ID KAT3_MOUSE Reviewed; 455 AA. AC Q71RI9; Q8BJ84; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 14-OCT-2015, entry version 101. DE RecName: Full=Kynurenine--oxoglutarate transaminase 3; DE EC=2.6.1.7; DE AltName: Full=Cysteine-S-conjugate beta-lyase 2; DE EC=4.4.1.13; DE AltName: Full=Kynurenine aminotransferase III; DE Short=KATIII; DE AltName: Full=Kynurenine--glyoxylate transaminase; DE EC=2.6.1.63; DE AltName: Full=Kynurenine--oxoglutarate transaminase III; GN Name=Ccbl2; Synonyms=Kat3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=16376499; DOI=10.1016/j.gene.2005.09.034; RA Yu P., Li Z., Zhang L., Tagle D.A., Cai T.; RT "Characterization of kynurenine aminotransferase III, a novel member RT of a phylogenetically conserved KAT family."; RL Gene 365:111-118(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen, 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 RT expression."; RL Cell 143:1174-1189(2010). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY RP 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., RA Zhang Y., 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). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 42-451 IN COMPLEXES WITH RP KYNURENINE AND GLUTAMINE, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, AND RP COFACTOR. RX PubMed=19029248; DOI=10.1128/MCB.01272-08; RA Han Q., Robinson H., Cai T., Tagle D.A., Li J.; RT "Biochemical and structural properties of mouse kynurenine RT aminotransferase III."; RL Mol. Cell. Biol. 29:784-793(2009). 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). Has transaminase activity CC towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, CC methionine, histidine, glutamine and asparagine with glyoxylate as CC an amino group acceptor (in vitro). Has lower activity with 2- CC oxoglutarate as amino group acceptor (in vitro). {ECO:0000250, CC ECO:0000269|PubMed:19029248}. CC -!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2- CC aminophenyl)-2,4-dioxobutanoate + L-glutamate. CC {ECO:0000269|PubMed:19029248}. CC -!- CATALYTIC ACTIVITY: An L-cysteine-S-conjugate + H(2)O = RSH + CC NH(3) + pyruvate. {ECO:0000269|PubMed:19029248}. CC -!- CATALYTIC ACTIVITY: L-kynurenine + glyoxylate = 4-(2-aminophenyl)- CC 2,4-dioxobutanoate + glycine. {ECO:0000269|PubMed:19029248}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:19029248}; CC -!- ENZYME REGULATION: Kynurenine transamination is competitively CC inhibited by cysteine, glutamine, histidine, methionine, leucine, CC or phenylalanine. {ECO:0000269|PubMed:19029248}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.7 mM for glutamine {ECO:0000269|PubMed:19029248}; CC KM=0.7 mM for histidine {ECO:0000269|PubMed:19029248}; CC KM=0.7 mM for cysteine {ECO:0000269|PubMed:19029248}; CC KM=0.9 mM for methionine {ECO:0000269|PubMed:19029248}; CC KM=1.1 mM for phenylalanine {ECO:0000269|PubMed:19029248}; CC KM=1.4 mM for asparagine {ECO:0000269|PubMed:19029248}; CC KM=1.5 mM for kynurenine {ECO:0000269|PubMed:19029248}; CC