D4ANI5 (D4ANI5_ARTBC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Kynureninase PIRNR PIRNR038800
EC=3.7.1.3 PIRNR PIRNR038800

Gene names

ORF Names:

ARB_05790 EMBL EFE35746.1

Organism

Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) [Complete proteome]

Taxonomic identifier

663331 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Onygenales › Arthrodermataceae › Arthroderma › Arthroderma benhamiae

Protein attributes

Sequence length	462 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
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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)
	D4ANI5 [UniParc]. Last modified May 18, 2010. Version 1. Checksum: D96BAC95B3EC56B1	FASTA	462	51,761
	10 20 30 40 50 60 MDFSKDPSSL TREYARNLDE QDPLRDFRKE FIIPSKADLT RTTLAPPTGE EERKLEESCV 70 80 90 100 110 120 YLCGNSLGLQ PVSTSEHVNS YLRSWALKGV LGHTEPHTDQ LTAEWLNIDD RAPELMAPLV 130 140 150 160 170 180 GAKESEVALM GTLTSNLHLL MASFYKPTKE RYKIIFEGKA FPSDHFAIES QARHHGLDPE 190 200 210 220 230 240 DAMVLIEPVS EDYPVLETSQ ILSVIDAHAD TAALILLPGI QYYTGQFFDM KTITAHAHSK 250 260 270 280 290 300 GLMVGWDCAH AVGNVELQFH DWDVDFAAWC SYKYLNSGAG AMAGLFVHEK HGMVTEDSFR 310 320 330 340 350 360 PRLSGWWGSD KSSRFIMDNK FVPRPGAAGY QVSNPSALDL AAVTASLKVF NKATMQALRR 370 380 390 400 410 420 KSVKLTAYLE YLIDREFPSK SERPFTIITP SDPDMRGAQL SLRLRAGLLD PVFSCLLRNG 430 440 450 460 VVLDERRPDV IRVAPAPLYN SFEDVWLFVR ELRVACDEAT AR

References

[1]

"Comparative and functional genomics provide insights into the pathogenicity of dermatophytic fungi." Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S., Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O., Schroeckh V. , Hertweck C., Hube B., White T.C., Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A. Genome Biol. 12:R7.1-R7.16(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4681 / CBS 112371.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ABSU01000003 Genomic DNA. Translation: EFE35746.1.
RefSeq	XP_003016391.1. XM_003016345.1.
3D structure databases
ProteinModelPortal	D4ANI5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	9521874.
KEGG	abe:ARB_05790.
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

D4ANI5_ARTBC

Accession

Primary (citable) accession number: D4ANI5

Entry history

Integrated into UniProtKB/TrEMBL:	May 18, 2010
Last sequence update:	May 18, 2010
Last modified:	March 6, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)