Reviewed, UniProtKB/Swiss-Prot A9V3C0 (KYNU_MONBE)

Names and origin

Protein names

Recommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase

Gene names

Name:	kynu
ORF Names:	26773

Organism

Monosiga brevicollis (Choanoflagellate) [Complete proteome]

Taxonomic identifier

81824 [NCBI]

Taxonomic lineage

Eukaryota › Choanoflagellida › Codonosigidae › Monosiga

Protein attributes

Sequence length	460 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.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
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: UniProtKB-SubCell
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 – 460	460	Kynureninase		PRO_0000361087
Regions
	Region	165 – 168	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	127	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	128	1	Pyridoxal phosphate By similarity
	Binding site	249	1	Pyridoxal phosphate By similarity
	Binding site	252	1	Pyridoxal phosphate By similarity
	Binding site	274	1	Pyridoxal phosphate By similarity
	Binding site	304	1	Pyridoxal phosphate By similarity
	Binding site	332	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	275	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9V3C0-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 8ED7320A036A9BDE	FASTA	460	51,259
	10 20 30 40 50 60 MHLARELGVN LADQRLAQAL DEADPLAHLR QEFSIPQMKD IKQADLKLVE AESDCIYLCG 70 80 90 100 110 120 NSLGLMPKRT RTIVNEELDT WATGGVTGHF PDGPGKRPWV SIDETVTDKC ARVVGALPEE 130 140 150 160 170 180 VAIMNTLTVN LHLLMVSLAH TMARQVPFYR PTSDRFKILV EAKAFPSDHF AVLSQLRMHG 190 200 210 220 230 240 HDESALIEVK PREGEHNIRE EDLLAILEEQ GDSIATVLVG GVHYYTGQFF DLQRLCAAAH 250 260 270 280 290 300 NKGCTFGVDL AHAVGNVPLQ LHDWDIDFAC WCTYKYLNSG PGGIAGAFIH KKHEGTSRPY 310 320 330 340 350 360 LQGWWGVQLN ERFRMDHDAS FMPGVRGLQL SNPGVLQTVA LLGSLEIYEQ TDMASLRAKS 370 380 390 400 410 420 LKLTAYLEQL MQALVNEEGH APRFEIITPT DPERRGCQLS ILFKVDIDAA FEALEKRGVV 430 440 450 460 CDVRRPDVMR IAPVPLYNTF TDVYRFVTTL RDALNASASS

References

[1]

"The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans." JGI Sequencing King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J., Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D., Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M. , Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S., Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T., McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D. Nature 451:783-788(2008) [PubMed: 18273011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MX1 / ATCC 50154.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH991556 Genomic DNA. Translation: EDQ88034.1.
RefSeq	XP_001747110.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5892477.
KEGG	mbr:MONBRDRAFT_26773.
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_MONBE

Accession

Primary (citable) accession number: A9V3C0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	February 5, 2008
Last modified:	September 22, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)