KM=7.1 mM for tryptophan {ECO:0000269|PubMed:19029248}; CC KM=3.0 mM for serine {ECO:0000269|PubMed:19029248}; CC KM=0.4 mM for glyoxylate {ECO:0000269|PubMed:19029248}; CC KM=0.6 mM for phenylpyruvate {ECO:0000269|PubMed:19029248}; CC pH dependence: CC Optimum pH is 9. {ECO:0000269|PubMed:19029248}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. CC {ECO:0000269|PubMed:19029248}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19029248}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q71RI9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q71RI9-2; Sequence=VSP_025605; CC -!- TISSUE SPECIFICITY: Widely expressed, with higher expression CC levels in liver, kidney, heart and neuroendocrine tissues. CC {ECO:0000269|PubMed:16376499}. CC -!- DEVELOPMENTAL STAGE: Expressed from postnatal day (PND) 7 and CC peaks in adult. {ECO:0000269|PubMed:16376499}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. 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; AF363737; AAQ15190.1; -; mRNA. DR EMBL; AK049569; BAC33817.1; -; mRNA. DR EMBL; AK145623; BAE26546.1; -; mRNA. DR EMBL; BC131942; AAI31943.1; -; mRNA. DR EMBL; BC132615; AAI32616.1; -; mRNA. DR CCDS; CCDS17881.1; -. [Q71RI9-2] DR CCDS; CCDS80040.1; -. [Q71RI9-1] DR RefSeq; NP_001280489.1; NM_001293560.1. [Q71RI9-1] DR RefSeq; NP_776124.1; NM_173763.4. [Q71RI9-2] DR RefSeq; XP_006501494.1; XM_006501431.2. [Q71RI9-2] DR RefSeq; XP_011238416.1; XM_011240114.1. [Q71RI9-2] DR UniGene; Mm.289643; -. DR PDB; 2ZJG; X-ray; 3.00 A; A/B=42-451. DR PDB; 3E2F; X-ray; 2.59 A; A/B=42-451. DR PDB; 3E2Y; X-ray; 2.26 A; A/B=42-451. DR PDB; 3E2Z; X-ray; 2.81 A; A/B=42-451. DR PDBsum; 2ZJG; -. DR PDBsum; 3E2F; -. DR PDBsum; 3E2Y; -. DR PDBsum; 3E2Z; -. DR ProteinModelPortal; Q71RI9; -. DR SMR; Q71RI9; 42-451. DR IntAct; Q71RI9; 3. DR MINT; MINT-1854868; -. DR STRING; 10090.ENSMUSP00000041675; -. DR PhosphoSite; Q71RI9; -. DR MaxQB; Q71RI9; -. DR PaxDb; Q71RI9; -. DR PRIDE; Q71RI9; -. DR Ensembl; ENSMUST00000044392; ENSMUSP00000041675; ENSMUSG00000040213. [Q71RI9-2] DR Ensembl; ENSMUST00000106218; ENSMUSP00000101825; ENSMUSG00000040213. [Q71RI9-1] DR GeneID; 229905; -. DR KEGG; mmu:229905; -. DR UCSC; uc008roz.2; mouse. [Q71RI9-1] DR CTD; 56267; -. DR MGI; MGI:2677849; Ccbl2. DR eggNOG; COG0436; -. DR GeneTree; ENSGT00650000093238; -. DR HOGENOM; HOG000223045; -. DR HOVERGEN; HBG008391; -. DR InParanoid; Q71RI9; -. DR KO; K00816; -. DR OMA; KQPIVNM; -. DR OrthoDB; EOG76DTSB; -. DR TreeFam; TF352342; -. DR BRENDA; 2.6.1.7; 3474. DR Reactome; R-MMU-71240; Tryptophan catabolism. DR NextBio; 379731; -. DR PRO; PR:Q71RI9; -. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; Q71RI9; -. DR CleanEx; MM_CCBL2; -. DR ExpressionAtlas; Q71RI9; baseline and differential. DR Genevisible; Q71RI9; MM. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; IDA:UniProtKB. DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB. DR GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB. DR GO; GO:0097052; P:L-kynurenine metabolic process; IDA:GOC. 