Q8PAD2 (KYNU_XANCP) 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:	XCC1553

Organism

Xanthomonas campestris pv. campestris

Taxonomic identifier

340 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

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.
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 Reference 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 – 424	424	Kynureninase		PRO_0000357018
Regions
	Region	134 – 137	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	106	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	107	1	Pyridoxal phosphate By similarity
	Binding site	219	1	Pyridoxal phosphate By similarity
	Binding site	222	1	Pyridoxal phosphate By similarity
	Binding site	244	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	245	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PAD2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: AFB4C7D41FC3C5AF	FASTA	424	46,200
	10 20 30 40 50 60 MMTDPLSRSH AAALDAADPL RALRDAFVFP QHGGQDQTYF VGNSLGLQPR QARAMVSEVL 70 80 90 100 110 120 DQWGALAVEG HFTGPTQWLT YHQLVRDGLA RVVGAQPDEV VAMNTLTVNL HLMMASFYRP 130 140 150 160 170 180 SAERAAILIE AGAFPSDRHA VESQLRLHGL DPDTHLIEVE PDAADGTLSM DAIAATIAQH 190 200 210 220 230 240 GPRLALVLWP GIQYRTGQAF ALGEIARLAR AQGAAVGFDL AHAVGNIPLS LHDDGVDFAV 250 260 270 280 290 300 WCHYKYLNAG PGAVGGCFVH ARHAHSNLPR MAGWWGHEQP TRFRMEPQFV PSPGAEGWQL 310 320 330 340 350 360 SNPPVLALAP LRASLELFDQ AGMPALRAKS EQLTGHLEQL IHTRVPQVLQ IVTPADPAQR 370 380 390 400 410 420 GCQLSLRVAG GRTQGRALFE YLQSVGVLGD WREPDVIRIA PVPLYNRFCD LHQLVEHVET WAAA

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM40848.1.
RefSeq	NP_636924.2. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8PAD2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	998117.
GenomeReviews	Gene locus XCC1553 in contig AE008922_GR.
KEGG	xcc:XCC1553.
PATRIC	24073904. VBIXanCam115730_1666.
Phylogenomic databases
HOGENOM	HBG523016.
OMA	TAEAHKR.
ProtClustDB	CLSK903751.
Enzyme and pathway databases
BioCyc	XCAM190485:XCC1553-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_XANCP

Accession

Primary (citable) accession number: Q8PAD2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program