A8XKT0 (KYNU_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynureninase
EC=3.7.1.3

Alternative name(s):
L-kynurenine hydrolase

Gene names

ORF Names:

CBG14833

Organism

Caenorhabditis briggsae

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity.
Catalytic activity	L-kynurenine + H2O = anthranilate + L-alanine. L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro tryptophan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	kynureninase 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 – 483	483	Kynureninase		PRO_0000356959
Regions
	Region	182 – 185	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	154	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	155	1	Pyridoxal phosphate By similarity
	Binding site	267	1	Pyridoxal phosphate By similarity
	Binding site	270	1	Pyridoxal phosphate By similarity
	Binding site	292	1	Pyridoxal phosphate By similarity
	Binding site	322	1	Pyridoxal phosphate By similarity
	Binding site	350	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	293	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8XKT0 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: F7BD3B8CB98C956A	FASTA	483	54,408
	10 20 30 40 50 60 MAEGQAPAPP QPEGDQECMC TQDKVLQFLN KMADESGIKD LTDPALAEFL TDSDALKGIR 70 80 90 100 110 120 DLFHYPKAGT LPDVDPTLVD PNADSIYLCG NSLGLMPKVT EEVMKEHLDK WAKMGVFGHM 130 140 150 160 170 180 TGEVPWAHSD EHCLEGVGRL VGAKKEEVSI ANSLTVNIHV LLTAFYKPTE TRHKILLESK 190 200 210 220 230 240 AFPSDHYAIE SQIRLKGRTV EESMVCMEPR EGEETLRTED IIDYIENNGD EIAIVFFSGI 250 260 270 280 290 300 QYYTGQLFDI KAITEAGHRK GCLVGWDLAH AFANVPLHLH WWDVDFAAWC SYKYGCTGAG 310 320 330 340 350 360 SIAGLFVHER FLHDKRDRML GWWSHKMSSR FTMDNVLDLD EGAAGYRISN PPIHCVAAML 370 380 390 400 410 420 GSLKIFDQVS LENLRSRSCY LTGYLEYLVK TLFGENSEQR TTKLSILIIT PENFHQRGCQ 430 440 450 460 470 480 LSLKFSSPID VIYPELVKRG VAVDKRYPNV IRVAPVHLYN NYVDVRRFIS VLQEVAHIVE DHA

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CAAC02000521 Genomic DNA. Translation: CAP33254.1.
RefSeq	XP_002644815.1. XM_002644769.1.
3D structure databases
ProteinModelPortal	A8XKT0.
SMR	A8XKT0. Positions 28-476.
ModBase	Search...
Protein-protein interaction databases
STRING	A8XKT0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8586811.
KEGG	cbr:CBG14833.
Organism-specific databases
CTD	8586811.
WormBase	CBG14833; CBP18263; WBGene00035224.
Phylogenomic databases
HOGENOM	HBG523016.
OMA	EIAIVFF.
PhylomeDB	A8XKT0.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K01556.
PANTHER	PTHR14084. Kynureninase. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
PIRSF	PIRSF038800. KYNU. 1 hit.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01814. Kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU_CAEBR

Accession

Primary (citable) accession number: A8XKT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	January 15, 2008
Last modified:	November 16, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project