ID A0A176W4K4_MARPO Unreviewed; 697 AA.
AC A0A176W4K4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_3309s1510 {ECO:0000313|EMBL:OAE27954.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE27954.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE27954.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE27954.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005138}.
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:OAE27954.1}.
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DR EMBL; LVLJ01001803; OAE27954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W4K4; -.
DR OrthoDB; 1104949at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016841; F:ammonia-lyase activity; IEA:InterPro.
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; 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; 2.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU003954};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
SQ SEQUENCE 697 AA; 74322 MW; A2CF707027A15E86 CRC64;
MAAMVMEVGT PALGEVAPAP GDAGWTVQLC MSPMKKGASA GDALHWARAA EAGAGSHWEE
VKAMVSEFEQ AKEVVIQGVT LSVAQVSAVA RNPQVTVVLD AATAKERVDA SNNWVAHNMT
KGTDTYGVTT GFGATSHRRT DKGADLQKEL IRFLNAGVLA DEASVLPVAT TRAAMLVRTN
TLMQGFSGIR WEILQTLQKL LNKHITPRLP LRGTITASGD LVGLLKPFEL QPKEGLAIVN
GTAVGAAQAA MACYDANVLA LFAEVASALF CEAMQGKPEF TDHLTHRLKH HPGQIEAAAV
MEFVLDGSAY MKAAAQLHAT DPLKKPKQDR YALRTSPQWL GPQIEVIRAA THAVAREINS
VNDNPLIDVA RDKALHGGNF QGTPIGVSMD NLRLALAAIG KLMFAQMSEL VNDFYNGGLP
SNLTGGPNPS LDYGFKGAEI AMASYCSELL YLANPVTTHV QSAEQHNQDV NSLGLISARK
TAEAVEILKL MASTFVVALC QAVDLRHLEE NMLATVKQAV SQAAKKTLFA DAAGALLPSR
FCEKDLLKVV DDTPPFSYVD DATSATYPLM TKLRQVLVGH ALASAEPDDG CSVFRRIAVF
EEEARAQLEQ AVPVARQQFD AGAAALPNKI LQCRSFPVYN LVRSLGTKLL IGTESRSPGE
DIQLVFEAIN AGKLAGPLLA CLDGWSGAPL PVDAPRV
//
