Reviewed, UniProtKB/Swiss-Prot Q2H7G2 (KYNU2_CHAGB)

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:	BNA5-2
ORF Names:	CHGG_05403

Organism

Chaetomium globosum (Soil fungus) [Complete proteome]

Taxonomic identifier

38033 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Chaetomiaceae › Chaetomium

Protein attributes

Sequence length	539 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.
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 – 539	539	Kynureninase 2		PRO_0000356975
Regions
	Region	199 – 202	4	Pyridoxal phosphate binding By similarity
	Compositional bias	321 – 381	61	Gly-rich
Sites
	Binding site	171	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	172	1	Pyridoxal phosphate By similarity
	Binding site	290	1	Pyridoxal phosphate By similarity
	Binding site	293	1	Pyridoxal phosphate By similarity
	Binding site	315	1	Pyridoxal phosphate By similarity
	Binding site	379	1	Pyridoxal phosphate By similarity
	Binding site	407	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	316	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2H7G2-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 6C22ABAB563342EA	FASTA	539	57,881
	10 20 30 40 50 60 MDTEYQSFVE TLRAGQKPEF PAHAKTIEYA RELDAHDKLS QLRSDFNIPT KGSLRKKALD 70 80 90 100 110 120 GGVAGETKEP RVPNGVSSAT KPNGTVNSDL KDDEASIYFV GNSLGAQPKC IRQYIDAHLE 130 140 150 160 170 180 TWASIGVNGH FTSFDNSPLA SWQDMAAACA AQSVDLVGAK SANEIIYMNT LTVNLHLMMA 190 200 210 220 230 240 SFYRPTAKRH KIIAEWKPFP SDSYALASQL HWHGLAPATS LIEIHPPNPT GSSPPTLTLT 250 260 270 280 290 300 TSHILATIDA HADSTALLLL PGIQYYTGQL FDMARITRHA RARGIVVGWD LAHAVGNVEL 310 320 330 340 350 360 ELHAWGVDFA VWCTYKYLNA GPGALGGVFV HGRHHSFHRG GGGSGGVGGG RGEGGDGDGG 370 380 390 400 410 420 DGGDGDGMAL GYRHRLAGWY GADKAVRFEM EKVFWPAEGA AGWQVSNPSV VDLACVRATL 430 440 450 460 470 480 GMFERVGMRA LRDKAVLLTG YLEWLLLGLL ADGVGKGGDG EAAFRIITPG HPADRGSQLS 490 500 510 520 530 LLLRGGLLEG VSKELADGGV VVDVRKPDVI RVAPVPMYCR FEDVWGFITV FNRALDRCA

References

[1]

"Annotation of the Chaetomium globosum CBS 148.51 genome." Birren B.W., Lander E.S., Galagan J.E., Devon K., Nusbaum C., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., Pushparaj V. , DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Kodira C.D., Yandava C., Zeng Q., Alvarado L., Oleary S., Untereiner W. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 6205 / CBS 148.51 / DSM 1962 / IFO 6347 / NRRL 1970.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH408031 Genomic DNA. Translation: EAQ88784.1.
RefSeq	XP_001221498.1.
3D structure databases
SMR	Q2H7G2. Positions 19-536.
ModBase	Search...
Genome annotation databases
GeneID	4391213.
Phylogenomic databases
OrthoDB	EOG9RZ0G9.
PhylomeDB	Q2H7G2.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU2_CHAGB

Accession

Primary (citable) accession number: Q2H7G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	March 21, 2006
Last modified:	February 9, 2010
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)