ID   KAT1_MOUSE              Reviewed;         424 AA.
AC   Q8BTY1; Q8BY27;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Kynurenine--oxoglutarate transaminase 1;
DE            EC=2.6.1.7;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase I;
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;
GN   Name=Ccbl1; Synonyms=Kat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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 (By similarity).
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: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; AK042391; BAC31248.1; -; mRNA.
DR   EMBL; AK088404; BAC40333.1; -; mRNA.
DR   EMBL; BC016206; AAH16206.1; -; mRNA.
DR   EMBL; BC052047; AAH52047.1; -; mRNA.
DR   IPI; IPI00331111; -.
DR   RefSeq; NP_765992.2; -.
DR   UniGene; Mm.216089; -.
DR   HSSP; Q56232; 1BJW.
DR   SMR; Q8BTY1; 4-421.
DR   PRIDE; Q8BTY1; -.
DR   Ensembl; ENSMUSG00000039648; Mus musculus.
DR   GeneID; 70266; -.
DR   KEGG; mmu:70266; -.
DR   MGI; MGI:1917516; Ccbl1.
DR   HOGENOM; Q8BTY1; -.
DR   HOVERGEN; Q8BTY1; -.
DR   BRENDA; 2.6.1.64; 244.
DR   BRENDA; 2.6.1.7; 244.
DR   BRENDA; 4.4.1.13; 244.
DR   NextBio; 331276; -.
DR   ArrayExpress; Q8BTY1; -.
DR   Bgee; Q8BTY1; -.
DR   CleanEx; MM_CCBL1; -.
DR   GermOnline; ENSMUSG00000039648; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; 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   Aminotransferase; Cytoplasm; Lyase; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    424       Kynurenine--oxoglutarate transaminase 1.
FT                                /FTId=PRO_0000123943.
FT   MOD_RES     247    247       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   CONFLICT    390    390       H -> R (in Ref. 1; BAC31248).
SQ   SEQUENCE   424 AA;  47564 MW;  5C1B3FE94534805B CRC64;
     MSKQLQARRL EGIDHNPWVE FTRLSKEYDV VNLGQGFPDF SPPDFAVQAF QQATTGNFML
     NQYTSAFGYP PLTKILASFF GKLLGQEMDP LKNVLVTVGA YGALFTAFQA LVDEGDEVII
     IEPAFNCYEP MTMMAGGRPV FVSLRLSPAP KGQLGSSNDW QLDPTELASK FTPRTKILVL
     NTPNNPLGKV FSKKELELVA ALCQQHDVLC FSDEVYQWLV YDGHQHISIA SLPGMWERTL
     TIGSAGKSFS ATGWKVGWVM GPDNIMKHLR TVHQNSIFHC PTQAQAAVAQ CFEREQQHFG
     QPSSYFLQLP QAMGLNRDHM IQSLQSVGLK PLIPQGSYFL IADISDFKSS MPDLPGAMDE
     PYDTRFAKWM IKNKGLSAIP VSTFYSQPHH KDFDHYIRFC FVKDKATLQA MDKRLCSWKG
     EPQA
//