A4I2F1 (A4I2F1_LEIIN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Kynureninase PIRNR PIRNR038800
EC=3.7.1.3 PIRNR PIRNR038800

Gene names

ORF Names:

LINJ_26_2250 EMBL CAM68941.1

Organism

Leishmania infantum

Taxonomic identifier

5671 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Leishmania

Protein attributes

Sequence length	468 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. PIRNR PIRNR038800
Catalytic activity	L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800 L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800
Cofactor	Pyridoxal phosphate By similarity. PIRNR PIRNR038800
Pathway	Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800 Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800
Subunit structure	Homodimer By similarity. PIRNR PIRNR038800
Subcellular location	Cytoplasm By similarity PIRNR PIRNR038800.
Sequence similarities	Belongs to the kynureninase family. PIRNR PIRNR038800

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis PIRNR PIRNR038800
Cellular component	Cytoplasm PIRNR PIRNR038800
Ligand	Pyridoxal phosphate PIRNR PIRNR038800
Molecular function	Hydrolase PIRNR PIRNR038800 EMBL CAM68941.1
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: UniProtKB-SubCell
Molecular function	kynureninase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A4I2F1 [UniParc]. Last modified May 1, 2007. Version 1. Checksum: 472636B6D3CD0F8D	FASTA	468	50,696
	10 20 30 40 50 60 MRNAAAETLL STVSTTGMAL TEDGFAEYMD EADPLREHRS SYHIPMMRDG TQFSYFAGNA 70 80 90 100 110 120 LGPQHVGVEA SMAAFLKKWR EQAVEGHLMQ PTPWFEIDQM CVKDMAAIVG AKDTEVAIMN 130 140 150 160 170 180 TPTVNLHLLL STFYHSQGSK KKIMIDPHSF PSDGYCLLSQ LETRGLNPAE DLIKITAPGT 190 200 210 220 230 240 KDWNGPVTAI PMEAFLSAID KRGDETAVII VSAVQHLTGQ WLDIPAIVKA AHAKKILVGV 250 260 270 280 290 300 DCAHAVGNVP LHLHDWDVDF AFWCTCKYLS SGPGSIGGVF VHNKHTSGAI PLNHLSRRWG 310 320 330 340 350 360 SEIQSCFPKH HSLEPATGAS ELHISTPSAA CYMILAPSLK LMASVGMEAI RQKSLLLTAY 370 380 390 400 410 420 LELLLSELVP PGCIEIVTPA DPNQRGAQLS LRILPNKLKS GQAAAPGYQC GAGGADEMDD 430 440 450 460 ASLLQRQLLD EGVMIHRCSP DVVPVAPAPM YNSFADVLRA VRIIASLF

References

[1]

"Comparative genomic analysis of three Leishmania species that cause diverse human disease." Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., Fraser A., Rajandream M.-A., Carver T., Norbertczak H., Chillingworth T., Hance Z. , Jagels K., Moule S., Ormond D., Rutter S., Sqaures R., Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S., Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P., Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R.O., Barrell B., Cruz A.K., Mottram J.C., Smith D.F., Berriman M. Nat. Genet. 39:839-847(2007) [PubMed: 17572675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	FR796458 Genomic DNA. Translation: CAM68941.1.
RefSeq	XP_001470562.1. XM_001470525.1.
3D structure databases
ProteinModelPortal	A4I2F1.
ModBase	Search...
Protein-protein interaction databases
STRING	A4I2F1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5069937.
KEGG	lif:LINJ_26_2250.
Phylogenomic databases
eggNOG	KOG3846.
HOGENOM	HBG523016.
OMA	TAEAHKR.
PhylomeDB	A4I2F1.
ProtClustDB	CLSZ2430281.
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.
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

A4I2F1_LEIIN

Accession

Primary (citable) accession number: A4I2F1

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2007
Last sequence update:	May 1, 2007
Last modified:	December 14, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)