Reviewed, UniProtKB/Swiss-Prot Q18026 (KYNU_CAEEL)

Names and origin

Protein names

Recommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase

Gene names

ORF Names:

C15H9.7

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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
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 – 478	478	Kynureninase		PRO_0000218660
Regions
	Region	178 – 181	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	150	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	151	1	Pyridoxal phosphate By similarity
	Binding site	263	1	Pyridoxal phosphate By similarity
	Binding site	266	1	Pyridoxal phosphate By similarity
	Binding site	288	1	Pyridoxal phosphate By similarity
	Binding site	318	1	Pyridoxal phosphate By similarity
	Binding site	346	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	289	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q18026-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E889450929EC94BD	FASTA	478	54,050
	10 20 30 40 50 60 MSDAPPQPEN EQECMCTQDK VLQFLNKMAD ESGIKDLTDP ALAEFLSDSD ALKEIRDLFH 70 80 90 100 110 120 YPKAGTLPDA DPSLVDPESD SIYLCGNSLG LMPKATGEVM KDHLDKWAKM GVFGHMSGEV 130 140 150 160 170 180 PWAHCDEYCL EGVGRLVGAK KEEVSVCNSL TVNIHVLLTS FYKPTETRHK ILLESKAFPS 190 200 210 220 230 240 DHYAIESQIR LKGRTVQDSM VCLEPREGEE TLRTEDILDY IEKNGDEIAI VFFSGIQYYT 250 260 270 280 290 300 GQLFDMRAIT EAGHRKGCFV GFDLAHAFAN VPLHLHWWDV DFACWCSYKY GCTGAGSIGG 310 320 330 340 350 360 LFVHERFLND QRERMLGWWS HKMSSRFVMD NVLDLDEGAA GYRISNPPIH TVAAMLGSLK 370 380 390 400 410 420 VFDQVSLENL RSRSCYLTGY LEYLVKTLFG ENSEQRTTKL SISIITPEEF HQRGCQLSLK 430 440 450 460 470 FSSPIDIIYP ELVKRGCAVD KRYPNVIRVA PVHLYNNYVD IRRFISVLQE VAHIVESE

References

[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"The Caenorhabditis elegans transcriptome project, a complementary view of the genome." Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y., Thierry-Mieg D., Thierry-Mieg J. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Bristol N2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U56965 Genomic DNA. Translation: AAB52668.1. AF303267 mRNA. Translation: AAG50225.1.
PIR	T15516.
RefSeq	NP_509023.1.
UniGene	Cel.19413
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q18026. 1 interaction.
STRING	Q18026.
Genome annotation databases
Ensembl	C15H9.7; C15H9.7; C15H9.7; Caenorhabditis elegans. [Genome view]
GeneID	180883.
KEGG	cel:C15H9.7.
NMPDR	fig|6239.3.peg.23462.
UCSC	C15H9.7. c. elegans.
Organism-specific databases
CTD	180883.
WormBase	WBGene00015802. C15H9.7.
WormPep	C15H9.7. CE06835. [WorfDB]
Phylogenomic databases
OMA	NFPTDVY.
Enzyme and pathway databases
BRENDA	3.7.1.3. 672.
Gene expression databases
ArrayExpress	Q18026.
Family and domain databases
InterPro	IPR010111. Kynureninase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR14084. Kynureninase. 1 hit.
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	911400.

Entry information

Entry name

KYNU_CAEEL

Accession

Primary (citable) accession number: Q18026

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project