ID A0A0W4ZPL5_PNEC8 Unreviewed; 449 AA. AC A0A0W4ZPL5; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 29-SEP-2021, entry version 25. 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=T552_00780 {ECO:0000313|EMBL:KTW30305.1}; OS Pneumocystis carinii (strain B80) (Rat pneumocystis pneumonia agent) OS (Pneumocystis carinii f. sp. carinii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Pneumocystidomycetes; Pneumocystidaceae; Pneumocystis. OX NCBI_TaxID=1408658 {ECO:0000313|EMBL:KTW30305.1, ECO:0000313|Proteomes:UP000054454}; RN [1] {ECO:0000313|Proteomes:UP000054454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B80 {ECO:0000313|Proteomes:UP000054454}; RX PubMed=26899007; DOI=10.1038/ncomms10740; RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A., RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M., RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K., RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M., RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J., RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W., RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.; RT "Genome analysis of three Pneumocystis species reveals adaptation RT mechanisms to life exclusively in mammalian hosts."; RL Nat. Commun. 7:10740-10740(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. {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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KTW30305.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LFVZ01000003; KTW30305.1; -; Genomic_DNA. DR RefSeq; XP_018227096.1; XM_018369382.1. DR EnsemblFungi; KTW30305; KTW30305; T552_00780. DR GeneID; 28935584; -. DR OrthoDB; 916879at2759; -. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR Proteomes; UP000054454; Unassembled WGS sequence. 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 95..395 FT /note="Aminotran_5" FT /evidence="ECO:0000259|Pfam:PF00266" FT BINDING 129 FT /note="Pyridoxal phosphate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 130 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 213 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 242 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 245 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 267 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 296 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT BINDING 325 FT /note="Pyridoxal phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" FT MOD_RES 268 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03017" SQ SEQUENCE 449 AA; 51316 MW; C53D1C2C01EFC425 CRC64; MYVVMMYIMD YEKVAMQNGF LTAISREFSD YLDEQDSLKE LRNEFELPVQ KNNEDKLCIY MSGNSLGLLS KRIRVLINEE LNVWAKQGVN GHFDHFYGRE WVRIEETVRE ELAKIVGGEK NEVVAMNSLT VNIHFLMASF YKPEGFRRKI LIEDRAFSSD YYAIASHLSW HGLNSETEIL TVSPLKGCYT LTTEHILQTI DKYANEIAMI FFSGVHYYTG QAFDISTITK YAKSKGIIVG WDLAHAIGNI ELKLHDWEVD FAVWCTYKYL NSGPGGIGGI FVHEYHANNR SRLLGWWGND LKTRFNMSNQ QFDSLYGASG FQISNPSVFN MISLLGSLEV FSKVSMSSIR RKSILLTGYL EYLLLTLCSN AYFTIITPSN PEERGAQLSL CFHKDFTQVI FDQLLANGVV VDLRKPDVIR VAPVPLYNTF GEVFDFVCIL KKILDSLTT //