KAT_DICDI
ID KAT_DICDI Reviewed; 435 AA.
AC Q54KM6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Kynurenine--oxoglutarate transaminase;
DE EC=2.6.1.7;
DE AltName: Full=Glutamine transaminase K;
DE EC=4.4.1.13;
DE AltName: Full=Glutamine--phenylpyruvate transaminase;
DE EC=2.6.1.64;
DE AltName: Full=Kynurenine aminotransferase;
GN Name=ccbl; Synonyms=kat; ORFNames=DDB_G0287269;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the
CC cysteine conjugates of certain halogenated alkenes and alkanes to form
CC reactive metabolites. Catalyzes the beta-elimination of S-conjugates
CC and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of
CC the C-S or C-Se bond (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate + L-glutamine = 2-oxoglutaramate + L-
CC phenylalanine; Xref=Rhea:RHEA:17593, ChEBI:CHEBI:16769,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:58359; EC=2.6.1.64;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AAFI02000099; EAL63836.1; -; Genomic_DNA.
DR RefSeq; XP_637331.1; XM_632239.1.
DR AlphaFoldDB; Q54KM6; -.
DR SMR; Q54KM6; -.
DR STRING; 44689.DDB0231138; -.
DR PaxDb; Q54KM6; -.
DR EnsemblProtists; EAL63836; EAL63836; DDB_G0287269.
DR GeneID; 8626029; -.
DR KEGG; ddi:DDB_G0287269; -.
DR dictyBase; DDB_G0287269; ccbl.
DR eggNOG; KOG0257; Eukaryota.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; Q54KM6; -.
DR OMA; SVAMTGW; -.
DR PhylomeDB; Q54KM6; -.
DR Reactome; R-DDI-71240; Tryptophan catabolism.
DR Reactome; R-DDI-8964208; Phenylalanine metabolism.
DR Reactome; R-DDI-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00334; UER00726.
DR PRO; PR:Q54KM6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0047316; F:glutamine-phenylpyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; ISS:dictyBase.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Lyase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..435
FT /note="Kynurenine--oxoglutarate transaminase"
FT /id="PRO_0000327725"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 413
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 262
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 435 AA; 48553 MW; 5E86530007DCB3F1 CRC64;
MLRNTVKRLM TYTFKPSKQT SSFGPSVWLE FSPLAIKYNA VNLGQGFPNF EPPKFVKDAM
IKTIEVGGFN QYTRSPGHIR LVKALSSVYS PYFGRELNAM TEIMVGVGAS ESLFAAISSI
VNEGDEVILI EPFFDIYIGP ILMAGGIPKF VTLKEEESSQ AGSSDKKRSS KHWKINKEEL
AAAFTDKTKL IILNNPHNPV GKVYSKEELQ EIADVVAKHG PNTTVISDEV YEWMTFDGEE
HHRFATLPGM WERTITIGSA GKTFSITGWK VGWCIGPSNI IGAIANTHQY VPFSVPTPTQ
EAVAIALEQP NIKDYFKELA TMYQNKRDTL LNSLTQAGLD PVIPQGTYFI MGDTSSIHLQ
GDQGKDTSIT GMGLHLRDWN IARYLTTEYG VTTIPPSAFY CDDHQKIPEN FVRFTFCKDD
LTLQKAHDNL LKLKK
