A4XAL2 (KYNU_SALTO) 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:	Strop_3530

Organism

Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP]

Taxonomic identifier

369723 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micromonosporineae › Micromonosporaceae › Salinispora

Protein attributes

Sequence length	429 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 – 429	429	Kynureninase		PRO_0000357011
Regions
	Region	137 – 140	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	109	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	110	1	Pyridoxal phosphate By similarity
	Binding site	222	1	Pyridoxal phosphate By similarity
	Binding site	225	1	Pyridoxal phosphate By similarity
	Binding site	247	1	Pyridoxal phosphate By similarity
	Binding site	278	1	Pyridoxal phosphate By similarity
	Binding site	306	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	248	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4XAL2 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: 49393A089963E960	FASTA	429	46,976
	10 20 30 40 50 60 MREEELIQEE KAANRLDTAD PGHRHLFHVP PADGGRYQQA AYLAGNSLGL QPRATRDELF 70 80 90 100 110 120 ADLEAWRRLG VEGHLAADRP WLPYHELLTA PTARLVGARP AEVVVMNSLT VNLHLLMVSF 130 140 150 160 170 180 YRPTGVRTRI VIEDSAFPSD SYAVRSQARF HGLDPDSTVV RLAPRPGEDT LRTADVRDLL 190 200 210 220 230 240 AAEGDTIALV LLGGVNYLTG ELMEIPEITA AGRAAGAVVG WDLAHAAGNV PLALHDWDVD 250 260 270 280 290 300 FAAWCSYKYL NSGPGGLSGV FVHERHLADP TLPRFEGWWS TEAATRFEMS PVARPPATAE 310 320 330 340 350 360 AWQVSNPPIL AMGPVRTSLE VFDSVGMTAL RERSVRLTGY LEWLLDQVTP GRPLAVVTPR 370 380 390 400 410 420 DPDRRGAQLS VRIGTGSAAE LAKRLRLEHG VVADAREPDV VRFAPVPLYS TYHDCWRVAD ALAATVEVH

References

[1]

"Complete sequence of Salinispora tropica CNB-440." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000667 Genomic DNA. Translation: ABP55961.1.
RefSeq	YP_001160339.1. NC_009380.1.
3D structure databases
ProteinModelPortal	A4XAL2.
ModBase	Search...
Protein-protein interaction databases
STRING	A4XAL2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5060004.
GenomeReviews	Gene locus Strop_3530 in contig CP000667_GR.
KEGG	stp:Strop_3530.
PATRIC	23446224. VBISalTro43511_3644.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3844.
HOGENOM	HBG523016.
OMA	TAEAHKR.
PhylomeDB	A4XAL2.
ProtClustDB	CLSK2459168.
Enzyme and pathway databases
BioCyc	STRO369723:STROP_3530-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_SALTO

Accession

Primary (citable) accession number: A4XAL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	May 29, 2007
Last modified:	December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program