Q71RI9 (KAT3_MOUSE) 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

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 › Mus

Protein attributes

Sequence length	455 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). Ref.4
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. Ref.4 RS-CH(2)-CH(NH3+)COO- = RSH + NH3 + pyruvate. Ref.4 L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine. Ref.4
Cofactor	Pyridoxal phosphate. Ref.4
Enzyme regulation	Kynurenine transamination is competitively inhibited by cysteine, glutamine, histidine, methionine, leucine, or phenylalanine. Ref.4
Subunit structure	Homodimer. Ref.4
Tissue specificity	Widely expressed, with higher expression levels in liver, kidney, heart and neuroendocrine tissues. Ref.1
Developmental stage	Expressed from postnatal day (PND) 7 and peaks in adult. Ref.1
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Biophysicochemical properties	Kinetic parameters: KM=0.7 mM for glutamine Ref.4 KM=0.7 mM for histidine KM=0.7 mM for cysteine KM=0.9 mM for methionine KM=1.1 mM for phenylalanine KM=1.4 mM for asparagine KM=1.5 mM for kynurenine KM=7.1 mM for tryptophan KM=3.0 mM for serine KM=0.4 mM for glyoxylate KM=0.6 mM for phenylpyruvate pH dependence: Optimum pH is 9. Temperature dependence: Optimum temperature is 60 degrees Celsius.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Lyase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from direct assay Ref.4. Source: UniProtKB kynurenine metabolic process Inferred from direct assay Ref.4. Source: UniProtKB
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
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 kynurenine-glyoxylate transaminase activity Inferred from direct assay Ref.4. Source: UniProtKB kynurenine-oxoglutarate transaminase activity Inferred from direct assay Ref.4. Source: UniProtKB protein homodimerization activity Inferred from physical interaction Ref.4. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q71RI9-1)

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: Q71RI9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 455

455

Kynurenine--oxoglutarate transaminase 3

PRO_0000287705

Sites

Binding site

54

1

Substrate

Binding site

72

1

Substrate; via amide nitrogen

Binding site

219

1

Substrate

Binding site

430

1

Substrate

Amino acid modifications

Modified residue

109

1

N6-acetyllysine By similarity

Modified residue

117

1

N6-acetyllysine By similarity

Modified residue

281

1

N6-(pyridoxal phosphate)lysine

Natural variations

Alternative sequence

1 – 35

35

Missing in isoform 2.

VSP_025605

Secondary structure

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455

Helix Strand Turn

Details...

