ID   KAT3_BOVIN              Reviewed;         455 AA.
AC   Q0P5G4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Kynurenine--oxoglutarate transaminase 3;
DE            EC=2.6.1.7;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase III;
DE   AltName: Full=Kynurenine aminotransferase III;
DE            Short=KATIII;
DE   AltName: Full=Cysteine-S-conjugate beta-lyase 2;
DE            EC=4.4.1.13;
GN   Name=CCBL2; Synonyms=KAT3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the irreversible transamination of the L-
CC       tryptophan metabolite L-kynurenine to form kynurenic acid (KA).
CC       May catalyze the beta-elimination of S-conjugates and Se-
CC       conjugates of L-(seleno)cysteine, resulting in the cleavage of the
CC       C-S or C-Se bond (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2-
CC       aminophenyl)-2,4-dioxobutanoate + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: RS-CH(2)-CH(NH(3)(+))COO(-) = RSH + NH(3) +
CC       pyruvate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; BC120067; AAI20068.1; -; mRNA.
DR   IPI; IPI00700507; -.
DR   RefSeq; NP_001068838.1; -.
DR   UniGene; Bt.40115; -.
DR   Ensembl; ENSBTAG00000000505; Bos taurus.
DR   GeneID; 508712; -.
DR   KEGG; bta:508712; -.
DR   HOVERGEN; Q0P5G4; -.
DR   OMA; Q0P5G4; LYEKFYQ.
DR   BRENDA; 2.6.1.7; 251.
DR   BRENDA; 4.4.1.13; 251.
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: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; Lyase; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    455       Kynurenine--oxoglutarate transaminase 3.
FT                                /FTId=PRO_0000287703.
FT   MOD_RES     280    280       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   455 AA;  51472 MW;  E353F80DCD854BD6 CRC64;
     MFLAWERLCT LSCRPKFLKT VWASKILGLS TSAKMSLRFK NAKRIEGLDS NIWIEFTKLA
     ADPSVVNLGQ GLPDISPPVY VKEELSKIAA IDNLNQYTRG FGHPSLVKAL SCLYEKFYHN
     KINPNEEILV TVGAYGSLFN AIQGLIDEGD EVIVIVPFFD CYESMVRMAG ATPVFVPLRC
     KPVDGKKCSS SDWTLDPQEL ASKFNSKTKA IILNTPHNPL GKVYTKEELQ VIADLCIKYD
     TLCISDEVYE WLVYTGNKHF KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPKHLIK
     HLQTVQQNTV YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR DRMVHLLESV
     GLKSIVPDGG YFIIADVSLL DVDLLDMKDS NEPYDYKFVK WMIKNKKLSA IPVSAFCNAE
     TKSQFEKFVR FCFIKKDSTL DAAEEIIKAW SRQNS
//