Reviewed, UniProtKB/Swiss-Prot Q8BTY1 (KAT1_MOUSE)

Names and origin

Protein names

Recommended name:
    Kynurenine--oxoglutarate transaminase 1
    EC=2.6.1.7
Alternative name(s):
    Kynurenine--oxoglutarate transaminase I
    Kynurenine aminotransferase I
      Short name=KATI
    Glutamine--phenylpyruvate transaminase
    EC=2.6.1.64
    Glutamine transaminase K
      Short name=GTK
    Cysteine-S-conjugate beta-lyase
    EC=4.4.1.13

Gene names

Name:	Ccbl1
Synonyms:	Kat

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes 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.
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. RS-CH(2)-CH(NH3+)COO- = RSH + NH3 + pyruvate.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid degradation; L-kynurenine degradation; kynurenic acid from L-kynurenine: step 1/2.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Lyase Transferase
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro cysteine-S-conjugate beta-lyase activity Inferred from electronic annotation. Source: EC glutamine-phenylpyruvate transaminase activity Inferred from electronic annotation. Source: EC kynurenine-oxoglutarate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 424	424	Kynurenine--oxoglutarate transaminase 1		PRO_0000123943
Amino acid modifications
	Modified residue	247	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	390	1	H → R in BAC31248. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BTY1-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 5C1B3FE94534805B	FASTA	424	47,564
	10 20 30 40 50 60 MSKQLQARRL EGIDHNPWVE FTRLSKEYDV VNLGQGFPDF SPPDFAVQAF QQATTGNFML 70 80 90 100 110 120 NQYTSAFGYP PLTKILASFF GKLLGQEMDP LKNVLVTVGA YGALFTAFQA LVDEGDEVII 130 140 150 160 170 180 IEPAFNCYEP MTMMAGGRPV FVSLRLSPAP KGQLGSSNDW QLDPTELASK FTPRTKILVL 190 200 210 220 230 240 NTPNNPLGKV FSKKELELVA ALCQQHDVLC FSDEVYQWLV YDGHQHISIA SLPGMWERTL 250 260 270 280 290 300 TIGSAGKSFS ATGWKVGWVM GPDNIMKHLR TVHQNSIFHC PTQAQAAVAQ CFEREQQHFG 310 320 330 340 350 360 QPSSYFLQLP QAMGLNRDHM IQSLQSVGLK PLIPQGSYFL IADISDFKSS MPDLPGAMDE 370 380 390 400 410 420 PYDTRFAKWM IKNKGLSAIP VSTFYSQPHH KDFDHYIRFC FVKDKATLQA MDKRLCSWKG EPQA

References

[1]

"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Thymus.

[2]

"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Salivary gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK042391 mRNA. Translation: BAC31248.1. AK088404 mRNA. Translation: BAC40333.1. BC016206 mRNA. Translation: AAH16206.1. BC052047 mRNA. Translation: AAH52047.1.
IPI	IPI00331111.
RefSeq	NP_765992.2.
UniGene	Mm.216089
3D structure databases
HSSP	HSSP built from PDB template 1BJW based on UniProtKB Q56232.
SMR	Q8BTY1. Positions 4-421.
ModBase	Search...
Proteomic databases
PRIDE	Q8BTY1.
Genome annotation databases
Ensembl	ENSMUSG00000039648. Mus musculus. [Contig view]
GeneID	70266.
KEGG	mmu:70266.
Organism-specific databases
MGI	MGI:1917516. Ccbl1.
Phylogenomic databases
HOGENOM	Q8BTY1.
HOVERGEN	Q8BTY1.
Enzyme and pathway databases
BRENDA	2.6.1.64. 244. 2.6.1.7. 244. 4.4.1.13. 244.
Gene expression databases
ArrayExpress	Q8BTY1.
Bgee	Q8BTY1.
CleanEx	MM_CCBL1.
GermOnline	ENSMUSG00000039648. Mus musculus.
Family and domain databases
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotrans_I/II. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
ProtoNet	Search...
Other Resources
NextBio	331276.
SOURCE	Search...

Entry information

Entry name

KAT1_MOUSE

Accession

Primary (citable) accession number: Q8BTY1
Secondary accession number(s): Q8BY27

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)