Q1DDU5 (KYNU_MYXXD) 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:	MXAN_0917

Organism

Myxococcus xanthus (strain DK 1622) [Complete proteome] [HAMAP]

Taxonomic identifier

246197 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Myxococcus › Myxococcus xanthus

Protein attributes

Sequence length	426 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 – 426	426	Kynureninase HAMAP-Rule MF_01970		PRO_0000357009
Regions
	Region	138 – 141	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	110	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	111	1	Pyridoxal phosphate By similarity
	Binding site	223	1	Pyridoxal phosphate By similarity
	Binding site	226	1	Pyridoxal phosphate By similarity
	Binding site	248	1	Pyridoxal phosphate By similarity
	Binding site	279	1	Pyridoxal phosphate By similarity
	Binding site	307	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	249	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1DDU5 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: 9F8B6DCA33680072	FASTA	426	47,760
	10 20 30 40 50 60 MTTPYLFEDS ESFARKLDAE DALRGYRDAF HFPPGPDGKP VVYLAGNSLG LQPRNAARYI 70 80 90 100 110 120 QEELEDWARL GVEGHHHGRH PWLHYHELVT EHAARLVGAK PLEVVVMNTL SVNLHLMMVS 130 140 150 160 170 180 FYRPTKQRFK ILVEAGAFPS DQYAVASQVR FHGYDAREAV LELKPREGEE TLRTEDILET 190 200 210 220 230 240 IERHGHEVAL VMLGSVNYLT GQAFDLAAIT KAAHAKGCFV GFDLAHGAGN LRLSLHDDGP 250 260 270 280 290 300 DFAVWCSYKY LNAGPGALGG VFVHERHAHT KDLPRFEGWW GHDKQTRFQM GPTFSALPGA 310 320 330 340 350 360 EGWQLSNPPI FQLAALRASL ELFDQAGMAA LRAKSERLTG YLEFLLDRLP EGFVRITTPR 370 380 390 400 410 420 DVKQRGAQLS LRFRGEPQGL LKRLGDAGII CDFRKPDIIR AAPAPLYNSF TDVYRFVKTL EGHARE

References

[1]

"Evolution of sensory complexity recorded in a myxobacterial genome." Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A. , Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B. Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DK 1622.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000113 Genomic DNA. Translation: ABF87345.1.
RefSeq	YP_629178.1. NC_008095.1.
3D structure databases
ProteinModelPortal	Q1DDU5.
ModBase	Search...
Protein-protein interaction databases
STRING	246197.MXAN_0917.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABF87345; ABF87345; MXAN_0917.
GeneID	4104929.
KEGG	mxa:MXAN_0917.
PATRIC	22644409. VBIMyxXan43560_0907.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3844.
HOGENOM	HOG000242438.
KO	K01556.
OMA	MVSFYRP.
ProtClustDB	CLSK2486953.
Enzyme and pathway databases
BioCyc	MXAN246197:GIWU-905-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_MYXXD

Accession

Primary (citable) accession number: Q1DDU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	July 11, 2006
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program