ID A0A0K9P3I0_ZOSMR Unreviewed; 712 AA.
AC A0A0K9P3I0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000256|RuleBase:RU003955};
DE EC=4.3.1.24 {ECO:0000256|RuleBase:RU003955};
GN ORFNames=ZOSMA_445G00020 {ECO:0000313|EMBL:KMZ62782.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ62782.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:0000256|RuleBase:RU003955};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005138, ECO:0000256|RuleBase:RU003955}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU003955}.
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:KMZ62782.1}.
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DR EMBL; LFYR01001320; KMZ62782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9P3I0; -.
DR STRING; 29655.A0A0K9P3I0; -.
DR OMA; YSLRCMP; -.
DR OrthoDB; 390692at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
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:KMZ62782.1};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051,
KW ECO:0000256|RuleBase:RU003955};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
SQ SEQUENCE 712 AA; 77325 MW; 2639AFCA796CEF2A CRC64;
MDAMDLCQVK LSNGATNGIT DADPLNWGAA AEELTGSHLQ EVKRMVEDFN NPLVKIEGAT
LKISQVAAVA TASAEVQLSE TARERVTASS HWVMDSMNKG TDSYGVTTGF GATSHRRTKQ
GGALQKELIR FLNAGIFGGS KDTANTLPSA TTRAAMLVRA NTLLQGYSGI RFEILEAMTK
FLNGNITPCL PLRGTITASG DLVPLSYIAG FLTGRTNSKA IGPDGKQITS SEAFAIAGIQ
EGFFQLQPKE GLALVNGTAV GSGLASMVLF DANILALSAE VLSAVFCEVM QGKPEFTDHL
THKLKHHPGQ IEAAAIMEHI LDGSSYMKMA AKIHEQDPLQ KPKQDRYALR TSPQWLGPQV
EVIRASTKSI EREINSVNDN PLIDVSRNKA LHGGNFQGTP IGVSMDNTRL AIAAIGKLMF
AQFSELVNDF YNNGLPSNLS GGRNPSLDYG FKGGEIAMAS YCSELQFLAN PVTNHVQSAE
QHNQDVNSLG LISARKTAES IEILKLMTST FLVGICQAID LRHMEENLKA SVKNTVSQVA
KRVLTMTANG ELHPSRFCEK DLLKVVDREY VFSYIDDPCS ATYPLMQKLR SVLVDHALNN
GDKEKDEAMS IFQKIAVFEE ELIAALPKEV EAARLAVEAG KPAIANRIEE CRSYPLYKFV
REELRTGLLT GEKVRSPGEE FDKVFVAINE GELVGPLMEC LKEWNGAPIP IC
//
