Reviewed, UniProtKB/Swiss-Prot A7SCH8 (KYNU_NEMVE)

Names and origin

Protein names

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

Gene names

Name:	kynu
ORF Names:	v1g235255

Organism

Nematostella vectensis (Starlet sea anemone) [Complete proteome]

Taxonomic identifier

45351 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Cnidaria › Anthozoa › Hexacorallia › Actiniaria › Edwardsiidae › Nematostella

Protein attributes

Sequence length	465 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
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 – 465	465	Kynureninase		PRO_0000361088
Regions
	Region	161 – 164	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	133	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	134	1	Pyridoxal phosphate By similarity
	Binding site	217	1	Pyridoxal phosphate By similarity
	Binding site	246	1	Pyridoxal phosphate By similarity
	Binding site	249	1	Pyridoxal phosphate By similarity
	Binding site	271	1	Pyridoxal phosphate By similarity
	Binding site	302	1	Pyridoxal phosphate By similarity
	Binding site	330	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	272	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7SCH8-1 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: 4F52CE41A24A5D9C	FASTA	465	52,709
	10 20 30 40 50 60 MAYKPTQTLR KLAEKSSLDI VSREFADYMD SKDPLRKMRD EFFYPRVKDL PGVDLSLVDG 70 80 90 100 110 120 DQDSIYFCGN SLGLQPRGCR ELIDRSLTKW EQMGVLGHTS GWCPWKPIED ILIKPMAEII 130 140 150 160 170 180 GAKDIEVVAM NTLTVNLHMM MVPFYRPTPQ RYKILMEGKA FPSDQYAAQS QVHFHGFDPD 190 200 210 220 230 240 KDIIEVFPRE GEQSLRTEDI LSAIEEHGNS ITLVLFSGVQ YYTGQFFDMK TITAAAQKKG 250 260 270 280 290 300 CVVGWDLAHA VGNVELHLHD WNVDFACWCT YKYLNSGPGG IAGAFVHEKH AYNFELPKFA 310 320 330 340 350 360 GWWGTDRNSR FQMRKEFEQI PGAHGYQCSN PPVFQCLLLR ASLDVFEKTS VKEIRAKGDL 370 380 390 400 410 420 LTAYLELLLL HYFSPSNDIT KNGNTPHVSI ITPADPKDRG CQLSVKFSVP VDKVFEELCK 430 440 450 460 RGFVGDIRHP DVMRIAPAPL YNSFADVHRF ISMLNAAFKT ITPNS

References

[1]

"Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization." Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A., Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J., Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R., Technau U., Martindale M.Q., Rokhsar D.S. Science 317:86-94(2007) [PubMed: 17615350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CH2 X CH6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS469623 Genomic DNA. Translation: EDO38606.1.
RefSeq	XP_001630669.1.
UniGene	Nve.12420
3D structure databases
SMR	A7SCH8. Positions 4-459.
ModBase	Search...
Genome annotation databases
GeneID	5510175.
KEGG	nve:NEMVE_v1g235255.
Phylogenomic databases
OMA	FAVGCTY.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. 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.
PANTHER	PTHR14084. Kynureninase. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU_NEMVE

Accession

Primary (citable) accession number: A7SCH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	October 2, 2007
Last modified:	February 9, 2010
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)