PALY2_PLEOS
ID PALY2_PLEOS Reviewed; 747 AA.
AC A0A4Y6HUD7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Phenylalanine ammonia-lyase 2 {ECO:0000303|PubMed:31655558};
DE EC=4.3.1.24 {ECO:0000269|PubMed:31655558};
DE AltName: Full=PoPAL2 {ECO:0000303|PubMed:31655558};
GN Name=PAL2 {ECO:0000303|PubMed:31655558};
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322 {ECO:0000312|EMBL:QDF60495.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL
RP STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=CCMSSC00389 {ECO:0000303|PubMed:31655558};
RX PubMed=31655558; DOI=10.1186/s12866-019-1594-4;
RA Hou L., Wang L., Wu X., Gao W., Zhang J., Huang C.;
RT "Expression patterns of two pal genes of Pleurotus ostreatus across
RT developmental stages and under heat stress.";
RL BMC Microbiol. 19:231-231(2019).
CC -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to
CC form trans-cinnamic acid and a free ammonium ion (PubMed:31655558).
CC Facilitates the commitment step in phenylpropanoid pathways that
CC produce secondary metabolites such as lignins, coumarins and flavonoids
CC (By similarity). {ECO:0000250|UniProtKB:P11544,
CC ECO:0000269|PubMed:31655558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine = (E)-cinnamate + NH4(+);
CC Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58095; EC=4.3.1.24;
CC Evidence={ECO:0000269|PubMed:31655558};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11544}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Very highly expressed in spores (PubMed:31655558).
CC Expression is higher in fruiting bodies than in primordia, and low in
CC mycelia (PubMed:31655558). In the fruiting body, present in the stipe,
CC cap, gill and pileipellis (PubMed:31655558).
CC {ECO:0000269|PubMed:31655558}.
CC -!- INDUCTION: Induced by thermal stress. {ECO:0000269|PubMed:31655558}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in delayed
CC primordium formation (PubMed:31655558). RNAi-mediated knockdown in
CC mycelia results in resistance to H2O2 (PubMed:31655558).
CC {ECO:0000269|PubMed:31655558}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; MK207024; QDF60495.1; -; mRNA.
DR VEuPathDB; FungiDB:PLEOSDRAFT_173727; -.
DR UniPathway; UPA00713; UER00725.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0009800; P:cinnamic acid biosynthetic process; IC:UniProtKB.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.10.274.20; -; 1.
DR Gene3D; 1.10.275.10; -; 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 PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR01226; phe_am_lyase; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT CHAIN 1..747
FT /note="Phenylalanine ammonia-lyase 2"
FT /id="PRO_0000454792"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 230
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT CROSSLNK 229..231
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 747 AA; 79946 MW; 94D295D85EE8A0BB CRC64;
MTILSGTTAA PRVNGTTMNG HSKPHTNGVH LNGHAPKATT ESPWPQSEEK TLLDKFVEAY
YEFESYKSGQ TVKVDGKTLS LAGVVAAARH HAKISLDDSA SIKDKVVKSR KVIADKVASG
ASVYGLSTGF GGSADTRTDQ PLSLGHALLQ HQHVGVLPSS SQPLDVLPLS DPMSATSMPE
AWVRAAMLIR MNSLIRGHSG VRWELIEKIA EIFDANITPV VPLRSSISAS GDLSPLSYIA
GTVVGNPSIR VFDGPAAFGA REMVPSAKAL ASHGIDPLPL ASKEPLGILN GTAFSAAVGA
LALNEAVHFA MLAQVCTAMG TEALVGTRLS FEPFIHATCR PHPGQIEAAR NIYNLLEGTT
FASVHHEEVH IAEDQGTLRQ DRYPLRTSPQ FLGPQLEDIL HAYVSVTQEC NSTTDNPLID
GETGEIHHGG NFQAMAVTNA MEKTRLALHH IGKLLFAQCT ELVNPAMNNG LPPSLAATDP
SLNYHTKGID IATAAYVSEL GYLANPVSTH IQSAEMHNQA VNSLALISAR ATVNSLDVLS
LLISSYLYIL CQALDLRALQ MEFVKGVEEI IREELSLLFA SVVSPAELEA LTSKVLSAAQ
TSLDTSGSMD APARMKKMAS TTTIPLFDFL TELTLPDAIS SGIAMVSIPS FRSHLASRAT
ALLDQLRRDY LSGQRGAAPA SPYLNKTRMV YEFVRLTLGV KMHGSENYAR FAKGLGVEDE
TIGQNISRIH EAIRDGKMQA ITVAMFA
