Q5WKB5 (KYNU_BACSK) Reviewed, UniProtKB/Swiss-Prot

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:	ABC0651

Organism

Bacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]

Taxonomic identifier

66692 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	427 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.
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 – 427	427	Kynureninase		PRO_0000356993
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)
	Q5WKB5 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 19F67CEC50D893AC	FASTA	427	48,667
	10 20 30 40 50 60 MPCFDSVYTK EYAQQLDAVD PLARFRNEFY IDEDSIYLDG NSLGLLSTRA EQSLLDVLDS 70 80 90 100 110 120 WKQYGIDGWT KGKHPWFYLS ESLGEKMASL VGAKAEEVIV TGSTTTNLHQ LVSSFFRPEG 130 140 150 160 170 180 KKTKILADEL NFPSDIYALK SQLHLQGFDP EEHLIQVKSD NGHLLNEEDI IAEMKEDIAL 190 200 210 220 230 240 IVLPSVLYRS GQILDMERLT TAAHQRNILI GFDLCHSIGA IPHQLRKWDV DFAFWCTYKH 250 260 270 280 290 300 VNGGPGSVAA LFVNEKHFGR RPGLAGWFSS NKQKQFDMEH TLTPAEHAGA FQIGTPHIFS 310 320 330 340 350 360 IAPLIGSLAI FAEAGIEQIR KKSLKLTDYM MTLIEHELSD YQFTIQNPRD ERRGAHLYIE 370 380 390 400 410 420 HDEAARICKA LKEENVIPDF RSPKGIRLAP VALYNTFKEV WNTIQVLKFI MKEERYKKFK NERDVVA

References

[1]

"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16." Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KSM-K16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006627 Genomic DNA. Translation: BAD63190.1.
RefSeq	YP_174151.1. NC_006582.1.
3D structure databases
ProteinModelPortal	Q5WKB5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5WKB5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000046564; EBBACP00000045325; EBBACG00000046555.
GeneID	3204717.
GenomeReviews	Gene locus ABC0651 in contig AP006627_GR.
KEGG	bcl:ABC0651.
NMPDR	fig|66692.3.peg.789.
PATRIC	18920560. VBIBacCla58185_0685.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3844.
GeneTree	EBGT00050000000895.
HOGENOM	HBG523016.
OMA	TAEAHKR.
ProtClustDB	CLSK904618.
Enzyme and pathway databases
BioCyc	BCLA66692:ABC0651-MONOMER.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	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_BACSK

Accession

Primary (citable) accession number: Q5WKB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program