Q6YP21 (KAT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynurenine--oxoglutarate transaminase 3
EC=2.6.1.7

Alternative name(s):
Cysteine-S-conjugate beta-lyase 2
EC=4.4.1.13
Kynurenine aminotransferase III
Short name=KATIII
Kynurenine--glyoxylate transaminase
EC=2.6.1.63
Kynurenine--oxoglutarate transaminase III

Gene names

Name:	CCBL2
Synonyms:	KAT3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond By similarity. Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) By similarity.
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. RS-CH(2)-CH(NH3+)COO- + H2O = RSH + NH3 + pyruvate. L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Caution	The first non-coding exon of CCBL2 is in common with that of RBMXL1.
Sequence caution	The sequence AAC72959.1 differs from that shown. Reason: Frameshift at position 336. The sequence AAH00819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAG29278.1 differs from that shown. Reason: Frameshift at position 336. The sequence CAI21695.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI21696.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI41339.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI41340.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Lyase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from electronic annotation. Source: Compara biosynthetic process Inferred from electronic annotation. Source: InterPro tryptophan catabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	cysteine-S-conjugate beta-lyase activity Inferred from electronic annotation. Source: EC kynurenine-glyoxylate transaminase activity Inferred from sequence or structural similarity. Source: UniProtKB kynurenine-oxoglutarate transaminase activity Inferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6YP21-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6YP21-2)

