ID A0A173LYY0_9MICO Unreviewed; 415 AA.
AC A0A173LYY0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN ORFNames=AUMI_115100 {ECO:0000313|EMBL:BAV00053.1};
OS Aurantimicrobium minutum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Aurantimicrobium.
OX NCBI_TaxID=708131 {ECO:0000313|EMBL:BAV00053.1, ECO:0000313|Proteomes:UP000243847};
RN [1] {ECO:0000313|EMBL:BAV00053.1, ECO:0000313|Proteomes:UP000243847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNC {ECO:0000313|EMBL:BAV00053.1,
RC ECO:0000313|Proteomes:UP000243847};
RA Nakai R., Fujisawa T., Nakamura Y., Nishide H., Uchiyama I., Baba T.,
RA Toyoda A., Fujiyama A., Naganuma T., Niki H.;
RT "Complete Genome Sequence of Aurantimicrobium minutum Type Strain KNCT, a
RT Planktonic Ultramicrobacterium Isolated from River Water.";
RL Genome Announc. 4:e00616-16(2016).
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|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; EC=3.7.1.3;
CC Evidence={ECO:0000256|PIRNR:PIRNR038800};
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|PIRNR:PIRNR038800};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRNR:PIRNR038800};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-alanine
CC and anthranilate from L-kynurenine: step 1/1.
CC {ECO:0000256|PIRNR:PIRNR038800}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC L-kynurenine: step 2/3. {ECO:0000256|PIRNR:PIRNR038800}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR038800}.
CC -!- SIMILARITY: Belongs to the kynureninase family.
CC {ECO:0000256|PIRNR:PIRNR038800}.
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DR EMBL; AP017457; BAV00053.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A173LYY0; -.
DR KEGG; amin:AUMI_115100; -.
DR OrthoDB; 9812626at2; -.
DR UniPathway; UPA00253; UER00329.
DR UniPathway; UPA00334; UER00455.
DR Proteomes; UP000243847; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0061981; F:3-hydroxykynureninase activity; IEA:RHEA.
DR GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006569; P:tryptophan catabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; KYNURENINASE; 1.
DR PANTHER; PTHR14084:SF0; KYNURENINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF038800; KYNU; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038800};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|PIRNR:PIRNR038800};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR038800};
KW Reference proteome {ECO:0000313|Proteomes:UP000243847}.
FT DOMAIN 126..361
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 415 AA; 45592 MW; 13FF99DF70DF89A8 CRC64;
MTSFETLAAQ LDQSDPLAVH RAKFYGTDEA TRTSTPGMPL AYFDGNSLGR PMQASFDRIE
AFLRHDWGTR LIRSWDEQWL NLPLELGNKI GSAALGAAPG QTFVGDSTSV LLYKMARAAI
AARPGRTEIV LDTDNFPTDR YLLEGIADEL SMTLVWIEAD TSAGVTPEQV SAVVNSNTAL
VLLSHVAYRS GFMADAPAIT KITHDAGALI VWDLSHSVGS VVVELDNWNV DIAVGCSYKY
LCGGPGAPAW AYVRRDLQTQ IEQPIQGWWG TKNMFLMGPG YDPENDLRRF ITGTTPVVGM
QAMIDPVELI GEVSIEAIRA KSLLLTQFVI DYTDEVLAPL GVTVATPRDP AQRGGHVTLN
HPDMREVNAL MWKEDIIPDY RDPHGLRIGL SPLTTSFQEV FLGMERVKET LLSLR
//
