ID KYNU_RAT STANDARD; PRT; 464 AA. AC P70712; DT 15-DEC-1998 (REL. 37, CREATED) DT 15-DEC-1998 (REL. 37, LAST SEQUENCE UPDATE) DT 15-DEC-1998 (REL. 37, LAST ANNOTATION UPDATE) DE KYNURENINASE (EC 3.7.1.3) (L-KYNURENINE HYDROLASE). OS RATTUS NORVEGICUS (RAT). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC RODENTIA; SCIUROGNATHI; MURIDAE; MURINAE; RATTUS. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=LIVER; RX MEDLINE; 97324088. RA TOMA S., NAKAMURA M., TONE S., OKUNO E., KIDO R., BRETON J., RA AVANZI N., COZZI L., SPECIALE C., MOSTARDINI M., GATTI S., BENATTI L.; RT "Cloning and recombinant expression of rat and human kynureninase."; RL FEBS LETT. 408:5-10(1997). CC -!- FUNCTION: CATALYZES THE CLEAVAGE OF L-KYNURENINE AND L-3- CC HYDROXYKYNURENINE INTO ANTHRANILIC AND 3-HYDROXYANTHRANILIC ACIDS, CC RESPECTIVELY. CC -!- CATALYTIC ACTIVITY: L-KYNURENINE + H(2)O = ANTHRANILATE + CC L-ALANINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: INVOLVED IN THE BIOSYNTHESIS OF NAD COFACTORS FROM CC TRYPTOPHAN THROUGH THE KYNURENINE PATHWAY. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SIMILARITY: BELONGS TO THE KYNURENINASE FAMILY. SLIGHTLY RELATED CC TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U68168; G1532216; -. KW HYDROLASE; PYRIDOXAL PHOSPHATE. FT BINDING 276 276 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 464 AA; 52453 MW; 37EE19F0 CRC32; MEPSPLELPV DAVRRIAAEL NCDPTDERVA LRLDEEDKLK RFKDCFYIPK MRDLPSIDLS LVNEDDNAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIGAY GHEVGKRPWI IGDESIVTLM KDIVGAHEKE IALMNALTVN LHLLLLSFFK PTPKRHKILL EAKAFPSDHY AIESQIQLHG LDVEKSMRMI KPREGEETLR MEDILEVIEK EGDSIAVVLF SGLHFYTGQL FNIPAITQAG HAKGCFVGFD LAHAVGNVEL HLHDWDVDFA CWCSYKYLNS GAGGLAGAFI HEKHAHTIKP ALVGWFGHEL STRFNMDNKL QLIPGVNGFR ISNPPILLVC SLHASLEIFQ QATMTALRRK SILLTGYLEY LLKHYHGGND TENKRPVVNI ITPSRAEERG CQLTLTFSIS KKGVFKELEK RGVVCDKREP EGIRVAPVPL YNSFHDVYKF IRLLTAILDS TERN //