[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney; NIH - Zebrafish Gene Collection (ZGC) project; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.

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.
CATALYTIC ACTIVITY: RS-CH²-CH(NH₃⁺)COO^- = RSH + NH₃ + pyruvate.
COFACTOR: Pyridoxal phosphate (By similarity).
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC053152; AAH53152.1; ALT_INIT; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_956638.1; -.

UniGene

Dr.82010

3D structure databases

HSSP

O59096; 1DJU. [HSSP ENTRY / PDB]

ModBase

Q7T3E5.

Organism-specific databases

ZFIN

ZDB-GENE-040426-1299; ccbl2.

Ontologies

GO:0047804;	Molecular function: cysteine-S-conjugate beta-lyase activity (inferred from electronic annotation from EC).
GO:0016212;	Molecular function: kynurenine-oxoglutarate transaminase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR001176; ACC_synthase.
IPR004839; Aminotrans_I/II.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.

Pfam

PF00155; Aminotran_1_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00753; ACCSYNTHASE.

Genome annotation databases

Ensembl

ENSDARG00000013423; Danio rerio. [Contig view]

GeneID

393315; -.

KEGG

dre:393315; -.

Phylogenomic databases

HOGENOM

Q7T3E5; -.

HOVERGEN

Q7T3E5; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aminotransferase; Lyase; Pyridoxal phosphate; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 450`	`450`	`Kynurenine--oxoglutarate transaminase 3.`	`PRO_0000287707`
`BINDING`	`278 278`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 450 AA [This is the length of the unprocessed precursor]

Molecular weight: 50345 Da [This is the MW of the unprocessed precursor]

CRC64: 473A55EBF1401312 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHPIHLLRIV SSVRRLLQTN RCRSFSSCQH NMASIKHKNA RRIEGLDKNV WVAFTSVAAD 

        70         80         90        100        110        120 
PSIVNLGQGY PDIPPPSYVK EGLAQAAMVD RLNQYTRGFG HPTLVKALSK VYGKVYDRQL 

       130        140        150        160        170        180 
DPFKEILVTV GGYGSLFSTM QALVEEGDEV IIIEPFFDCY VPMVKMAGAK PVLIPLRLKS 

       190        200        210        220        230        240 
TATTGISSAD WVLDQEELAS KFNSKTKAII VNTPNNPIGK IFSRSELQAI ADLCIKHDTL 

       250        260        270        280        290        300 
CFSDEVYEWL IYKGHEHVKI ATLPGMWDRT ITVGSAGKTF SVTGWKLGWS IGPEHLIRHL 

       310        320        330        340        350        360 
QTVMQNSLYT CPTPLQEAVG RGLLRDFELM GQPDCYFSAL ALELEGKRDR MAAMLAQTGM 

       370        380        390        400        410        420 
TPVVPEGGYF MIVDVTALNQ DLTHMGDDEP YDYKFVKWMI KEKKLAAIPV TAFVGEDSVK 

       430        440        450 
QFEKYIRLCF IKQESTLDAA EAILKNWNKG

Q7T3E5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools