Reviewed, UniProtKB/Swiss-Prot Q7RXY2 (KYNU1_NEUCR)

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:	bna-5-1
ORF Names:	NCU00463

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	472 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 – 472	472	Kynureninase 1		PRO_0000218663
Regions
	Region	162 – 165	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	247	1	Pyridoxal phosphate By similarity
	Binding site	250	1	Pyridoxal phosphate By similarity
	Binding site	272	1	Pyridoxal phosphate By similarity
	Binding site	314	1	Pyridoxal phosphate By similarity
	Binding site	342	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	273	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7RXY2-1 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: 8BEAFE163C96995C	FASTA	472	51,627
	10 20 30 40 50 60 MSTAAVQDAR KQAEALDNED SIAFVRDEFN IPTKAQIASS RLADSHPAAL PASEDDAKCI 70 80 90 100 110 120 YLCGNSLGVQ PKRTVTRLNQ YLTTWATQGV QGHFKPLEES PLPTWLDADA KAAELIAPVV 130 140 150 160 170 180 GANVSEVAVM QTLTANIHLL MSAFYRPDIN GRHKIILENK AFPSDHFAVE TQIRHHSLST 190 200 210 220 230 240 EKSMVLIESS SKDNIISTEE VLSVISAHAD TTALLLLPGI QYYTGQLLDI PAITAFAHKH 250 260 270 280 290 300 GIFVIWDLAH AVGNVPLYLH DWGVDAAAWC SYKYLNGGPG CIGGLFVHTN NSVVTKEITD 310 320 330 340 350 360 EKPEEGYNNR LAGWWGNDKK TRFVMANKFH PVAGAAGFQL SNPSILDITS LSASLEIFQE 370 380 390 400 410 420 AGGMEALRSK SLKLTSFLEA TLGHMKEEDR AHFRIITPSK SEERGAQLSL MLSDGLLDTV 430 440 450 460 470 MKELEARGVI VDERKPNVIR VAPAPLYNTF KDCVLFVEAF SAALEVAKQH AL

References

[1]

"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABX02000001 Genomic DNA. Translation: EAA27546.2.
RefSeq	XP_956782.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q7RXY2.
Genome annotation databases
GeneID	3872929.
KEGG	ncr:NCU00463.
Enzyme and pathway databases
BRENDA	3.7.1.3. 266.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 2 hits.
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_NEUCR

Accession

Primary (citable) accession number: Q7RXY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	December 4, 2007
Last modified:	September 22, 2009
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)