Reviewed, UniProtKB/Swiss-Prot A0M4Y1 (KYNU_GRAFK)

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:	GFO_2720

Organism

Gramella forsetii (strain KT0803) [Complete proteome] [HAMAP]

Taxonomic identifier

411154 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length	425 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 – 425	425	Kynureninase		PRO_0000357008
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	274	1	Pyridoxal phosphate By similarity
	Binding site	302	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	244	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0M4Y1-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 15B0BFA75F3E2AD1	FASTA	425	49,068
	10 20 30 40 50 60 MQFENTREFA KKLDNEDKIS KYRDEFIFPK VNGKDVIYFV GNSLGLQPKT ARKYVDEVMK 70 80 90 100 110 120 DWAELAVEGH FYAEKSWWDY HERFSEKLAR VVGANPSEVT VMNTLTVNLH LLMVSFYRPS 130 140 150 160 170 180 GKRYKIICEE KAFPSDQYMI SSQVRFHGYE PSDAIVEIMK REGENNFRTE DILKKIEEVG 190 200 210 220 230 240 EECALVLIGG VNYYTGQVFD METITKAGHD IGAFVGWDLA HGAGNIELKL SEWNVDFAAW 250 260 270 280 290 300 CSYKYMNSGP GNASGCFINK KYHNKKDIPR FEGWWGHNKE RRFLMEPEFQ PEPTADAWQI 310 320 330 340 350 360 SNAPILALAP YLASLEMFDE VGMPALIEKR NKIVAYLEFV LHEIDEEVDS SFEIITPADQ 370 380 390 400 410 420 NERGTQLSVF LHGEGKELFR YLMDQGVITD WREPNVIRLA PAPFYCSFED MYEFGQILKK GILSK

References

[1]

"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter." Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O. Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU207366 Genomic DNA. Translation: CAL67676.1.
RefSeq	YP_862743.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A0M4Y1.
Genome annotation databases
GeneID	4650934.
GenomeReviews	Gene locus GFO_2720 in contig CU207366_GR.
KEGG	gfo:GFO_2720.
NMPDR	fig|411154.5.peg.2570.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	WQPLSGW.
Family and domain databases
InterPro	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.
TIGRFAMs	TIGR01814. kynureninase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KYNU_GRAFK

Accession

Primary (citable) accession number: A0M4Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	December 12, 2006
Last modified:	November 3, 2009
This is version 22 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)