ID A0A135LJZ3_PENPA Unreviewed; 732 AA.
AC A0A135LJZ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Phenylalanine ammonia-lyase {ECO:0000313|EMBL:KXG49297.1};
GN ORFNames=PGRI_031670 {ECO:0000313|EMBL:KXG49297.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG49297.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG49297.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG49297.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG49297.1}.
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DR EMBL; LHQR01000065; KXG49297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LJZ3; -.
DR STRING; 5078.A0A135LJZ3; -.
DR OMA; GTRRNFH; -.
DR OrthoDB; 1030318at2759; -.
DR Proteomes; UP000070168; 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:KXG49297.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168}.
SQ SEQUENCE 732 AA; 79251 MW; EC33100FB5DA1D53 CRC64;
MGSIAPVLAY DVNHQWATPH VQHTLNSWSE LKKHVKAGTI FIDGQSLDVA SVVAIARNGV
RLALKEDQSV IEGIEASVET LQGYLSKGYY LYGVNTGFGG SADTRTQDLY GLQRGLMQLT
QSAILTKEDK SDAPNGHEYL ESHSMPSVWT RATILIRCNA NIRGHSAMTR NVVDSMIKLL
EHDIVPVIPL RGSVSASGDL MPLAYISGAI QGSPDVYVRV GGQKGLPRVI TAQQALEEAS
ITPIVLGPKE GLSLINGTAA AAAVASIGCY EANQLAVVSQ LLTALTSEAL YANNEWAHPF
IAATRPHQGQ IEAAQNMRTF LRGSKLSYGL EQTKDRFSSG LAQERYALRS SPQWLAPQLE
DLLSAEKQLH VELNSTSDNP VVNSLDNDIH CGANFQAASV TSATEKIRLA LQSIGRMLFS
QTSEMINHDL SNGLPPNLAA DDPSISFCLK GLDINTAAYT SELGFLANPV SNHVQTAEMN
NQGINSLGLL SARQTMASVE VLSMIVANSL YTGCQGVDLR ALHRTFIANL ENPARQLVVG
FLPNESWPVA TAHKFFNSFW KLFEEAWYDT VAYDAPERAR KASESLTTAI VAHADQIPAL
VSIENVAGLS KDFEALVLDS YLTHREAFFR NPTTSEYLGQ GTKAIYLFVR EKLGVPMHRG
LIEHPVAGDK DGNMIDGRPK KTIGSWVSII YEAVRSGSLY SEVFEFLQAA GDVKGSKLSK
GTNGTNGTNG IH
//
