B2FL97 (KYNU_STRMK) 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:	Smlt3160

Organism

Stenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]

Taxonomic identifier

522373 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Stenotrophomonas › Stenotrophomonas maltophilia group › Stenotrophomonas maltophilia

Protein attributes

Sequence length	424 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. HAMAP-Rule MF_01970
Catalytic activity	L-kynurenine + H2O = anthranilate + L-alanine. HAMAP-Rule MF_01970 L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. HAMAP-Rule MF_01970
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. HAMAP-Rule MF_01970 Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. HAMAP-Rule MF_01970
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	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: 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 – 424	424	Kynureninase HAMAP-Rule MF_01970		PRO_0000357013
Regions
	Region	133 – 136	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	105	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	106	1	Pyridoxal phosphate By similarity
	Binding site	218	1	Pyridoxal phosphate By similarity
	Binding site	221	1	Pyridoxal phosphate By similarity
	Binding site	243	1	Pyridoxal phosphate By similarity
	Binding site	274	1	Pyridoxal phosphate By similarity
	Binding site	302	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	244	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2FL97 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 9B81C2D46958FDC4	FASTA	424	46,800
	10 20 30 40 50 60 MSDLLSRTHA IALDAADPLR PLRNEFLIPR HGGGEQTYFV GNSLGLQPRG AQAAVQEVMK 70 80 90 100 110 120 QWGELAVEGH FTGPTQWLSY HRLVSAQLAR VVGALPSEVV AMNTLSVNLH LMMVSFYRPT 130 140 150 160 170 180 AQRPVILMEA GAFPTDRHAV EAQIRFHGFD PAECLVEVQP DEANGTISLT AIERAIAEHG 190 200 210 220 230 240 PRLALVLWPG VQYRTGQAFD LDAITRAARL QGARIGFDLA HSVGNLPLRL HDVAPDFAVW 250 260 270 280 290 300 CHYKYLNSGP GAVAGAFVHE RHHRDTTLPR FAGWWGHEEA TRFQMAPQFT PAIGAEGWQL 310 320 330 340 350 360 SNPPILGLAP LRASLDLFER AGMEALRSKS LALTGMLEAL VRARLSGVLD IITPAEPQRR 370 380 390 400 410 420 GCQLSLRVIG GRERGRALFE HLRGIGVLGD WREPDVIRIS PTPLYNRYLD VHHFVEEVEA WAGL

References

[1]

"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants." Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B. Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K279a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM743169 Genomic DNA. Translation: CAQ46604.1.
RefSeq	YP_001972895.1. NC_010943.1.
3D structure databases
ProteinModelPortal	B2FL97.
ModBase	Search...
Protein-protein interaction databases
STRING	522373.Smlt3160.
Proteomic databases
PRIDE	B2FL97.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAQ46604; CAQ46604; Smlt3160.
GeneID	6391370.
KEGG	sml:Smlt3160.
PATRIC	23701787. VBISteMal45202_2956.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3844.
HOGENOM	HOG000242438.
KO	K01556.
OMA	MVSFYRP.
ProtClustDB	CLSK903751.
Enzyme and pathway databases
BioCyc	SMAL522373:GJE8-3057-MONOMER.
UniPathway	UPA00253; UER00329. UPA00334; UER00455.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
HAMAP	MF_01970. Kynureninase.
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

KYNU_STRMK

Accession

Primary (citable) accession number: B2FL97

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	June 10, 2008
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program