Reviewed, UniProtKB/Swiss-Prot Q1DZA6 (KYNU_COCIM)

Names and origin

Protein names

Recommended name:
    Kynureninase
    EC=3.7.1.3
Alternative name(s):
    L-kynurenine hydrolase
    Biosynthesis of nicotinic acid protein 5

Gene names

Name:	BNA5
ORF Names:	CIMG_04357

Organism

Coccidioides immitis (Valley fever fungus) [Complete proteome]

Taxonomic identifier

5501 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Coccidioides

Protein attributes

Sequence length	480 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.
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 – 480	480	Kynureninase		PRO_0000360868
Regions
	Region	166 – 169	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	138	1	Pyridoxal phosphate; via amide nitrogen By similarity
	Binding site	139	1	Pyridoxal phosphate By similarity
	Binding site	252	1	Pyridoxal phosphate By similarity
	Binding site	255	1	Pyridoxal phosphate By similarity
	Binding site	277	1	Pyridoxal phosphate By similarity
	Binding site	315	1	Pyridoxal phosphate By similarity
	Binding site	343	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	278	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1DZA6-1 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: BDB23F5C91D5D94E	FASTA	480	53,525
	10 20 30 40 50 60 MVDSSKAPLP FRDSALSFKR EYAESLDAQD PLREFRNQFI IPSKADLKRK SLAVAEGESP 70 80 90 100 110 120 SSDCIYLCGN SLGLQPKNAR MYIDRFLQTW ATKAVLGHFT KLEDSPFPPY MDYDDVTSKL 130 140 150 160 170 180 MAQVVGALPS EVAVMSTLTG NLHLLMASFY RPTKEKYKII LEGKAFPSDH YAVESQIRHH 190 200 210 220 230 240 GFDPKDAMVL IEPKDLKEPV LPTERILKTI DEHASSTALI LLPGIQYYSG QYLDIPTITA 250 260 270 280 290 300 HAHSKGLLIG WDCAHAAGNV ELKLHDWDVD FAAWCTYKYV NSGPGSMGAL FVHEKHGQVN 310 320 330 340 350 360 LENKEDPYRH RLTGWWGGDK SLRFLMDNNF VPRPGAAGFQ LSNPSVLDMT AVLSSLDIFD 370 380 390 400 410 420 KATMPALRKK SLELTAYLEH LLLNSPEGVR PSDDPFSIIT PSDPEARGAQ LSVLLKPGLL 430 440 450 460 470 480 DSVFSHLVDN GVILDERKPD VIRVAPAPLY NTFTDVWDFV QIFFDACRKA AQEKDTTSHG

References

[1]

"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives." Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W. Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH476727 Genomic DNA. Translation: EAS33333.1.
RefSeq	XP_001244916.1.
3D structure databases
SMR	Q1DZA6. Positions 18-466.
ModBase	Search...
Genome annotation databases
GeneID	4564403.
Phylogenomic databases
OrthoDB	EOG9RZ0G9.
PhylomeDB	Q1DZA6.
Family and domain databases
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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_COCIM

Accession

Primary (citable) accession number: Q1DZA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	July 11, 2006
Last modified:	February 9, 2010
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)