similarity

Amino acid modifications

Modified residue2811N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence1 – 3434Missing in isoform 2.
VSP_009878

Experimental info

Sequence conflict1411R → A in AAB32197. Ref.2
Sequence conflict1411R → A in AAF06837. Ref.4
Sequence conflict2111I → V in AAB32197. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E792A6BA2EA08502

FASTA45751,652
        10         20         30         40         50         60 
MFRSAAALSV HLMWPLWGRK AGASLTRCLH QSLTMTKRLQ ARRLDGIDQN LWVEFGKLTK 

        70         80         90        100        110        120 
EYDVVNLGQG FPDFSPPDFA TQAFQQATSG NFMLNQYTRA FGYPPLTNVL ASFFGKLLGQ 

       130        140        150        160        170        180 
EMDPLTNVLV TVGAYGALFT RFQALVDEGD EVIIMEPAFD CYEPMTMMAG GCPVFVTLKP 

       190        200        210        220        230        240 
SPAPKGKLGA SNDWQLDPAE LASKFTPRTK ILVLNTPNNP LGKVFSRMEL ELVANLCQQH 

       250        260        270        280        290        300 
DVVCISDEVY QWLVYDGHQH VSIASLPGMW DRTLTIGSAG KSFSATGWKV GWVMGPDNIM 

       310        320        330        340        350        360 
KHLRTVHQNS IFHCPTQAQA AVAQCFEREQ QHFGQPSSYF LQLPQAMELN RDHMIRSLQS 

       370        380        390        400        410        420 
VGLKLWISQG SYFLIADISD FKSKMPDLPG AEDEPYDRRF AKWMIKNMGL VGIPVSTFFS 

       430        440        450 
RPHQKDFDHY IRFCFVKDKA TLQAMDERLR KWKELQP

« Hide

Isoform 2 [UniParc].

Checksum: CEE7194633F96AA1
Show »

FASTA42347,873

References

[1]"Isolation and expression of a cDNA coding for rat kidney cytosolic cysteine conjugate beta-lyase."
Perry S.J., Schofield M.A., MacFarlane M., Lock E.A., King L.J., Gibson G.G., Goldfarb P.S.
Mol. Pharmacol. 43:660-665(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 39-62; 228-259 AND 388-401, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"Molecular cloning of rat kynurenine aminotransferase: identity with glutamine transaminase K."
Mosca M., Cozzi L., Breton J., Speciale C., Okuno E., Schwarcz R., Benatti L.
FEBS Lett. 353:21-24(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Identification of a mitochondrial form of kynurenine aminotransferase/glutamine transaminase K from rat brain."
Malherbe P., Alberati-Giani D., Koehler C., Cesura A.M.
FEBS Lett. 367:141-144(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cerebellum.
[4]"Tissue expression and translational control of rat kynurenine aminotransferase/glutamine transaminase K mRNAs."
Mosca M., Croci C., Mostardini M., Breton J., Malyszko J., Avanzi N., Toma S., Benatti L., Gatti S.
Biochim. Biophys. Acta 1628:1-10(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[5]"Crystallization and characterization of human liver kynurenine--glyoxylate aminotransferase. Identity with alanine--glyoxylate aminotransferase and serine--pyruvate aminotransferase."
Okuno E., Minatogawa Y., Nakamura M., Kamoda N., Nakanishi J., Makino M., Kido R.
Biochem. J. 189:581-590(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, PH DEPENDENCE.
[6]"Measurement of rat brain kynurenine aminotransferase at physiological kynurenine concentrations."
Okuno E., Schmidt W., Parks D.A., Nakamura M., Schwarcz R.
J. Neurochem. 57:533-540(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY AS KYNURENINE--OXOGLUTARATE TRANSAMINASE, KINETIC PARAMETERS, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S61960 mRNA. Translation: AAB26845.1.
S74029 mRNA. Translation: AAB32197.1.
Z49696 mRNA. Translation: CAA89696.1.
AF100154 Genomic DNA. Translation: AAF06837.1.
AF267749 mRNA. No translation available.
IPIIPI00411232.
IPI00411233.
PIRS66270.
RefSeqNP_001013182.3. NM_001013164.3.
UniGeneRn.110564.

3D structure databases

ProteinModelPortalQ08415.
SMRQ08415. Positions 38-453.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021865.

PTM databases

PhosphoSiteQ08415.

Proteomic databases

PaxDbQ08415.
PRIDEQ08415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID311844.
KEGGrno:311844.
UCSCRGD:1306912. rat.

Organism-specific databases

CTD883.
RGD1306912. Ccbl1.

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223045.
HOVERGENHBG008391.
InParanoidQ08415.
KOK00816.
OrthoDBEOG44QT0Z.

Enzyme and pathway databases

BRENDA2.6.1.7. 5301.
UniPathwayUPA00334; UER00726.

Gene expression databases

ArrayExpressQ08415.
GenevestigatorQ08415.
GermOnlineENSRNOG00000016097. Rattus norvegicus.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNetSearch...

Other

NextBio664289.

Entry information

Entry nameKAT1_RAT
AccessionPrimary (citable) accession number: Q08415
Secondary accession number(s): Q9R096
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents