B2AP14 (B2AP14_PODAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names	Recommended name: Kynureninase PIRNR PIRNR038800 EC=3.7.1.3 PIRNR PIRNR038800
Organism	Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) [Complete proteome]
Taxonomic identifier	515849 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Lasiosphaeriaceae › Podospora › Podospora anserina

Protein attributes

Sequence length	474 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
Gene Ontology (GO)
Biological_process	L-kynurenine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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)
	B2AP14 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: DCB0CA4CB24A6003	FASTA	474	52,305
	10 20 30 40 50 60 MDSLTAAFRS GQKPSFPAEA GTLEYAQSLD QQDKLGHLRK EFNIPTRTSL KKKALNGVSP 70 80 90 100 110 120 GENDSEDEKS IYFVGNSLGA QPKAVRRALE SQLETWASIG VNGHFSTLEN SPLSSWQDLA 130 140 150 160 170 180 ESCARKSVDL VGAAVPEEII YMNTLTANLH LMMASFYKPT AERDKVIIEW KPFPSDWYAI 190 200 210 220 230 240 QSQIRHHNLS PSTSLIEIQP TPDLYLTTES ILATITEHAP STALVLLPGI QYYTGQLLDI 250 260 270 280 290 300 KTITAHAHSL GIPCVGWDLA HAAGNVPLHL HDWNVDFAVW CTYKYINAGP GSTAGLFLHQ 310 320 330 340 350 360 KHHSKNLDRL EGWYGADKSV RFLMEKEFKP SKGASGWQLS NPSAIDLASV SAALGVFESV 370 380 390 400 410 420 GERYMERLRG KAVVLTGYLE CLLEGLIRGG VGRKGEEQAF RIITPGNPLE RGTQLSLMLR 430 440 450 460 470 EGILEGVSKV LAEEGVVCDA RKPDVIRVAP VPMYCRFEDV WRFVEIFKGA LARV

References

[1]

"The genome sequence of the model ascomycete fungus Podospora anserina." Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M., Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V., Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M., Contamine V., Arnaise S. , Bourdais A., Berteaux-Lecellier V., Gautheret D., de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B., El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H., Debuchy R., Wincker P., Weissenbach J., Silar P. Genome Biol. 9:R77.1-R77.22(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU633873 Genomic DNA. Translation: CAP65719.1.
RefSeq	XP_001905477.1. XM_001905442.1.
3D structure databases
ProteinModelPortal	B2AP14.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6189648.
KEGG	pan:PODANSg2503.
Phylogenomic databases
KO	K01556.
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

B2AP14_PODAN

Accession

Primary (citable) accession number: B2AP14

Entry history

Integrated into UniProtKB/TrEMBL:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)