Reviewed, UniProtKB/Swiss-Prot Q5B0H8 (KYNU1_EMENI)

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:	AN5952

Organism

Emericella nidulans (Aspergillus nidulans) [Complete proteome]

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	487 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 – 487	487	Kynureninase 1		PRO_0000356977
Regions
	Region	177 – 180	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	149	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	150	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	329	1	Pyridoxal phosphate By similarity
	Binding site	357	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	289	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5B0H8-1 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 0E77B19E6DCFE55D	FASTA	487	54,517
	10 20 30 40 50 60 MGSRLHVQQI KNGPPLPYKD DIRAFTRDYA ASLDAQDPLS HFREEFIIPS VKDLKRKTLD 70 80 90 100 110 120 PSEGEYSSMY LDARCIYLCG NSLGLQPRNT KKYINYYLRT WAIKGVTGHF THHDDELLPP 130 140 150 160 170 180 FVDVDSAGAK LMAPVVGALE SEVAVMGSLT TNLHLLMASF YRPTTERYKI IIEGKAFPSD 190 200 210 220 230 240 HYAVESQIKH HNLQPKDAMV LIEPQDPEHP ILETDRILRV IDEHASTTAL LLLSAIQYYT 250 260 270 280 290 300 GQYFNIEKIT AHAQSKGIVV GWDCAHAAGN VDLKLHDWNV DFAAWCNYKY LNSGPGGMAG 310 320 330 340 350 360 IFVHEKHGEV KAGQGDGELE LFRPRLSGWW GGDKATRFLM DNHFVPQSGA AGYQLSNPSV 370 380 390 400 410 420 LDMNAVVASL ELFNRTSMAE IRQKSLNLTG YLEHLLLASL DGVSDKPFSI ITPPNPSERG 430 440 450 460 470 480 AQLSLRLAPG LLDSVLETLE EYAVVIDERK PDVIRVAPAP LYNTYEEVWQ FCQIFSEACR KALEKKD

References

[1]

"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACD01000101 Genomic DNA. Translation: EAA57815.1.
RefSeq	XP_663556.1.
3D structure databases
SMR	Q5B0H8. Positions 22-478.
ModBase	Search...
Genome annotation databases
GeneID	2870933.
KEGG	ani:AN5952.2.
Phylogenomic databases
PhylomeDB	Q5B0H8.
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

KYNU1_EMENI

Accession

Primary (citable) accession number: Q5B0H8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	April 26, 2005
Last modified:	February 9, 2010
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)