ID KAT3_HUMAN Reviewed; 454 AA. AC Q6YP21; B3KQ13; O95335; Q5JS27; Q5T9T7; Q5T9T8; Q6AI27; Q6ICW1; AC Q9BVY5; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 09-DEC-2015, entry version 106. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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] (ISOFORM 2). RC TISSUE=Fetal kidney; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Stomach; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-454 (ISOFORM 1). RC TISSUE=Placenta; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-454, AND VARIANT RP PRO-206. RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.; RT "Full-insert sequence of mapped XREF EST."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-338, AND VARIANT RP PRO-206. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 3), CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). 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) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2- CC aminophenyl)-2,4-dioxobutanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: An L-cysteine-S-conjugate + H(2)O = RSH + CC NH(3) + pyruvate. CC -!- CATALYTIC ACTIVITY: L-kynurenine + glyoxylate = 4-(2-aminophenyl)- CC 2,4-dioxobutanoate + glycine. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6YP21-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6YP21-2; Sequence=VSP_025603, VSP_025604; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=Q6YP21-3; Sequence=VSP_042841; CC Note=Initiator Met-1 is removed. Contains a N-acetylserine at CC position 2. {ECO:0000244|PubMed:22814378}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC -!- CAUTION: The first non-coding exon of CCBL2 is in common with that CC of RBMXL1. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC72959.1; Type=Frameshift; Positions=336; Evidence={ECO:0000305}; CC Sequence=AAH00819.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=CAG29278.1; Type=Frameshift; Positions=336; Evidence={ECO:0000305}; CC Sequence=CAI21695.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI21696.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI41339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI41340.1; Type=Erroneous gene model prediction; Evidence={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; AY028624; AAK26163.1; -; mRNA. DR EMBL; CR627392; CAH10487.1; -; mRNA. DR EMBL; AK057176; BAG51875.1; -; mRNA. DR EMBL; AL445991; CAI41345.1; -; Genomic_DNA. DR EMBL; AL139416; CAI21695.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL445991; CAI21695.1; JOINED; Genomic_DNA. DR EMBL; AL445991; CAI41339.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL139416; CAI41339.1; JOINED; Genomic_DNA. DR EMBL; AL139416; CAI21696.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL445991; CAI21696.1; JOINED; Genomic_DNA. DR EMBL; AL445991; CAI41340.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL139416; CAI41340.1; JOINED; Genomic_DNA. DR EMBL; BC000819; AAH00819.1; ALT_INIT; mRNA. DR EMBL; AF091090; AAC72959.1; ALT_FRAME; mRNA. DR EMBL; CR450282; CAG29278.1; ALT_FRAME; mRNA. DR CCDS; CCDS30766.1; -. [Q6YP21-1] DR CCDS; CCDS30767.1; -. [Q6YP21-3] DR RefSeq; NP_001008661.1; NM_001008661.2. [Q6YP21-1] DR RefSeq; NP_001008662.1; NM_001008662.2. [Q6YP21-3] DR UniGene; Hs.481898; -. DR ProteinModelPortal; Q6YP21; -. DR SMR; Q6YP21; 41-450. DR BioGrid; 121128; 13. DR IntAct; Q6YP21; 6. DR MINT; MINT-1402454; -. DR STRING; 9606.ENSP00000260508; -. DR BindingDB; Q6YP21; -. DR ChEMBL; CHEMBL2046260; -. DR PhosphoSite; Q6YP21; -. DR BioMuta; CCBL2; -. DR DMDM; 74710502; -. DR MaxQB; Q6YP21; -. DR PaxDb; Q6YP21; -. DR PRIDE; Q6YP21; -. DR Ensembl; ENST00000260508; ENSP00000260508; ENSG00000137944. [Q6YP21-1] DR Ensembl; ENST00000370491; ENSP00000359522; ENSG00000137944. [Q6YP21-3] DR GeneID; 56267; -. DR KEGG; hsa:56267; -. DR UCSC; uc001dmp.2; human. [Q6YP21-1] DR CTD; 56267; -. DR GeneCards; CCBL2; -. DR HGNC; HGNC:33238; CCBL2. DR HPA; HPA026538; -. DR HPA; HPA027168; -. DR MIM; 610656; gene. DR neXtProt; NX_Q6YP21; -. DR PharmGKB; PA162381274; -. DR eggNOG; KOG0257; Eukaryota. DR eggNOG; COG0436; LUCA. DR GeneTree; ENSGT00650000093238; -. DR HOGENOM; HOG000223045; -. DR HOVERGEN; HBG008391; -. DR InParanoid; Q6YP21; -. DR KO; K00816; -. DR OMA; ARKVHDF; -. DR OrthoDB; EOG76DTSB; -. DR PhylomeDB; Q6YP21; -. DR TreeFam; TF352342; -. DR BioCyc; MetaCyc:HS06422-MONOMER; -. DR BRENDA; 2.6.1.7; 2681. DR Reactome; R-HSA-71240; Tryptophan catabolism. DR GenomeRNAi; 56267; -. DR NextBio; 61929; -. DR PRO; PR:Q6YP21; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; Q6YP21; -. DR CleanEx; HS_CCBL2; -. DR ExpressionAtlas; Q6YP21; baseline and differential. DR Genevisible; Q6YP21; HS. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC. DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; ISS:UniProtKB. DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB. DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. DR GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB. DR GO; GO:0097052; P:L-kynurenine metabolic process; ISS:GOC. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006569; P:tryptophan catabolic process; TAS:Reactome. 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 Acetylation; Alternative splicing; Aminotransferase; KW Complete proteome; Lyase; Polymorphism; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 454 Kynurenine--oxoglutarate transaminase 3. FT /FTId=PRO_0000287704. FT BINDING 53 53 Substrate. {ECO:0000250}. FT BINDING 71 71 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 218 218 Substrate. {ECO:0000250}. FT BINDING 429 429 Substrate. {ECO:0000250}. FT MOD_RES 116 116 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 116 116 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q71RI9}. FT MOD_RES 280 280 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. FT VAR_SEQ 1 34 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_042841. FT VAR_SEQ 152 167 VILIVPFYDCYEPMVR -> YNACTVKFTNLKCTAG (in FT isoform 2). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_025603. FT VAR_SEQ 168 454 Missing (in isoform 2). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_025604. FT VARIANT 206 206 S -> P (in dbSNP:rs1059370). FT {ECO:0000269|Ref.6, ECO:0000269|Ref.7}. FT /FTId=VAR_032352. FT CONFLICT 251 251 W -> R (in Ref. 7; CAG29278). FT {ECO:0000305}. SQ SEQUENCE 454 AA; 51400 MW; 2059D4646058BBB3 CRC64; MFLAQRSLCS LSGRAKFLKT ISSSKILGFS TSAKMSLKFT NAKRIEGLDS NVWIEFTKLA ADPSVVNLGQ GFPDISPPTY VKEELSKIAA IDSLNQYTRG FGHPSLVKAL SYLYEKLYQK QIDSNKEILV TVGAYGSLFN TIQALIDEGD EVILIVPFYD CYEPMVRMAG ATPVFIPLRS KPVYGKRWSS SDWTLDPQEL ESKFNSKTKA IILNTPHNPL GKVYNREELQ VIADLCIKYD TLCISDEVYE WLVYSGNKHL KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPNHLIK HLQTVQQNTI YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR DRMVRLLESV GLKPIVPDGG YFIIADVSLL DPDLSDMKNN EPYDYKFVKW MTKHKKLSAI PVSAFCNSET KSQFEKFVRF CFIKKDSTLD AAEEIIKAWS VQKS //