ID   A0A6A7BSS5_9PEZI        Unreviewed;       511 AA.
AC   A0A6A7BSS5;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   29-SEP-2021, entry version 6.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 5 {ECO:0000256|HAMAP-Rule:MF_03017};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_03017};
GN   Name=BNA5 {ECO:0000256|HAMAP-Rule:MF_03017};
GN   ORFNames=K470DRAFT_259878 {ECO:0000313|EMBL:KAF2858376.1};
OS   Piedraia hortae CBS 480.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Capnodiales; Piedraiaceae; Piedraia.
OX   NCBI_TaxID=1314780 {ECO:0000313|EMBL:KAF2858376.1};
RN   [1] {ECO:0000313|EMBL:KAF2858376.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 480.64 {ECO:0000313|EMBL:KAF2858376.1};
RA   Haridas S., Albert R., Binder M., Bloem J., LaButti K., Salamov A.,
RA   Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA   Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA   Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA   Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA   Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA   Grigoriev I.;
RT   "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT   emergence of pathogens.";
RL   Stud. Mycol. 0:0-0(2020).
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. {ECO:0000256|HAMAP-
CC       Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + H(+) +
CC         L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:58125; Evidence={ECO:0000256|HAMAP-Rule:MF_03017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine;
CC         Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972; EC=3.7.1.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
CC         ECO:0000256|PIRNR:PIRNR038800};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03017,
CC         ECO:0000256|PIRNR:PIRNR038800};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine
CC       and anthranilate from L-kynurenine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family. {ECO:0000256|HAMAP-
CC       Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03017}.
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DR   EMBL; MU006011; KAF2858376.1; -; Genomic_DNA.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA.
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.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03017, ECO:0000256|PIRNR:PIRNR038800};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03017};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_03017};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_03017}.
FT   DOMAIN          155..418
FT                   /note="Aminotran_5"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..212
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   COMPBIAS        88..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         181
FT                   /note="Pyridoxal phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   BINDING         182
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   BINDING         295
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   BINDING         298
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   BINDING         320
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   BINDING         353
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   BINDING         381
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03017"
SQ   SEQUENCE   511 AA;  57901 MW;  24DC1FBE3D2235B7 CRC64;
     MQVPEQANGD AMDVTYPDDS SDESHVVPET ANAEIAEITA RLRRGEPAGW PERGQRCSYS
     RELDALDPLR HLRKQFLIPS TDSYNKTKLE DTVPDDFTGS ESEERSATYL SGNSLGVQPK
     AVRRYIDNQL ETWASIGVHG HSRLMENSPL MPWLDMAERC SRQTAPLVGA QPHEIIYMNS
     LSVNLHLMMF SFYKPEGRKT KILCEWRPFP SDFYVIESQL RIRGMENITD HIITVRPVNE
     DSYLSTADIL QKIEANSGEL ALILLPGVQY YTGQVLDMAR ITAFARNRRI PIGWDLAHAV
     GNVELSLHDW DVDFACWCSY KYLNAGPGAI SGVFVHDRHG QVQPRYRPRL TGWYGHERST
     RFDMDNIFRP TPGAAGYQIS NPSAMDLAIL SAALTAFEHT SMKALRDKSL LLTSYTEHLL
     ELTLAKCPQP YPPFRIITPR DARERGAQLS LLFHHDWFDV TAECLERHSI ACDKRKPNVI
     RVAPVALYNN FKEVDYFVNV VALALGSRFP S
//