Kynureninase - Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast)

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Q6BI19 (KYNU_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 50. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Kynureninase
EC=3.7.1.3

Alternative name(s):
Biosynthesis of nicotinic acid protein 5
L-kynurenine hydrolase

Gene names

Name:	BNA5
Ordered Locus Names:	DEHA2G14080g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length	460 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

460

Kynureninase

PRO_0000218662

Regions

Region

4

Pyridoxal phosphate binding By similarity

Sites

Binding site

1

Pyridoxal phosphate; via amide nitrogen By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Binding site

1

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

1

N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6BI19 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 56DB4A0D03FBFF9C
Show »

460

52,093

        10         20         30         40         50         60 
MSIEQAKKLD ECFPTYKEEF EIPTFKSLGI QNDEYEDSTD SIYLCGNSLG LMPKITRTAI 

        70         80         90        100        110        120 
NDELNAWSER GVESHFRHPG EEKGLTSWVD IDLPLLPLIA PIVGGKENEV AVMGTLTSNL 

       130        140        150        160        170        180 
NAMLMSFYKP SGKKTKILFE KQAFPSDYYA FLNAAKIFGY NEDHLIQIEI KEGKTYIETE 

       190        200        210        220        230        240 
DIIETITNHQ DELALVCFSG IQYYTGQFFN IGEITECAKS FGITVGWDLA HAVGNVPLQL 

       250        260        270        280        290        300 
HDWDVDFAVW CSYKYLNSGP GGIAGIFVHE KHTKDNSIEQ FKPRLAGWWG NNASDRFKML 

       310        320        330        340        350        360 
EVFDPIKSAL SYRQSNPSVI DVVAVKSSLE LFKKVGGISE LRKKSVELTG FLQALLTSSK 

       370        380        390        400        410        420 
YYIKQEETTD RLGFKILSPL NKGDRGCQLS VLFQPHYEEY SKNIMERVNK YLSDHAIVCD 

       430        440        450        460 
ERRPDVIRLA PLPLYNTFSE TFIAVQRLIE AMDKIAANEI

References

[1]

"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.

expand/collapse author list

Souciet J.-L.
Nature 430:35-44(2004) [PubMed: 15229592] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382139 Genomic DNA. Translation: CAG90638.1.
RefSeq	XP_462152.1. XM_462152.1.
3D structure databases
ProteinModelPortal	Q6BI19.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6BI19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2905066.
GenomeReviews	Gene locus DEHA2G14080g in contig CR382139_GR.
KEGG	dha:DEHA2G14080g.
Phylogenomic databases
eggNOG	fuNOG06509.
HOGENOM	HBG523016.
OMA	TAEAHKR.
OrthoDB	EOG4TB7KQ.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K01556.
PANTHER	PTHR14084. Kynureninase. 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

KYNU_DEBHA

Accession

Primary (citable) accession number: Q6BI19

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	August 16, 2004
Last modified:	December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents