ID A0A166A6J9_EXIGL Unreviewed; 721 AA.
AC A0A166A6J9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Phenylalanine ammonia-lyase {ECO:0000313|EMBL:KZV88969.1};
GN ORFNames=EXIGLDRAFT_161712 {ECO:0000313|EMBL:KZV88969.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88969.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV88969.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88969.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR EMBL; KV426085; KZV88969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166A6J9; -.
DR STRING; 1314781.A0A166A6J9; -.
DR InParanoid; A0A166A6J9; -.
DR OrthoDB; 1030318at2759; -.
DR Proteomes; UP000077266; 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:KZV88969.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
SQ SEQUENCE 721 AA; 76635 MW; 61EF9AFB87BC929A CRC64;
MLLRDLDSSG SGGTMPFDMH TDGVTNGATP TAIAPPPYAG LLKVFLNSER ELKLFQSGTA
PVLDGKSLSV PAVVAAARYG VQVALDDAPE VQARVAASRK VIDEKLASAT SIYGVSTGFG
GSADTRTDQY HTLGAALLQH HHSGVLSVEN GSGFANDKLP LPQGDPLATT SMPVAWVRGA
IAVRINSVIR GHSGVRWVVM EQMRELLNRR LTPVVPLRGS ISASGDLTPL AYVAGAVTKH
PHIRVHTPTG DIIRASETDL PPVALQPKEQ LGLMNGTAFS AAVGALATHD ALHMALLSQV
CTALGTEALL GTQASHVPFI HDICRPHPGQ VESARIIHSL LDGSKLASTG TEEEVSIVQD
AGQLRQDRYP LRTAAQYLGP QIEDILAAHA SVSLECNSTT DNPLIDGARG HIHHGGNFQA
MAVTNAMEKT RLALFHIGKI IFAQSTELLN PAFNRGLPPS VAASDPSTNY HAKGLDIATA
AYVSELGFLA NPVGTHVQSA EMHNQAVNSL ALISARATMT ALDVLSMLFA TYIYVLCQAV
DMRAMHDDFE RSIPSTLASL LSTHFAADAS SLSDTFQRSI VQEMQNVLEH NSTQDAADRM
AGAARSAALP LYNTLPARAA DVPKFVESLG AELLSTYERL REEYLEGKKT AAPFLGGTRA
LYEFVRGELG VKIHGLSNLR GFVGDGLDAY GERGVGENVS VIYESIRNGR VQRVLAGMFA
Q
//
