Reviewed, UniProtKB/Swiss-Prot Q7S332 (KYNU2_NEUCR)

Names and origin

Protein names

Recommended name:
    Kynureninase 2
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase 2
    Biosynthesis of nicotinic acid protein 5-2

Gene names

Name:	bna-5-2
ORF Names:	NCU09183

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	485 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 – 485	485	Kynureninase 2		PRO_0000356981
Regions
	Region	183 – 186	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	155	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	156	1	Pyridoxal phosphate By similarity
	Binding site	267	1	Pyridoxal phosphate By similarity
	Binding site	270	1	Pyridoxal phosphate By similarity
	Binding site	292	1	Pyridoxal phosphate By similarity
	Binding site	330	1	Pyridoxal phosphate By similarity
	Binding site	358	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	293	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7S332-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: CC38185722A45A37	FASTA	485	54,175
	10 20 30 40 50 60 MSDFTSKVKV LRDGQKPEFP SNANTLEYAQ SLDAQDELRH FRNEFIIPTR ASLKKKALDG 70 80 90 100 110 120 IIPGTQANGT TTSTDADTPC IYFVGNSLGA QPKAVRHYLE AQLETWASIG VNGHFSSLSN 130 140 150 160 170 180 SPLTPWQDMA ADCAAKSAAI VGAADPSEVV IMNTLTVNLH FMMASFYRPT DKRHKIILEW 190 200 210 220 230 240 RPFPSDWYAF QSQIEWHGLD PEKSIVEMQP DENLYLSTEK ILATIDEHAE DAALLLLPGI 250 260 270 280 290 300 QYYTGQLFDI PRITKYAQER GIVVGWDLAH CAGNVELQLH DWNVDFAVWC TYKYLNGGPG 310 320 330 340 350 360 SMAGAFVHER HGKVDMSLGK PVFKPRLSGW YGADKSVRFN MDKEFQPTPG AQGFQVSNPS 370 380 390 400 410 420 AIDLTSLAAA LSVFNKTSMK DLRSKALVLT AYTEHLLDEI VRRQPEGEEP AFKIITPRDP 430 440 450 460 470 480 LQRGTQLSLL LRDGLMDKVA AALEENGVVC DKRKPNVIRV APVPMYCRFE DVWKFMEIFE AAIRG

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	AABX02000069 Genomic DNA. Translation: EAA29857.1.
RefSeq	XP_959093.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q7S332.
Genome annotation databases
GeneID	3875240.
KEGG	ncr:NCU09183.
NMPDR	fig|5141.1.peg.9508.
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

KYNU2_NEUCR

Accession

Primary (citable) accession number: Q7S332

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	December 15, 2003
Last modified:	September 22, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)