Q5DGJ1 (KYNU_SCHJA) 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:

SJCHGC00887

Organism

Schistosoma japonicum (Blood fluke)

Taxonomic identifier

6182 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
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
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 – 436	436	Kynureninase		PRO_0000356960
Regions
	Region	116 – 119	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	88	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	89	1	Pyridoxal phosphate By similarity
	Binding site	202	1	Pyridoxal phosphate By similarity
	Binding site	205	1	Pyridoxal phosphate By similarity
	Binding site	227	1	Pyridoxal phosphate By similarity
	Binding site	280	1	Pyridoxal phosphate By similarity
	Binding site	308	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	228	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5DGJ1 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: D2585D22865EC083	FASTA	436	50,248
	10 20 30 40 50 60 MKILQYKSIE NVQYSKNILY FCGHSMGLQP KSTKIYINKI LNQWKNLGVL SYHYGELPAS 70 80 90 100 110 120 YCDEQLSIDC AQWIVNAKFN EVSITCNLTV NMHVLIAKFY RPTNEKYCIL IENDIFPSDY 130 140 150 160 170 180 YVLESHIQWH GYNTNDCFIK LKPRLHEYCL RNDDILPEII KNQHRIALIW LPGIQYITGQ 190 200 210 220 230 240 LFNMKLITEW GHQYAKCPVG WDLAHAVGNI PLYLHDWNID MAVWCSYKYL NGSPGAIGGL 250 260 270 280 290 300 FIHEKHHHEE GSYGPKFIEF TNNNNITIFN NINGPQLTGW WSHRSETRFN MTGNMELAKG 310 320 330 340 350 360 ANAYRLSNPP LLLAAALTVS VNIIKSCGGM INLREKSIKL TDYLEYLITN SSLALKHDHY 370 380 390 400 410 420 CLVTPSNSNE RGAQLTISVT HMNIQVVYEN LLKLGVICDY RLPNFLRITP IPLYNSFEDV 430 YLLAKCLHQV LNDTLN

References

[1]

"New perspectives on host-parasite interplay by comparative transcriptomic and proteomic analyses of Schistosoma japonicum." Liu F., Lu J., Hu W., Wang S.-Y., Cui S.-J., Chi M., Yan Q., Wang X.-R., Song H.-D., Xu X.-N., Wang J.-J., Zhang X.-L., Zhang X., Wang Z.-Q., Xue C.-L., Brindley P.J., McManus D.P., Yang P.-Y. , Feng Z., Chen Z., Han Z.-G. PLoS Pathog. 2:268-281(2006) [PubMed: 16617374] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY813333 mRNA. Translation: AAW25065.1.
3D structure databases
ProteinModelPortal	Q5DGJ1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5DGJ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
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_SCHJA

Accession

Primary (citable) accession number: Q5DGJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	March 29, 2005
Last modified:	September 21, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)