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Reviewed, UniProtKB/Swiss-Prot Q08415 (KAT1_RAT)

Last modified May 26, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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

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Protein attributes

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

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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.

L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine.

RS-CH(2)-CH(NH3+)COO- = RSH + NH3 + pyruvate.

Cofactor

Pyridoxal phosphate.

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Isoform 2: Cytoplasm.

Isoform 1: Mitochondrion matrix.

Sequence similarities

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

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

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

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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.

Checksum: CEE7194633F96AA1
Show »

FASTA42347,873

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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: 8502223] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
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: 7926014] [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: 7796908] [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: 12850267] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).

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Cross-references

Sequence databases

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.
UniGeneRn.110564

3D structure databases

HSSPHSSP built from PDB template 1BJW based on UniProtKB Q56232.
SMRQ08415. Positions 38-453.
ModBaseSearch...

Proteomic databases

PRIDEQ08415.

Genome annotation databases

EnsemblENSRNOG00000016097. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD1306912. Ccbl1.

Phylogenomic databases

HOVERGENQ08415.

Enzyme and pathway databases

BRENDA2.6.1.64. 248.
2.6.1.7. 248.
4.4.1.13. 248.

Gene expression databases

ArrayExpressQ08415.
GermOnlineENSRNOG00000016097. Rattus norvegicus.

Family and domain databases

InterProIPR001176. ACC_synthase.
IPR004839. Aminotrans_I/II.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00753. ACCSYNTHASE.
ProtoNetSearch...

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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: May 26, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents