KAT1_MOUSE
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 03-AUG-2022, entry version 149.
DE RecName: Full=Kynurenine--oxoglutarate transaminase 1 {ECO:0000250|UniProtKB:Q16773};
DE EC=2.6.1.7 {ECO:0000250|UniProtKB:Q16773};
DE AltName: Full=Cysteine-S-conjugate beta-lyase {ECO:0000250|UniProtKB:Q16773};
DE EC=4.4.1.13 {ECO:0000250|UniProtKB:Q16773};
DE AltName: Full=Glutamine transaminase K;
DE Short=GTK;
DE AltName: Full=Glutamine--phenylpyruvate transaminase {ECO:0000250|UniProtKB:Q16773};
DE EC=2.6.1.64 {ECO:0000250|UniProtKB:Q16773};
DE AltName: Full=Kynurenine aminotransferase 1;
DE AltName: Full=Kynurenine aminotransferase I;
DE Short=KATI;
DE AltName: Full=Kynurenine--oxoglutarate transaminase I;
GN Name=Kyat1; Synonyms=Ccbl1, Kat;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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/6J, 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-82 AND LYS-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in
CC the tryptophan catabolic pathway which is also a broad spectrum
CC antagonist of the three ionotropic excitatory amino acid receptors
CC among others. Metabolizes the cysteine conjugates of certain
CC halogenated alkenes and alkanes to form reactive metabolites. Catalyzes
CC the beta-elimination of S-conjugates and Se-conjugates of L-
CC (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.
CC {ECO:0000250|UniProtKB:Q16773}.
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 Evidence={ECO:0000250|UniProtKB:Q16773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000250|UniProtKB:Q16773};
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 Evidence={ECO:0000250|UniProtKB:Q16773};
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 Evidence={ECO:0000250|UniProtKB:Q16773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC Evidence={ECO:0000250|UniProtKB:Q16773};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q16773};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16773}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q16773}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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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 CCDS; CCDS15874.1; -.
DR RefSeq; NP_765992.2; NM_172404.2.
DR RefSeq; XP_006498377.2; XM_006498314.2.
DR AlphaFoldDB; Q8BTY1; -.
DR SMR; Q8BTY1; -.
DR STRING; 10090.ENSMUSP00000109291; -.
DR iPTMnet; Q8BTY1; -.
DR PhosphoSitePlus; Q8BTY1; -.
DR EPD; Q8BTY1; -.
DR jPOST; Q8BTY1; -.
DR MaxQB; Q8BTY1; -.
DR PaxDb; Q8BTY1; -.
DR PRIDE; Q8BTY1; -.
DR ProteomicsDB; 301731; -.
DR DNASU; 70266; -.
DR Ensembl; ENSMUST00000044038; ENSMUSP00000038612; ENSMUSG00000039648.
DR Ensembl; ENSMUST00000113661; ENSMUSP00000109291; ENSMUSG00000039648.
DR Ensembl; ENSMUST00000113662; ENSMUSP00000109292; ENSMUSG00000039648.
DR Ensembl; ENSMUST00000113663; ENSMUSP00000109293; ENSMUSG00000039648.
DR GeneID; 70266; -.
DR KEGG; mmu:70266; -.
DR UCSC; uc008jbo.1; mouse.
DR CTD; 883; -.
DR MGI; MGI:1917516; Kyat1.
DR VEuPathDB; HostDB:ENSMUSG00000039648; -.
DR eggNOG; KOG0257; Eukaryota.
DR GeneTree; ENSGT00940000158797; -.
DR InParanoid; Q8BTY1; -.
DR OMA; SQGANQY; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q8BTY1; -.
DR TreeFam; TF105482; -.
DR BRENDA; 2.6.1.7; 3474.
DR Reactome; R-MMU-71240; Tryptophan catabolism.
DR Reactome; R-MMU-8964208; Phenylalanine metabolism.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00334; UER00726.
DR BioGRID-ORCS; 70266; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8BTY1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BTY1; protein.
DR Bgee; ENSMUSG00000039648; Expressed in esophagus and 251 other tissues.
DR ExpressionAtlas; Q8BTY1; baseline and differential.
DR Genevisible; Q8BTY1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; ISO:MGI.
DR GO; GO:0047316; F:glutamine-phenylpyruvate transaminase activity; ISO:MGI.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006575; P:cellular modified amino acid metabolic process; IEA:InterPro.
DR GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0097052; P:L-kynurenine metabolic process; ISO:MGI.
DR GO; GO:0006090; P:pyruvate metabolic process; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR034614; KAT_I.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807:SF14; PTHR43807:SF14; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Lyase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..424
FT /note="Kynurenine--oxoglutarate transaminase 1"
FT /id="PRO_0000123943"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT MOD_RES 82
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT MOD_RES 413
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 390
FT /note="H -> R (in Ref. 1; BAC31248)"
FT /evidence="ECO:0000305"
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