Helix

44 – 46

3

Helix

53 – 56

4

Beta strand

66 – 68

3

Helix

80 – 90

11

Helix

93 – 96

4

Helix

105 – 114

10

Beta strand

119 – 121

3

Turn

125 – 127

3

Helix

139 – 143

5

Beta strand

152 – 158

7

Helix

163 – 169

7

Beta strand

173 – 178

6

Helix

191 – 193

3

Helix

198 – 202

5

Beta strand

209 – 217

9

Helix

227 – 240

14

Beta strand

243 – 247

5

Turn

249 – 252

4

Helix

263 – 265

3

Helix

270 – 272

3

Beta strand

273 – 276

4

Helix

297 – 308

12

Turn

309 – 311

3

Helix

316 – 330

15

Turn

331 – 334

4

Helix

339 – 359

21

Beta strand

364 – 367

4

Beta strand

373 – 377

5

Helix

394 – 406

13

Beta strand

407 – 409

3

Helix

413 – 416

4

Turn

419 – 421

3

Helix

422 – 425

4

Beta strand

428 – 432

5

Helix

437 – 448

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 94FA35EC67121EF2	FASTA	455	51,126
	10 20 30 40 50 60 MLLAQRRLIS LGCRSKPIKT IYSSSKVLGL CTSAKMALKF KNAKRIEGLD SNVWVEFTKL 70 80 90 100 110 120 AADPSVVNLG QGFPDISPPS YVKEELSKAA FIDNMNQYTR GFGHPALVKA LSCLYGKIYQ 130 140 150 160 170 180 RQIDPNEEIL VAVGAYGSLF NSIQGLVDPG DEVIIMVPFY DCYEPMVRMA GAVPVFIPLR 190 200 210 220 230 240 SKPTDGMKWT SSDWTFDPRE LESKFSSKTK AIILNTPHNP LGKVYTRQEL QVIADLCVKH 250 260 270 280 290 300 DTLCISDEVY EWLVYTGHTH VKIATLPGMW ERTITIGSAG KTFSVTGWKL GWSIGPAHLI 310 320 330 340 350 360 KHLQTVQQNS FYTCATPLQA ALAEAFWIDI KRMDDPECYF NSLPKELEVK RDRMVRLLNS 370 380 390 400 410 420 VGLKPIVPDG GYFIIADVSS LGADLSDMNS DEPYDYKFVK WMTKHKKLTA IPVSAFCDSK 430 440 450 SKPHFEKLVR FCFIKKDSTL DAAEEIFRAW NSQKS
	Isoform 2 [UniParc]. Checksum: A6925006F7CE1C9C	FASTA	420	47,321
	10 20 30 40 50 60 MALKFKNAKR IEGLDSNVWV EFTKLAADPS VVNLGQGFPD ISPPSYVKEE LSKAAFIDNM 70 80 90 100 110 120 NQYTRGFGHP ALVKALSCLY GKIYQRQIDP NEEILVAVGA YGSLFNSIQG LVDPGDEVII 130 140 150 160 170 180 MVPFYDCYEP MVRMAGAVPV FIPLRSKPTD GMKWTSSDWT FDPRELESKF SSKTKAIILN 190 200 210 220 230 240 TPHNPLGKVY TRQELQVIAD LCVKHDTLCI SDEVYEWLVY TGHTHVKIAT LPGMWERTIT 250 260 270 280 290 300 IGSAGKTFSV TGWKLGWSIG PAHLIKHLQT VQQNSFYTCA TPLQAALAEA FWIDIKRMDD 310 320 330 340 350 360 PECYFNSLPK ELEVKRDRMV RLLNSVGLKP IVPDGGYFII ADVSSLGADL SDMNSDEPYD 370 380 390 400 410 420 YKFVKWMTKH KKLTAIPVSA FCDSKSKPHF EKLVRFCFIK KDSTLDAAEE IFRAWNSQKS

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: 16376499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: C57BL/6. Tissue: Brain.
[2]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6J.
[3]	"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] (ISOFORM 2). Tissue: Brain.
[4]	"Biochemical and structural properties of mouse kynurenine aminotransferase III." Han Q., Robinson H., Cai T., Tagle D.A., Li J. Mol. Cell. Biol. 29:784-793(2009) [PubMed: 19029248] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 42-451 IN COMPLEXES WITH KYNURENINE AND GLUTAMINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF363737 mRNA. Translation: AAQ15190.1.
AK049569 mRNA. Translation: BAC33817.1.
AK145623 mRNA. Translation: BAE26546.1.
BC131942 mRNA. Translation: AAI31943.1.
BC132615 mRNA. Translation: AAI32616.1.

IPI

IPI00454201.
IPI00845690.

RefSeq

NP_776124.1. NM_173763.3.

UniGene

Mm.289643.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZJG	X-ray	3.00	A/B	42-451	[»]
3E2F	X-ray	2.59	A/B	42-451	[»]
3E2Y	X-ray	2.26	A/B	42-451	[»]
3E2Z	X-ray	2.81	A/B	42-451	[»]

ProteinModelPortal

Q71RI9.

SMR

Q71RI9. Positions 42-451.

ModBase

Search...

Protein-protein interaction databases

STRING

Q71RI9.

PTM databases

PhosphoSite

Q71RI9.

Proteomic databases

PRIDE

Q71RI9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000044392; ENSMUSP00000041675; ENSMUSG00000040213.
ENSMUST00000106218; ENSMUSP00000101825; ENSMUSG00000040213.

GeneID

229905.

KEGG

mmu:229905.

UCSC

uc008roz.1. mouse.
uc008rpa.1. mouse.

Organism-specific databases

CTD

56267.

MGI

MGI:2677849. Ccbl2.

Phylogenomic databases

eggNOG

roNOG05849.

GeneTree

ENSGT00530000063107.

HOGENOM

HBG645860.

HOVERGEN

HBG008391.

InParanoid

Q71RI9.

OMA

RNLQMVH.

OrthoDB

EOG42JNRH.

PhylomeDB

Q71RI9.

Enzyme and pathway databases

BRENDA

2.6.1.7. 3474.

Gene expression databases

ArrayExpress

Q71RI9.

Bgee

Q71RI9.

CleanEx

MM_CCBL2.

Genevestigator

Q71RI9.

Family and domain databases

InterPro

IPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

KO

K00816.

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

PRINTS

PR00753. ACCSYNTHASE.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

ProtoNet

Search...

Other

NextBio

379731.

SOURCE

Search...

Entry information

Entry name

KAT3_MOUSE

Accession

Primary (citable) accession number: Q71RI9
Secondary accession number(s): Q8BJ84

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	July 5, 2004
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program