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Database: UniProt/TrEMBL
Entry: M9TU90_9ACTN
LinkDB: M9TU90_9ACTN
Original site: M9TU90_9ACTN 
ID   M9TU90_9ACTN            Unreviewed;       398 AA.
AC   M9TU90;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-SEP-2017, entry version 31.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970};
GN   ORFNames=F750_3385 {ECO:0000313|EMBL:AGJ55852.1};
OS   Streptomyces sp. PAMC 26508.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1265601 {ECO:0000313|EMBL:AGJ55852.1, ECO:0000313|Proteomes:UP000012995};
RN   [1] {ECO:0000313|EMBL:AGJ55852.1, ECO:0000313|Proteomes:UP000012995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC26508 {ECO:0000313|EMBL:AGJ55852.1,
RC   ECO:0000313|Proteomes:UP000012995};
RA   Shin S.C., Park H.;
RT   "Genome sequence of Streptomyces sp. PAMC26508, isolated from
RT   Antarctic lichen Cladonia borealis.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-
CC       hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-
CC       hydroxyanthranilic acid (3-OHAA), respectively.
CC       {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01970,
CC         ECO:0000256|PIRNR:PIRNR038800};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
CC       alanine and anthranilate from L-kynurenine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}.
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DR   EMBL; CP003990; AGJ55852.1; -; Genomic_DNA.
DR   RefSeq; WP_014155399.1; NC_021055.1.
DR   ProteinModelPortal; M9TU90; -.
DR   EnsemblBacteria; AGJ55852; AGJ55852; F750_3385.
DR   KEGG; strp:F750_3385; -.
DR   PATRIC; fig|1265601.4.peg.3220; -.
DR   KO; K01556; -.
DR   OrthoDB; POG091H0D63; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000012995; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR   GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01970; Kynureninase; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010111; Kynureninase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR14084; PTHR14084; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF038800; KYNU; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01814; kynureninase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000012995};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800, ECO:0000313|EMBL:AGJ55852.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800}.
FT   DOMAIN       30    361       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      126    129       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING      97     97       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING      98     98       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     195    195       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     198    198       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     220    220       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     250    250       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     276    276       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     221    221       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   398 AA;  42310 MW;  55D8FBF4E193BACD CRC64;
     MSDLEERAEA LDSADGLAAL RELFTLDDTV YLDGNSLGAL PRHVPARMQD VITREWGSLR
     IRSWDESGWW TAPERIGDRI APLVGAAAGQ IVVGDSTSVN VFKAVVAASR LADEGRDEIL
     VDATTFPTDG YIAGSAARMT GHRVVPVDPA EVRGALGPRT AVVLLNHVDF RTGRLHDLPG
     LTAAVHEAGA LAVWDLCHSA GALPVGLDAH GVDLAVGCTY KYLNGGPGSP AYLYVAERHQ
     TAFDSPLPGW TSHADPFAMS PGYAPAEGSV RGRVGTPDIL SMLALEAALD VWDGVSVDAV
     RAKSLALTDF FLECVAAYVP EGRVVPVTPA AHEERGSQVS LRCENADETE AVMRALTERG
     VVGDLRRPDI LRFGFTPLYV GFADAERAAR ILAEVLAV
//
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