ID   A0A0F0I134_ASPPU        Unreviewed;       720 AA.
AC   A0A0F0I134;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Aromatic amino acid lyase {ECO:0000313|EMBL:KJK61415.1};
GN   ORFNames=P875_00042331 {ECO:0000313|EMBL:KJK61415.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61415.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK61415.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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:KJK61415.1}.
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DR   EMBL; JZEE01000675; KJK61415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0I134; -.
DR   STRING; 1403190.A0A0F0I134; -.
DR   Proteomes; UP000033540; 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:KJK61415.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
SQ   SEQUENCE   720 AA;  78917 MW;  A8FB5D29F1B72DB8 CRC64;
     MDLLNMGNLS DFQTHIQTAY QARQRLQNLQ REGTFNVDGA TLDISAIVAV AYYGCIPKIT
     TDPAVLEKIE ASVQVLRDHL DKGYHVYGVN TGFGGSADSR TDRVVALQSG LSQLLQAGVL
     VTSDKETNVD LERQVRLDSH AVPVPWVRAA MLVRCNSNAR GHSAVTLSVM KSILQLLESR
     ITPVVPLRGS ISASGDLIPL SYIAGAIEGN PDVHVHVQKS HKSQIMSSRD ALLSAGMEPQ
     VLGPKEGLGL VNGTSFSAAL SSLVMYETHQ LVVLVQAISA VALEALMGNA ESFHPFISAI
     RPHDGQMECA RNILSFLQGS RLAQGIQSVK THTRQGLMQD RYALRCVPQW IGPQLEDLLL
     AHKQVTVELN STTDNPLIDP ETGDILHGGN FQAVSVTSAM EKTRSCLQMF GRLLFSQSTE
     LVDPSLNNGL PTNLVADDPS LSFTMKGVDI SMASYMAELA YLANPVSSHV QAAEMRNQSI
     NSMAFVSSRY TMQAVEIVSL MCACSLYIGC QALDLRVLHL TYLDNIKPQI HLLTSDLFSS
     YLSDQELATL TESLWENISK SWSTTTRQGI PERVQVAVKN AIPTLLDTLK EKRGPGLSDL
     NRWETQAADL LNKTYQNTAD TFFNQQNTEE FLGAGAKILY RTVRQDLNVP FHLGFVEHPT
     VNNETLNGRS KKTIGSWISI IYEAIRDGRL MGPFMESLAS KSSSADDSLT KIRSLRMSRL
//