ID   A0A137Q1C1_9AGAR        Unreviewed;       720 AA.
AC   A0A137Q1C1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Phenylalanine ammonia-lyase {ECO:0000313|EMBL:KXN81031.1};
GN   ORFNames=AN958_06277 {ECO:0000313|EMBL:KXN81031.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN81031.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN81031.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN81031.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR   EMBL; KQ963538; KXN81031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137Q1C1; -.
DR   STRING; 1714833.A0A137Q1C1; -.
DR   OrthoDB; 1030318at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016841; F:ammonia-lyase activity; IEA:InterPro.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
DR   CDD; cd00332; PAL-HAL; 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR   InterPro; IPR005922; Phe_NH3-lyase.
DR   InterPro; IPR023144; Phe_NH3-lyase_shielding_dom_sf.
DR   NCBIfam; TIGR01226; phe_am_lyase; 1.
DR   PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR   PANTHER; PTHR10362:SF80; PHENYLALANINE AMMONIA-LYASE 2; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU003954, ECO:0000313|EMBL:KXN81031.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  78051 MW;  5381752BF6EAEBD6 CRC64;
     MLLNRSTSYN ETTPAKVDQG IHGHSHLPPT LLSEFLKSHR ELERYRHGAP VRVDGQTLSL
     AGVVGVARHG ASVILDESPV IKSVVAKSRT VIENNVNNGT SVYGLSTGFG GSADTRTDQP
     LLLGHALLQH QHVGILPTSE EPPERLPLLD PSTATTMPES WVRGAILVRM NSLIRGHSGV
     RWDIIEKMHE ILKADLIPRV PLRGSISASG DLSPLSYVAG TIAGTPAIRV YHGSHKFGAR
     QTSRAPDALR AHGIESVALA SKEHLGILNG TAFSASVGAL ALHEAIHLSL LAQVCTAMGT
     EALLGARGSF DPFIHATARP HPGQVECAKN IWDLLEGSKF ARAHEKEVAL KDDQYTLRQD
     RYPLRTAPQF LGPQIEDLFS ALTSLSQECN STTDNPLIDG ETGQIHHGGN FQAMTVTNAM
     EKTRLALHHI GKILFAQSTE LLNPTMNNGL PPSLAASDPS LNYHVKGVDI ATAAYTAELG
     YLASPVSTHI QSAEMHNQAV NSMALVAGRA TINSIDVLSM LLATYLYNLC QALDLRALQA
     EFMARLPNLL RDALRIHLAS KITLTDEDVL VSSLIRVMHE TLDKFTTMDN EDRMRAVADS
     TTSTLVNFFA ESDGVDLKTI NEFRSRVASH TAGIHDELRK EFLTGLKGAT PASPYLSKTK
     AVYEYIRETL GVKMHGFENY TGFVNGLCVD ELSIGGNISI IYEAIRDGKT QNVIVSLFDA
//