Reviewed, UniProtKB/Swiss-Prot Q71RI9 (KAT3_MOUSE)

Names and origin

Protein names

Recommended name:
    Kynurenine--oxoglutarate transaminase 3
    EC=2.6.1.7
Alternative name(s):
    Kynurenine--oxoglutarate transaminase III
    Kynurenine aminotransferase III
      Short name=KATIII
    Cysteine-S-conjugate beta-lyase 2
    EC=4.4.1.13

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

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.
Catalytic activity	L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. RS-CH(2)-CH(NH3+)COO- = RSH + NH3 + pyruvate.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homodimer By similarity.
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.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Lyase Transferase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
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-oxoglutarate transaminase activity Inferred from electronic annotation. Source: EC 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

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 By similarity

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. 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.
+	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.

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q71RI9.

PTM databases

PhosphoSite

Q71RI9.

Proteomic databases

PRIDE

Q71RI9.

Genome annotation databases

Ensembl

ENSMUST00000106217; ENSMUSP00000101824; ENSMUSG00000040213; Mus musculus. [Genome view]
ENSMUST00000106218; ENSMUSP00000101825; ENSMUSG00000040213; Mus musculus. [Genome view]

GeneID

229905.

KEGG

mmu:229905.

UCSC

uc008rpa.1. mouse.

Organism-specific databases

CTD

229905.

MGI

MGI:2677849. Ccbl2.

Phylogenomic databases

eggNOG

roNOG05849.

HOGENOM

HBG645860.

HOVERGEN

Q71RI9.

InParanoid

Q71RI9.

OMA

NKHIKIA.

OrthoDB

EOG9C8BBR.

PhylomeDB

Q71RI9.

Enzyme and pathway databases

BRENDA

2.6.1.7. 244.
4.4.1.13. 244.

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.
[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

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:	January 19, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)