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Kynureninase (EC 3.7.1.3) (Biosynthesis of nicotinic acid protein 5) (L-kynurenine hydrolase)

 F7VS63_SORMK            Unreviewed;       495 AA.
F7VS63;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
05-DEC-2018, entry version 48.
RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000256|HAMAP-Rule:MF_03017};
AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
Name=BNA5 {ECO:0000256|HAMAP-Rule:MF_03017};
ORFNames=SMAC_01897 {ECO:0000313|EMBL:CCC08349.1};
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) /
K-hell).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Sordaria.
NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC08349.1, ECO:0000313|Proteomes:UP000001881};
[1] {ECO:0000313|EMBL:CCC08349.1, ECO:0000313|Proteomes:UP000001881}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
{ECO:0000313|Proteomes:UP000001881};
TISSUE=Mycelium {ECO:0000313|EMBL:CCC08349.1};
PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D.,
Poeggeler S., Read N., Seiler S., Smith K., Zickler D., Kueck U.,
Freitag M.;
"De novo assembly of a 40 Mb eukaryotic genome from short sequence
reads: Sordaria macrospora, a model organism for fungal
morphogenesis.";
PLoS Genet. 6:E1000891-E1000891(2010).
-!- 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.
{ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
-!- CATALYTIC ACTIVITY:
Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate +
H(+) + L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972,
ChEBI:CHEBI:58125; EC=3.7.1.3; Evidence={ECO:0000256|HAMAP-
Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine;
Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972;
EC=3.7.1.3; Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
-!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
alanine and anthranilate from L-kynurenine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SIMILARITY: Belongs to the kynureninase family.
{ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03017}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:CCC08349.1}.
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EMBL; CABT02000005; CCC08349.1; -; Genomic_DNA.
RefSeq; XP_003348873.1; XM_003348825.1.
ProteinModelPortal; F7VS63; -.
STRING; 771870.XP_003348873.1; -.
EnsemblFungi; CCC08349; CCC08349; SMAC_01897.
GeneID; 10806334; -.
KEGG; smp:SMAC_01897; -.
EuPathDB; FungiDB:SMAC_01897; -.
eggNOG; KOG3846; Eukaryota.
eggNOG; COG3844; LUCA.
InParanoid; F7VS63; -.
KO; K01556; -.
OrthoDB; EOG092C20ON; -.
UniPathway; UPA00253; UER00329.
UniPathway; UPA00334; UER00455.
Proteomes; UP000001881; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_01970; Kynureninase; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR010111; Kynureninase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
PANTHER; PTHR14084; PTHR14084; 1.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF038800; KYNU; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR01814; kynureninase; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000001881};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03017,
ECO:0000256|PIRNR:PIRNR038800};
Reference proteome {ECO:0000313|Proteomes:UP000001881}.
DOMAIN 92 311 Aminotran_5. {ECO:0000259|Pfam:PF00266}.
REGION 185 188 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_03017}.
COILED 22 42 {ECO:0000256|SAM:Coils}.
BINDING 156 156 Pyridoxal phosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03017}.
BINDING 157 157 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 270 270 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 273 273 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 295 295 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 337 337 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
BINDING 365 365 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_03017}.
MOD_RES 296 296 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_03017}.
SEQUENCE 495 AA; 54196 MW; 76235340CF95BE8C CRC64;
MTASSWPTNN DNHPTNSPAK WKNMSTAAVQ DARKQAEALD NEDPIAFIRD EFNIPTKAQI
ASSRLADSHP AALPASKDDA KSVYLCGNSL GVQPKRTVTR LNQYLTTWAT QGVQGHFKPL
EESPLPTWLD ADAKAAELIA PVVGADVSEV AVMQTLTANI HLLMSAFYRP DINNRHKVIL
ENKAFPSDHF VVETQIRHHS LSTEKSMVLI DSSSKDNIIT TQEILSVISA HADTTALLLL
PGIQYYTGQL LDIPAITAFA HKHGIFVIWD LAHAVGNVPL YLHDWGVDAA AWCSYKYLNG
GPGCIGGLFV HTNNSIVTKE ITDEKPEEGY SNRLAGWWGN DKKTRFVMAN KFHPVAGAAG
FQLSNPSILD ITSLSASLEI FQEAGGMEAL RSKSLKLTNF LEATLGGMKE EDRAHFRIIT
PSKPEERGAQ LSLMLSDGLL DTVMKELEAR GVIVDERRPN VIRVAPAPLY NTFSDCVQFV
EAFSAALEAA TKRAL


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