C3ZVC9 (C3ZVC9_BRAFL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Kynureninase PIRNR PIRNR038800
EC=3.7.1.3 PIRNR PIRNR038800

Gene names

ORF Names:

BRAFLDRAFT_237019 EMBL EEN43546.1

Organism

Branchiostoma floridae (Florida lancelet) (Amphioxus) [Reference proteome]

Taxonomic identifier

7739 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Cephalochordata › Branchiostomidae › Branchiostoma

Protein attributes

Sequence length	456 AA.
Sequence status	Fragment.
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-kynurenine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 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
Experimental info
	Non-terminal residue	1	1	EMBL EEN43546.1

Sequences

	Sequence		Length	Mass (Da)
	C3ZVC9 [UniParc]. Last modified July 28, 2009. Version 1. Checksum: 8B296AA2D2258AB9	FASTA	456	50,807
	10 20 30 40 50 60 ADVLREKAAA LGCRPEDQAF AVAMDTEDPL RGLREDFHIP KMKDLPPTDP TLVCADDDCV 70 80 90 100 110 120 YMCGNSLGLQ PKGVRKYLEQ DLDYWARYGV FGHFEGPRPW ALCDEYVTEQ SARIVGESNR 130 140 150 160 170 180 GKTVNLHLLL VSFYRPTATR HKILIEGKAF PSDHYAMESQ IRFHGYDPAT SLLLAEPRPG 190 200 210 220 230 240 EQTLRTDDLV SLIEREGDAI AAIVFSGVQY YTGQLFDMET ITRAGHSKGC VVGFDLAHAV 250 260 270 280 290 300 GNAELHLHDW GVDFACWCTY KYMNSGAGGL AGAFVHEKHA AADMPKLLGW WGHKMSTRFR 310 320 330 340 350 360 MDNKLDLSPG VNGFRVSNPP PLLVSPLLAS LDVFQKTTMA DLRRKSVLLT GYLEFLIKKF 370 380 390 400 410 420 YPKPMASEPK EASEDAIRPW VEIITPSDPA QRGCQLSLMF SVPIGAVFKE LERRGVACDK 430 440 450 REPNVLRIAP APLYNSFCDV HRFVSLLGQS LQAAQL

References

[1]

"The amphioxus genome and the evolution of the chordate karyotype." US DOE Joint Genome Institute (JGI-PGF) Putnam N.H., Butts T., Ferrier D.E., Furlong R.F., Hellsten U., Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.K., Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J., Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J. , Kapitonov V.V., Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A., Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T., Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W., Satoh N., Rokhsar D.S. Nature 453:1064-1071(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S238N-H82 EMBL EEN43546.1. Tissue: Testes EMBL EEN43546.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG666688 Genomic DNA. Translation: EEN43546.1.
RefSeq	XP_002587535.1. XM_002587489.1.
3D structure databases
ProteinModelPortal	C3ZVC9.
ModBase	Search...
Protein-protein interaction databases
STRING	7739.JGI237019.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7252149.
KEGG	bfo:BRAFLDRAFT_237019.
Phylogenomic databases
eggNOG	COG3844.
OMA	CHSVGAI.
Enzyme and pathway databases
UniPathway	UPA00253; UER00329. UPA00334; UER00455.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
HAMAP	MF_01970. Kynureninase.
InterPro	IPR000192. Aminotrans_V/Cys_dSase. IPR010111. Kynureninase. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
PANTHER	PTHR14084. PTHR14084. 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

C3ZVC9_BRAFL

Accession

Primary (citable) accession number: C3ZVC9

Entry history

Integrated into UniProtKB/TrEMBL:	July 28, 2009
Last sequence update:	July 28, 2009
Last modified:	May 29, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)