A6H1P7 (KYNU_FLAPJ) 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:	FP2215

Organism

Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511) [Reference proteome] [HAMAP]

Taxonomic identifier

402612 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium › Flavobacterium psychrophilum

Protein attributes

Sequence length	425 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. HAMAP-Rule MF_01970
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. HAMAP-Rule MF_01970
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	Complete proteome Reference 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 – 425	425	Kynureninase HAMAP-Rule MF_01970		PRO_0000357006
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)
	A6H1P7 [UniParc]. Last modified July 24, 2007. Version 1. Checksum: 43111D4A09B97240	FASTA	425	49,035
	10 20 30 40 50 60 MIFQNTLEFA QQLDNQDELK EYKNEFIFPQ HEGKNVIYFT GNSLGLQPKS ARNYVDEVMN 70 80 90 100 110 120 DWANLAVEGH FYADKPWWDY QERFANPLSK IVGAKPLEVT VMNTLTVNLH LLMVSFYRPT 130 140 150 160 170 180 KKRYKIICEE KAFPSDQYMF QSQVNFHGYK PEDAIVEIKR REGEHNIRLE DILSKIEAVG 190 200 210 220 230 240 DELALVLFGG VNYYTGQVFD MKTITEAGHK QGAKVGFDLA HAAGNIKLEL HDWNVDFAAW 250 260 270 280 290 300 CSYKYMNSGP GNASGCFVHE KHHSDSNLPR FAGWWGHNKE RRFKMEPTFD PVHGADGWQI 310 320 330 340 350 360 SNLPILSLAP YLASVEMFAE VGIEKLIRKR NQITAYLEFI LHEIDKEVKG HFEILTPTNQ 370 380 390 400 410 420 EERACQLSVF LHGEGRSLFD YLMKNGVVTD WREPNVIRLA PVPLYCSFED MYNFGQILKK GILEN

References

[1]

"Complete genome sequence of the fish pathogen Flavobacterium psychrophilum." Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B., Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F., Claverol S., Dumetz F., Le Henaff M., Benmansour A. Nat. Biotechnol. 25:763-769(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JIP02/86 / ATCC 49511.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM398681 Genomic DNA. Translation: CAL44271.1.
RefSeq	YP_001297072.1. NC_009613.1.
3D structure databases
ProteinModelPortal	A6H1P7.
ModBase	Search...
Protein-protein interaction databases
STRING	402612.FP2215.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL44271; CAL44271; FP2215.
GeneID	5300761.
KEGG	fps:FP2215.
PATRIC	21909450. VBIFlaPsy4505_2262.
Phylogenomic databases
eggNOG	COG3844.
HOGENOM	HOG000242438.
KO	K01556.
OMA	MVSFYRP.
ProtClustDB	CLSK2487569.
Enzyme and pathway databases
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_FLAPJ

Accession

Primary (citable) accession number: A6H1P7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	July 24, 2007
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program