ID   KAT1_RAT                Reviewed;         457 AA.
AC   Q08415; Q9R096;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   26-MAY-2009, entry version 63.
DE   RecName: Full=Kynurenine--oxoglutarate transaminase 1, mitochondrial;
DE            Short=Kynurenine--oxoglutarate transaminase I;
DE            EC=2.6.1.7;
DE   AltName: Full=Kynurenine aminotransferase I;
DE            Short=KATI;
DE   AltName: Full=Glutamine--phenylpyruvate transaminase;
DE            EC=2.6.1.64;
DE   AltName: Full=Glutamine transaminase K;
DE            Short=GTK;
DE   AltName: Full=Cysteine-S-conjugate beta-lyase;
DE            EC=4.4.1.13;
DE   Flags: Precursor;
GN   Name=Ccbl1; Synonyms=Kat;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC   TISSUE=Kidney;
RX   MEDLINE=93275300; PubMed=8502223;
RA   Perry S.J., Schofield M.A., MacFarlane M., Lock E.A., King L.J.,
RA   Gibson G.G., Goldfarb P.S.;
RT   "Isolation and expression of a cDNA coding for rat kidney cytosolic
RT   cysteine conjugate beta-lyase.";
RL   Mol. Pharmacol. 43:660-665(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=95010756; PubMed=7926014; DOI=10.1016/0014-5793(94)01003-X;
RA   Mosca M., Cozzi L., Breton J., Speciale C., Okuno E., Schwarcz R.,
RA   Benatti L.;
RT   "Molecular cloning of rat kynurenine aminotransferase: identity with
RT   glutamine transaminase K.";
RL   FEBS Lett. 353:21-24(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Cerebellum;
RX   MEDLINE=95317413; PubMed=7796908; DOI=10.1016/0014-5793(95)00546-L;
RA   Malherbe P., Alberati-Giani D., Koehler C., Cesura A.M.;
RT   "Identification of a mitochondrial form of kynurenine
RT   aminotransferase/glutamine transaminase K from rat brain.";
RL   FEBS Lett. 367:141-144(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=12850267; DOI=10.1016/S0167-4781(03)00071-X;
RA   Mosca M., Croci C., Mostardini M., Breton J., Malyszko J., Avanzi N.,
RA   Toma S., Benatti L., Gatti S.;
RT   "Tissue expression and translational control of rat kynurenine
RT   aminotransferase/glutamine transaminase K mRNAs.";
RL   Biochim. Biophys. Acta 1628:1-10(2003).
CC   -!- FUNCTION: Catalyzes the irreversible transamination of the L-
CC       tryptophan metabolite L-kynurenine to form kynurenic acid (KA).
CC       Metabolizes the cysteine conjugates of certain halogenated alkenes
CC       and alkanes to form reactive metabolites. Catalyzes the beta-
CC       elimination of S-conjugates and Se-conjugates of L-
CC       (seleno)cysteine, resulting in the cleavage of the C-S or C-Se
CC       bond (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2-
CC       aminophenyl)-2,4-dioxobutanoate + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: L-glutamine + phenylpyruvate = 2-
CC       oxoglutaramate + L-phenylalanine.
CC   -!- CATALYTIC ACTIVITY: RS-CH(2)-CH(NH(3)(+))COO(-) = RSH + NH(3) +
CC       pyruvate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation;
CC       kynurenic acid from L-kynurenine: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q08415-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08415-2; Sequence=VSP_009878;
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S61960; AAB26845.1; -; mRNA.
DR   EMBL; S74029; AAB32197.1; -; mRNA.
DR   EMBL; Z49696; CAA89696.1; -; mRNA.
DR   EMBL; AF100154; AAF06837.1; -; Genomic_DNA.
DR   EMBL; AF267749; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00411232; -.
DR   IPI; IPI00411233; -.
DR   PIR; S66270; S66270.
DR   UniGene; Rn.110564; -.
DR   HSSP; Q56232; 1BJW.
DR   SMR; Q08415; 38-453.
DR   PRIDE; Q08415; -.
DR   Ensembl; ENSRNOG00000016097; Rattus norvegicus.
DR   RGD; 1306912; Ccbl1.
DR   HOVERGEN; Q08415; -.
DR   BRENDA; 2.6.1.64; 248.
DR   BRENDA; 2.6.1.7; 248.
DR   BRENDA; 4.4.1.13; 248.
DR   ArrayExpress; Q08415; -.
DR   GermOnline; ENSRNOG00000016097; Rattus norvegicus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase ...; IEA:InterPro.
DR   GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:EC.
DR   GO; GO:0047316; F:glutamine-phenylpyruvate transaminase activity; IEA:EC.
DR   GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001176; ACC_synthase.
DR   InterPro; IPR004839; Aminotrans_I/II.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Aminotransferase; Cytoplasm; Lyase;
KW   Mitochondrion; Pyridoxal phosphate; Transferase; Transit peptide.
FT   TRANSIT       1     28       Mitochondrion (Potential).
FT   CHAIN        29    457       Kynurenine--oxoglutarate transaminase 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001221.
FT   MOD_RES     281    281       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   VAR_SEQ       1     34       Missing (in isoform 2).
FT                                /FTId=VSP_009878.
FT   CONFLICT    141    141       R -> A (in Ref. 2 and 4).
FT   CONFLICT    211    211       I -> V (in Ref. 2; AAB32197).
SQ   SEQUENCE   457 AA;  51652 MW;  E792A6BA2EA08502 CRC64;
     MFRSAAALSV HLMWPLWGRK AGASLTRCLH QSLTMTKRLQ ARRLDGIDQN LWVEFGKLTK
     EYDVVNLGQG FPDFSPPDFA TQAFQQATSG NFMLNQYTRA FGYPPLTNVL ASFFGKLLGQ
     EMDPLTNVLV TVGAYGALFT RFQALVDEGD EVIIMEPAFD CYEPMTMMAG GCPVFVTLKP
     SPAPKGKLGA SNDWQLDPAE LASKFTPRTK ILVLNTPNNP LGKVFSRMEL ELVANLCQQH
     DVVCISDEVY QWLVYDGHQH VSIASLPGMW DRTLTIGSAG KSFSATGWKV GWVMGPDNIM
     KHLRTVHQNS IFHCPTQAQA AVAQCFEREQ QHFGQPSSYF LQLPQAMELN RDHMIRSLQS
     VGLKLWISQG SYFLIADISD FKSKMPDLPG AEDEPYDRRF AKWMIKNMGL VGIPVSTFFS
     RPHQKDFDHY IRFCFVKDKA TLQAMDERLR KWKELQP
//