C7ZJ53 (C7ZJ53_NECH7) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Kynureninase PIRNR PIRNR038800
EC=3.7.1.3 PIRNR PIRNR038800

Gene names

ORF Names:

NECHADRAFT_49794 EMBL EEU35954.1

Organism

Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) (Fusarium solani subsp. pisi) [Reference proteome]

Taxonomic identifier

660122 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Nectria › Nectria haematococca complex › Nectria haematococca › Fusarium solani subsp. pisi

Protein attributes

Sequence length	496 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. PIRNR PIRNR038800
Catalytic activity	L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800 L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800
Cofactor	Pyridoxal phosphate By similarity. PIRNR PIRNR038800
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800 Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800
Subunit structure	Homodimer By similarity. PIRNR PIRNR038800
Subcellular location	Cytoplasm By similarity PIRNR PIRNR038800.
Sequence similarities	Belongs to the kynureninase family. PIRNR PIRNR038800

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis PIRNR PIRNR038800
Cellular component	Cytoplasm PIRNR PIRNR038800
Ligand	Pyridoxal phosphate PIRNR PIRNR038800
Molecular function	Hydrolase PIRNR PIRNR038800
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-kynurenine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway de novo NAD biosynthetic process from tryptophan Inferred from electronic annotation. Source: EnsemblFungi 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...

Sequences

	Sequence		Length	Mass (Da)
	C7ZJ53 [UniParc]. Last modified October 13, 2009. Version 1. Checksum: 8FA291034D95655B	FASTA	496	55,011
	10 20 30 40 50 60 MELSGFVDRL RSGASPKFPQ DANSLEFARH LDSQDKLSHL RDEFVIPTKR SLKKKALDGS 70 80 90 100 110 120 IPSHGASSNG TNGTNGHSNG HNGSSDDSEQ CLYFVGNSLG AQPKAVREYL NAQLETWASI 130 140 150 160 170 180 GVNGHFSAMG NSPLTPWQDM AEDCAIKSAD IVGASPSEIV IMNTLTANLH FLMASFYKPN 190 200 210 220 230 240 EKRHKIILEW KPFPSDHYAI ESQVVWHGLD PEKSMVKIHP NDDFIITTDL ILSTIDEHAE 250 260 270 280 290 300 DTALLLLPGI QYYSGQLFDI PRITAYAQER GIVVGWDLAH AAGNVELKLH DWNVDFACWC 310 320 330 340 350 360 TYKYINAGPG SIAGAYVHEK HGKVEFKDDS GKPTYRPRLM GWYGGDKSVR FNMDNKFVPT 370 380 390 400 410 420 VGAGGFQLSN PSAIDLASLS GALSVFNKTK MYEIRSKALV LTAYAEHLLD QIISESSDET 430 440 450 460 470 480 PLFRIITPRD PAQRGTQLSV LLREGLMERV SEALEENGVI CDKRKPDVIR VAPVPLYTRF 490 EDVWKFMQVL RGALSQ

References

[1]

"The genome of Nectria haematococca: contribution of supernumerary chromosomes to gene expansion." Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C., Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C., Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M., Nelson D.R., Straney D. , Napoli C.A., Barker B.M., Gribskov M., Rep M., Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L., Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E., Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E., VanEtten H.D. PLoS Genet. 5:E1000618-E1000618(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG698932 Genomic DNA. Translation: EEU35954.1.
RefSeq	XP_003041667.1. XM_003041621.1.
3D structure databases
ProteinModelPortal	C7ZJ53.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	NechaT49794; NechaP49794; NechaG49794.
GeneID	9674071.
KEGG	nhe:NECHADRAFT_49794.
Phylogenomic databases
KO	K01556.
OrthoDB	EOG4TB7KQ.
Enzyme and pathway databases
UniPathway	UPA00253; UER00329. UPA00334; UER00455.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHER	PTHR14084. PTHR14084. 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

C7ZJ53_NECH7

Accession

Primary (citable) accession number: C7ZJ53

Entry history

Integrated into UniProtKB/TrEMBL:	October 13, 2009
Last sequence update:	October 13, 2009
Last modified:	March 6, 2013
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)