P83788 (KYNU_PSEFL) 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

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Catalytic activity	L-kynurenine + H2O = anthranilate + L-alanine. Ref.1 L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. Ref.1
Cofactor	Pyridoxal phosphate.
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. Ref.1
Sequence similarities	Belongs to the kynureninase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	3D-structure
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 – 416

416

Kynureninase

PRO_0000357010

Regions

Region

129 – 132

4

Pyridoxal phosphate binding

Sites

Binding site

97

1

Pyridoxal phosphate; via amide nitrogen

Binding site

98

1

Pyridoxal phosphate

Binding site

172

1

Pyridoxal phosphate

Binding site

201

1

Pyridoxal phosphate

Binding site

204

1

Pyridoxal phosphate

Binding site

226

1

Pyridoxal phosphate Probable

Binding site

256

1

Pyridoxal phosphate Probable

Binding site

282

1

Pyridoxal phosphate Probable

Amino acid modifications

Modified residue

227

1

N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis

132

1

D → A: Reduces binding to pyridoxal phosphate and strongly reduces catalytic activity. Ref.1

Mutagenesis

132

1

D → E: Enhances binding to pyridoxal phosphate. Ref.1

Mutagenesis

201

1

D → E: Enhances binding to pyridoxal phosphate. Ref.1

Secondary structure

1

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416

Helix Strand Turn

Details...

Helix

4 – 12

9

Helix

17 – 22

6

Helix

44 – 53

10

Helix

63 – 66

4

Helix

72 – 75

4

Helix

80 – 83

4

Beta strand

91 – 93

3

Helix

97 – 115

19

Beta strand

121 – 125

5

Helix

130 – 136

7

Helix

140 – 143

4

Beta strand

148 – 154

7

Helix

155 – 157

3

Helix

158 – 161

4

Beta strand

166 – 174

9

Helix

184 – 193

10

Beta strand

197 – 201

5

Turn

203 – 205

3

Turn

213 – 215

3

Beta strand

220 – 222

3

Beta strand

238 – 241

4

Turn

243 – 248

6

Helix

276 – 278

3

Helix

285 – 290

6

Helix

298 – 300

3

Helix

303 – 325

23

Helix

338 – 340

3

Beta strand

345 – 348

4

Helix

354 – 360

7

Turn

370 – 372

3

Beta strand

373 – 376

4

Turn

380 – 382

3

Helix

385 – 394

10

Helix

398 – 401

4

Turn

402 – 404

3

Sequences

	Sequence		Length	Mass (Da)
	P83788 [UniParc]. Last modified March 15, 2004. Version 1. Checksum: 50C3DE62A20C779D	FASTA	416	45,905
	10 20 30 40 50 60 MTTRNDCLAL DAQDSLAPLR QQFALPEGVI YLDGNSLGAR PVAALARAQA VIAEEWGNGL 70 80 90 100 110 120 IRSWNSAGWR DLSERLGNRL ATLIGARDGE VVVTDTTSIN LFKVLSAALR VQATRSPERR 130 140 150 160 170 180 VIVTETSNFP TDLYIAEGLA DMLQQGYTLR LVDSPEELPQ AIDQDTAVVM LTHVNYKTGY 190 200 210 220 230 240 MHDMQALTAL SHECGALAIW DLAHSAGAVP VDLHQAGADY AIGCTYKYLN GGPGSQAFVW 250 260 270 280 290 300 VSPQLCDLVP QPLSGWFGHS RQFAMEPRYE PSNGIARYLC GTQPITSLAM VECGLDVFAQ 310 320 330 340 350 360 TDMASLRRKS LALTDLFIEL VEQRCAAHEL TLVTPREHAK RGSHVSFEHP EGYAVIQALI 370 380 390 400 410 DRGVIGDYRE PRIMRFGFTP LYTTFTEVWD AVQILGEILD RKTWAQAQFQ VRHSVT

References

[1]

"Three-dimensional structure of kynureninase from Pseudomonas fluorescens." Momany C., Levdikov V., Blagova L., Lima S., Phillips R.S. Biochemistry 43:1193-1203(2004) [PubMed: 14756555] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, HOMODIMERIZATION, MUTAGENESIS OF ASP-132 AND ASP-201.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QZ9	X-ray	1.85	A	1-416	[»]

ProteinModelPortal

P83788.

SMR

P83788. Positions 2-405.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-7065.

Family and domain databases

InterPro

IPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.

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_PSEFL

Accession

Primary (citable) accession number: P83788

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	March 15, 2004
Last modified:	May 31, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program