Reviewed, UniProtKB/Swiss-Prot A7GPY3 (KYNU_BACCN)

Names and origin

Protein names

Recommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase

Gene names

Name:	kynU
Ordered Locus Names:	Bcer98_1903

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
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: InterPro
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 – 428	428	Kynureninase		PRO_0000356989
Regions
	Region	132 – 135	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	104	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	105	1	Pyridoxal phosphate By similarity
	Binding site	213	1	Pyridoxal phosphate By similarity
	Binding site	216	1	Pyridoxal phosphate By similarity
	Binding site	238	1	Pyridoxal phosphate By similarity
	Binding site	267	1	Pyridoxal phosphate By similarity
	Binding site	295	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	239	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GPY3-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 84577A7CA0A046FA	FASTA	428	48,442
	10 20 30 40 50 60 MDQNPFEASY EYAIQSDKQD ELAAFQNEFY KKADTIYLDG NSLGLLSKRA EKSLLTMLNS 70 80 90 100 110 120 WKEHGIDGWT EGEYPWFFLS EQLSEHIAPL IGALSEEIIV TGSTTTNIHQ VIATFYEPKG 130 140 150 160 170 180 IRTKILADEL TFPSDIYALQ SQIRLKGLDP NEHLVRVKSR DGRTLDEEDI IAAMTDDIAL 190 200 210 220 230 240 ILLPAVLYRS GQILDMKRLT AEAHKRGIHI GFDLCHSIGA IPHQFQEWGV DFAVWCNYKY 250 260 270 280 290 300 LNAGPGSVGG LYVNKKHFAR LPGLSGWFSS RKDKQFDMEH TLTAAEHAGA YQIGTPHIFS 310 320 330 340 350 360 IAPLIGSLEI FKEAGIDRLR QKSLHITRYM LHLIDYELTD KGFTIGNPLE DEKRGGHIYL 370 380 390 400 410 420 EHPEAARICK ALKANGVIPD FRAPNGIRLA PVALYNTYEE VWKSVRILKK IMTNEEYKQF ENKRGVVA

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000764 Genomic DNA. Translation: ABS22191.1.
RefSeq	YP_001375186.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7GPY3.
Genome annotation databases
GeneID	5345277.
GenomeReviews	Gene locus Bcer98_1903 in contig CP000764_GR.
KEGG	bcy:Bcer98_1903.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	NFPTDVY.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 2 hits.
PANTHER	PTHR14084. Kynureninase. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU_BACCN

Accession

Primary (citable) accession number: A7GPY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	September 11, 2007
Last modified:	November 3, 2009
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)