Reviewed, UniProtKB/Swiss-Prot A1C688 (KYNU1_ASPCL)

Names and origin

Protein names

Recommended name:
    Kynureninase 1
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase 1
    Biosynthesis of nicotinic acid protein 5-1

Gene names

Name:	bna5-1
ORF Names:	ACLA_069390

Organism

Aspergillus clavatus [Complete proteome]

Taxonomic identifier

5057 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 – 486	486	Kynureninase 1		PRO_0000356961
Regions
	Region	174 – 177	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	146	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	147	1	Pyridoxal phosphate By similarity
	Binding site	260	1	Pyridoxal phosphate By similarity
	Binding site	263	1	Pyridoxal phosphate By similarity
	Binding site	285	1	Pyridoxal phosphate By similarity
	Binding site	326	1	Pyridoxal phosphate By similarity
	Binding site	354	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	286	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1C688-1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: B4275CBDF28D6821	FASTA	486	54,747
	10 20 30 40 50 60 MGSRLHTREI QNGPPLPYND DIRAFSKEYA ESLDAQDPLH RFRNEFVIPS KEDLKRTTLD 70 80 90 100 110 120 PNQEPEHSPT PSLYLCGNSL GLQPQSTRKY IEYYLRAWAT KGVTGHFVQH DDQLLPPFVD 130 140 150 160 170 180 VDAAGARLMA PIVGAMESEV AVMGTLTTNL HILMASFYQP TQERYKIIIE GKAFPSDHYA 190 200 210 220 230 240 VESQIKHHNF DPKDGMVLIE PEDHTRPVLD TEHIIRTIDE HASSTAVILL SAIQYYTGQY 250 260 270 280 290 300 FDIKRITAHA QSKGILVGWD CAHAAGNVDL QLHDWNVDFA AWCTYKYLNS GPGGTAALFV 310 320 330 340 350 360 HERHGRVNLE QVNSESEPFR PRLSGWWGGD KKTRFLMDNN FIPQPGAAGF QLSNPSVLDM 370 380 390 400 410 420 NAVVASLELF KQASMAEIRK KSLHITGYLE HLLLNYPLDT PSEKKPFTII TPSNPAERGA 430 440 450 460 470 480 QLSVRLQPGL LDHVLETLED NAVVIDERKP DVIRVAPAPL YNTYTDVWEF CRIFHEACQK ALKARG

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed: 18404212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DS027045 Genomic DNA. Translation: EAW13909.1.
RefSeq	XP_001275335.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4707638.
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...

Entry information

Entry name

KYNU1_ASPCL

Accession

Primary (citable) accession number: A1C688

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)