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Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)

 H0BFV6_9ACTN            Unreviewed;       405 AA.
H0BFV6;
22-FEB-2012, integrated into UniProtKB/TrEMBL.
22-FEB-2012, sequence version 1.
28-MAR-2018, entry version 37.
RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970};
ORFNames=SPW_4143 {ECO:0000313|EMBL:EHM27420.1};
Streptomyces sp. W007.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1055352 {ECO:0000313|EMBL:EHM27420.1, ECO:0000313|Proteomes:UP000004626};
[1] {ECO:0000313|EMBL:EHM27420.1, ECO:0000313|Proteomes:UP000004626}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=W007 {ECO:0000313|EMBL:EHM27420.1,
ECO:0000313|Proteomes:UP000004626};
PubMed=22374958; DOI=10.1128/JB.06701-11;
Qin S., Zhang H., Li F., Zhu B., Zheng H.;
"Draft Genome Sequence of Marine Streptomyces sp. Strain W007, Which
Produces Angucyclinone Antibiotics with a Benz[a]anthracene
Skeleton.";
J. Bacteriol. 194:1628-1629(2012).
-!- 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_01970, ECO:0000256|PIRNR:PIRNR038800}.
-!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_01970,
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_01970, ECO:0000256|PIRNR:PIRNR038800}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SIMILARITY: Belongs to the kynureninase family.
{ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EHM27420.1}.
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EMBL; AGSW01000147; EHM27420.1; -; Genomic_DNA.
RefSeq; WP_007452920.1; NZ_AGSW01000147.1.
EnsemblBacteria; EHM27420; EHM27420; SPW_4143.
PATRIC; fig|1055352.3.peg.4237; -.
UniPathway; UPA00253; UER00329.
UniPathway; UPA00334; UER00455.
Proteomes; UP000004626; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; -; 2.
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;
Complete proteome {ECO:0000313|Proteomes:UP000004626};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800, ECO:0000313|EMBL:EHM27420.1};
Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
DOMAIN 76 351 Aminotran_5. {ECO:0000259|Pfam:PF00266}.
REGION 132 135 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01970}.
BINDING 103 103 Pyridoxal phosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01970}.
BINDING 104 104 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 201 201 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 204 204 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 226 226 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 256 256 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 282 282 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
MOD_RES 227 227 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_01970}.
SEQUENCE 405 AA; 42789 MW; F61C6CF71F64096B CRC64;
MSETSRDSLR ERALVLDAAD PLAARRKLFA LDDDGVYLDG NSLGALPVHV PARVQDVLTR
QWGELRIRSW DESGWWTAPE RIGDRIAPLV GAAAGQIVVG DSTSVNVFKA VVAAARIAGE
GRDEILVDAT TFPTDGYIAA SAARLTGHRI VPVAPADVPA ALGPRTAAVL LNHVDYRSGR
LHDLPGLTAA VHAAGAVVVW DLCHSAGALP VGLDEHGVDL AVGCTYKYLN GGPGSPAYLY
VAERHQAAFD SPLPGWNSHA DPFGMTPDYA PADGSVRGRV GTPDIVSMLT LEAALDVWDG
VSVDVVRAKS LALTDFFLEC VEAYAPAGRV TSVTPAAHAE RGSQVALRCD GAEPVMRRLI
ERGVVGDLRR PDVLRFGFTP LYVGFADAER AARILAEVLS GDTVG


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