A1CHT0 (KYNU2_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kynureninase 2
EC=3.7.1.3

Alternative name(s):
Biosynthesis of nicotinic acid protein 5-2
L-kynurenine hydrolase 2

Gene names

Name:	bna5-2
ORF Names:	ACLA_049070

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	464 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 – 464	464	Kynureninase 2		PRO_0000356962
Regions
	Region	163 – 166	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	135	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	136	1	Pyridoxal phosphate By similarity
	Binding site	248	1	Pyridoxal phosphate By similarity
	Binding site	251	1	Pyridoxal phosphate By similarity
	Binding site	273	1	Pyridoxal phosphate By similarity
	Binding site	313	1	Pyridoxal phosphate By similarity
	Binding site	341	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	274	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1CHT0 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 011392A1F27E2766	FASTA	464	51,324
	10 20 30 40 50 60 MSTTTTSSKP EFPADAATKE YAASLDASDP LAGFREKFII PSKANIASKK LAKPGLSSEP 70 80 90 100 110 120 CIYFCGNSLG IQPKATAKYL EAQLDTWSSI GVSGHFTNVE DSPLREWQNL AEQAAESMSR 130 140 150 160 170 180 VVGAAPEEVA AMGTLTMNLH LLLASFYRPT ATKHKILMDW KAFPSDHYAI ESHIAWHDLD 190 200 210 220 230 240 PKESMVLIGP DEGTFEIPTE KILSYIDQHA DDAALILLPG IQYYTGQLFD IQKITEYAQS 250 260 270 280 290 300 RGLVVGWDLA HAYGNVHLKL HDWNVDFAAW CTYKYGNAGP GAMAGLFVHE RHGRVDYREG 310 320 330 340 350 360 EDSPKFRHRL TGWYGGDKSV RFKMDNNFKP IPGAGGYQIS NPSAIDLASL CAALSVFDET 370 380 390 400 410 420 SMAELRRKSV LMTAYLEHLL LKDTTDESRL FDIITPSEPA ARGAQLSLLL RPGLLHKVAQ 430 440 450 460 RLQEAGIICD KREPGVVRVA PVPLYNTFTE VWTFVEQLKA ALEE

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
EMBL GenBank DDBJ	DS027054 Genomic DNA. Translation: EAW10435.1.
RefSeq	XP_001271861.1. XM_001271860.1.
3D structure databases
ProteinModelPortal	A1CHT0.
ModBase	Search...
Protein-protein interaction databases
STRING	A1CHT0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADACLAT00005044; CADACLAP00004943; CADACLAG00005044.
GeneID	4704039.
KEGG	act:ACLA_049070.
Phylogenomic databases
GeneTree	EFGT00050000005118.
OrthoDB	EOG4TB7KQ.
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.
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

KYNU2_ASPCL

Accession

Primary (citable) accession number: A1CHT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program