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_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase; KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 455 Kynurenine--oxoglutarate transaminase 3. FT /FTId=PRO_0000287705. FT BINDING 54 54 Substrate. FT BINDING 72 72 Substrate; via amide nitrogen. FT BINDING 219 219 Substrate. FT BINDING 430 430 Substrate. FT MOD_RES 117 117 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 117 117 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 281 281 N6-(pyridoxal phosphate)lysine. FT VAR_SEQ 1 35 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_025605. FT HELIX 44 46 {ECO:0000244|PDB:3E2Y}. FT HELIX 53 56 {ECO:0000244|PDB:3E2Y}. FT HELIX 57 62 {ECO:0000244|PDB:3E2Z}. FT STRAND 66 68 {ECO:0000244|PDB:3E2Y}. FT STRAND 70 72 {ECO:0000244|PDB:3E2F}. FT HELIX 80 90 {ECO:0000244|PDB:3E2Y}. FT HELIX 93 96 {ECO:0000244|PDB:3E2Y}. FT HELIX 105 119 {ECO:0000244|PDB:3E2Y}. FT TURN 125 127 {ECO:0000244|PDB:3E2Y}. FT STRAND 128 133 {ECO:0000244|PDB:3E2Y}. FT HELIX 134 146 {ECO:0000244|PDB:3E2Y}. FT STRAND 152 158 {ECO:0000244|PDB:3E2Y}. FT HELIX 163 169 {ECO:0000244|PDB:3E2Y}. FT STRAND 173 178 {ECO:0000244|PDB:3E2Y}. FT HELIX 191 193 {ECO:0000244|PDB:3E2Y}. FT HELIX 198 202 {ECO:0000244|PDB:3E2Y}. FT STRAND 209 217 {ECO:0000244|PDB:3E2Y}. FT TURN 219 221 {ECO:0000244|PDB:3E2Y}. FT HELIX 227 240 {ECO:0000244|PDB:3E2Y}. FT STRAND 243 247 {ECO:0000244|PDB:3E2Y}. FT TURN 249 252 {ECO:0000244|PDB:3E2Y}. FT HELIX 263 265 {ECO:0000244|PDB:3E2Y}. FT TURN 267 269 {ECO:0000244|PDB:3E2Z}. FT HELIX 270 272 {ECO:0000244|PDB:3E2Y}. FT STRAND 273 278 {ECO:0000244|PDB:3E2Y}. FT HELIX 279 282 {ECO:0000244|PDB:3E2Y}. FT HELIX 286 288 {ECO:0000244|PDB:3E2Y}. FT STRAND 291 294 {ECO:0000244|PDB:3E2Y}. FT HELIX 297 308 {ECO:0000244|PDB:3E2Y}. FT TURN 309 311 {ECO:0000244|PDB:3E2Y}. FT HELIX 316 330 {ECO:0000244|PDB:3E2Y}. FT TURN 331 334 {ECO:0000244|PDB:3E2Y}. FT STRAND 335 338 {ECO:0000244|PDB:2ZJG}. FT HELIX 339 359 {ECO:0000244|PDB:3E2Y}. FT TURN 360 362 {ECO:0000244|PDB:3E2Y}. FT STRAND 364 367 {ECO:0000244|PDB:3E2Y}. FT STRAND 369 377 {ECO:0000244|PDB:3E2Y}. FT HELIX 379 381 {ECO:0000244|PDB:3E2Y}. FT HELIX 394 406 {ECO:0000244|PDB:3E2Y}. FT STRAND 407 409 {ECO:0000244|PDB:3E2Y}. FT HELIX 413 416 {ECO:0000244|PDB:3E2Y}. FT TURN 419 421 {ECO:0000244|PDB:3E2Y}. FT HELIX 422 425 {ECO:0000244|PDB:3E2Y}. FT STRAND 428 432 {ECO:0000244|PDB:3E2Y}. FT HELIX 437 448 {ECO:0000244|PDB:3E2Y}. SQ SEQUENCE 455 AA; 51126 MW; 94FA35EC67121EF2 CRC64; MLLAQRRLIS LGCRSKPIKT IYSSSKVLGL CTSAKMALKF KNAKRIEGLD SNVWVEFTKL AADPSVVNLG QGFPDISPPS YVKEELSKAA FIDNMNQYTR GFGHPALVKA LSCLYGKIYQ RQIDPNEEIL VAVGAYGSLF NSIQGLVDPG DEVIIMVPFY DCYEPMVRMA GAVPVFIPLR SKPTDGMKWT SSDWTFDPRE LESKFSSKTK AIILNTPHNP LGKVYTRQEL QVIADLCVKH DTLCISDEVY EWLVYTGHTH VKIATLPGMW ERTITIGSAG KTFSVTGWKL GWSIGPAHLI KHLQTVQQNS FYTCATPLQA ALAEAFWIDI KRMDDPECYF NSLPKELEVK RDRMVRLLNS VGLKPIVPDG GYFIIADVSS LGADLSDMNS DEPYDYKFVK WMTKHKKLTA IPVSAFCDSK SKPHFEKLVR FCFIKKDSTL DAAEEIFRAW NSQKS //