The sequence of this isoform differs from the canonical sequence as follows:
     152-167: VILIVPFYDCYEPMVR → YNACTVKFTNLKCTAG
     168-454: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q6YP21-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 454	454	Kynurenine--oxoglutarate transaminase 3		PRO_0000287704
Sites
	Binding site	53	1	Substrate By similarity
	Binding site	71	1	Substrate; via amide nitrogen By similarity
	Binding site	218	1	Substrate By similarity
	Binding site	429	1	Substrate By similarity
Amino acid modifications
	Modified residue	116	1	N6-acetyllysine Ref.8
	Modified residue	280	1	N6-(pyridoxal phosphate)lysine By similarity
Natural variations
	Alternative sequence	1 – 34	34	Missing in isoform 3.		VSP_042841
	Alternative sequence	152 – 167	16	VILIV…EPMVR → YNACTVKFTNLKCTAG in isoform 2.		VSP_025603
	Alternative sequence	168 – 454	287	Missing in isoform 2.		VSP_025604
	Natural variant	206	1	S → P. Ref.6 Ref.7 Corresponds to variant rs1059370 [ dbSNP | Ensembl ].		VAR_032352
Experimental info
	Sequence conflict	251	1	W → R in CAG29278. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 2059D4646058BBB3	FASTA	454	51,400
	10 20 30 40 50 60 MFLAQRSLCS LSGRAKFLKT ISSSKILGFS TSAKMSLKFT NAKRIEGLDS NVWIEFTKLA 70 80 90 100 110 120 ADPSVVNLGQ GFPDISPPTY VKEELSKIAA IDSLNQYTRG FGHPSLVKAL SYLYEKLYQK 130 140 150 160 170 180 QIDSNKEILV TVGAYGSLFN TIQALIDEGD EVILIVPFYD CYEPMVRMAG ATPVFIPLRS 190 200 210 220 230 240 KPVYGKRWSS SDWTLDPQEL ESKFNSKTKA IILNTPHNPL GKVYNREELQ VIADLCIKYD 250 260 270 280 290 300 TLCISDEVYE WLVYSGNKHL KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPNHLIK 310 320 330 340 350 360 HLQTVQQNTI YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR DRMVRLLESV 370 380 390 400 410 420 GLKPIVPDGG YFIIADVSLL DPDLSDMKNN EPYDYKFVKW MTKHKKLSAI PVSAFCNSET 430 440 450 KSQFEKFVRF CFIKKDSTLD AAEEIIKAWS VQKS
	Isoform 2 [UniParc]. Checksum: 6CA0C2A9BC6BA211	FASTA	167	18,352
	10 20 30 40 50 60 MFLAQRSLCS LSGRAKFLKT ISSSKILGFS TSAKMSLKFT NAKRIEGLDS NVWIEFTKLA 70 80 90 100 110 120 ADPSVVNLGQ GFPDISPPTY VKEELSKIAA IDSLNQYTRG FGHPSLVKAL SYLYEKLYQK 130 140 150 160 QIDSNKEILV TVGAYGSLFN TIQALIDEGD EYNACTVKFT NLKCTAG
	Isoform 3 [UniParc]. Checksum: 1BB37BC0D96DB2EE	FASTA	420	47,753
	10 20 30 40 50 60 MSLKFTNAKR IEGLDSNVWI EFTKLAADPS VVNLGQGFPD ISPPTYVKEE LSKIAAIDSL 70 80 90 100 110 120 NQYTRGFGHP SLVKALSYLY EKLYQKQIDS NKEILVTVGA YGSLFNTIQA LIDEGDEVIL 130 140 150 160 170 180 IVPFYDCYEP MVRMAGATPV FIPLRSKPVY GKRWSSSDWT LDPQELESKF NSKTKAIILN 190 200 210 220 230 240 TPHNPLGKVY NREELQVIAD LCIKYDTLCI SDEVYEWLVY SGNKHLKIAT FPGMWERTIT 250 260 270 280 290 300 IGSAGKTFSV TGWKLGWSIG PNHLIKHLQT VQQNTIYTCA TPLQEALAQA FWIDIKRMDD 310 320 330 340 350 360 PECYFNSLPK ELEVKRDRMV RLLESVGLKP IVPDGGYFII ADVSLLDPDL SDMKNNEPYD 370 380 390 400 410 420 YKFVKWMTKH KKLSAIPVSA FCNSETKSQF EKFVRFCFIK KDSTLDAAEE IIKAWSVQKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family." Yu P., Li Z., Zhang L., Tagle D.A., Cai T. Gene 365:111-118(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Fetal kidney.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Stomach.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-454 (ISOFORM 1). Tissue: Placenta.
[6]	"Full-insert sequence of mapped XREF EST." Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-454, VARIANT PRO-206.
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-338, VARIANT PRO-206.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY028624 mRNA. Translation: AAK26163.1. CR627392 mRNA. Translation: CAH10487.1. AK057176 mRNA. Translation: BAG51875.1. AL445991 Genomic DNA. Translation: CAI41345.1. AL139416, AL445991 Genomic DNA. Translation: CAI21695.1. Sequence problems. AL445991, AL139416 Genomic DNA. Translation: CAI41339.1. Sequence problems. AL139416, AL445991 Genomic DNA. Translation: CAI21696.1. Sequence problems. AL445991, AL139416 Genomic DNA. Translation: CAI41340.1. Sequence problems. BC000819 mRNA. Translation: AAH00819.1. Different initiation. AF091090 mRNA. Translation: AAC72959.1. Frameshift. CR450282 mRNA. Translation: CAG29278.1. Frameshift.
IPI	IPI00465006. IPI00465373.
RefSeq	NP_001008661.1. NM_001008661.2. NP_001008662.1. NM_001008662.2.
UniGene	Hs.481898.
3D structure databases
ProteinModelPortal	Q6YP21.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6YP21. 6 interactions.
MINT	MINT-1402454.
STRING	9606.ENSP00000260508.
PTM databases
PhosphoSite	Q6YP21.
Polymorphism databases
DMDM	74710502.
Proteomic databases
PaxDb	Q6YP21.
PRIDE	Q6YP21.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000260508; ENSP00000260508; ENSG00000137944. ENST00000370485; ENSP00000359516; ENSG00000137944. ENST00000370486; ENSP00000359517; ENSG00000137944. ENST00000370491; ENSP00000359522; ENSG00000137944.
GeneID	56267.
KEGG	hsa:56267.
UCSC	uc001dmp.2. human.
Organism-specific databases
CTD	56267.
GeneCards	GC01M089401.
HGNC	HGNC:33238. CCBL2.
HPA	HPA026538. HPA027168.
MIM	610656. gene.
neXtProt	NX_Q6YP21.
PharmGKB	PA162381274.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0436.
HOGENOM	HOG000223045.
HOVERGEN	HBG008391.
InParanoid	Q6YP21.
KO	K00816.
OMA	KRDRMVH.
Enzyme and pathway databases
BRENDA	2.6.1.7. 2681.
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q6YP21.
Bgee	Q6YP21.
CleanEx	HS_CCBL2.
Genevestigator	Q6YP21.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00142. L-Glutamic Acid. DB00114. Pyridoxal Phosphate.
GenomeRNAi	56267.
NextBio	61929.
SOURCE	Search...

Entry information

Entry name

KAT3_HUMAN

Accession

Primary (citable) accession number: Q6YP21
Secondary accession number(s): B3KQ13 , O95335, Q5JS27, Q5T9T7, Q5T9T8, Q6AI27, Q6ICW1, Q9BVY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.