Reviewed, UniProtKB/Swiss-Prot Q3BV40 (KYNU_XANC5)

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:	XCV1642

Organism

Xanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]

Taxonomic identifier

316273 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 – 423	423	Kynureninase		PRO_0000357015
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	273	1	Pyridoxal phosphate By similarity
	Binding site	301	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	244	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3BV40-1 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: FF6D735827C0EC09	FASTA	423	45,937
	10 20 30 40 50 60 MTDLLSRAHA VALDAADPLR GLRDAFVFPQ HGDDDQTYFV GNSLGLQPRA ARAMVDEVLD 70 80 90 100 110 120 RWGALAVEGH FTGPTQWLTY HQLVRDGLAR VVGAQPGEVV AMNTLSVNLH LMMASFYRPT 130 140 150 160 170 180 AERGAILIEA GAFPSDRHAV ESQLRLHGLD PATHLIEVDA DEPNGTVSMT AIAEAIAQHG 190 200 210 220 230 240 PRLALVLWPG IQYRTGQAFD LAEIVRLARA QGAAVGFDLA HAVGNLPLTL HDDGVDFAVW 250 260 270 280 290 300 CHYKYLNAGP GAVGGCFVHA RHANSDLPRM AGWWGHEQQT RFRMDPQFVP SPGAEGWQLS 310 320 330 340 350 360 NPPVLALAPL RASLALFDQA GMAALRAKSE QLTGHLEQLI HARVPQALQI VTPAEPARRG 370 380 390 400 410 420 CQLSLRVAGG RARGRALFEH LHAAGVLGDW REPDVIRIAP VPLYNRFSDL HTFVEQVEAW AAA

References

[1]

"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence." Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O. J. Bacteriol. 187:7254-7266(2005) [PubMed: 16237009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM039952 Genomic DNA. Translation: CAJ23317.1.
RefSeq	YP_363373.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q3BV40.
Genome annotation databases
GeneID	3731276.
GenomeReviews	Gene locus XCV1642 in contig AM039952_GR.
KEGG	xcv:XCV1642.
NMPDR	fig|316273.3.peg.1705.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3BV40.
OMA	WQPLSGW.
Enzyme and pathway databases
BioCyc	XCAM316273:XCV1642-MON.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR14084. Kynureninase. 1 hit.
Pfam	PF00266. Aminotran_5. 1 hit. [Graphical view]
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU_XANC5

Accession

Primary (citable) accession number: Q3BV40

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 22, 2005
Last modified:	November 3, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)