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Database: UniProt
Entry: A0A176VFY7_MARPO
LinkDB: A0A176VFY7_MARPO
Original site: A0A176VFY7_MARPO 
ID   A0A176VFY7_MARPO        Unreviewed;       299 AA.
AC   A0A176VFY7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Phenylalanine ammonia-lyase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AXG93_1860s1010 {ECO:0000313|EMBL:OAE19292.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE19292.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE19292.1, 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:OAE19292.1};
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   -!- 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:OAE19292.1}.
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DR   EMBL; LVLJ01003902; OAE19292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VFY7; -.
DR   OrthoDB; 1067982at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR008948; L-Aspartase-like.
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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
SQ   SEQUENCE   299 AA;  33278 MW;  66524278AD2AEABC CRC64;
     MDNMRLAIAA MGKLMFAQMS ELVNDFYNGG LPSNLTGGPN PSLDYGFKGA EIAMASYTSE
     LLYLANPVTT HVQSAEQHNQ DVNSLGLISA RKTEEAIEIF KLMCSTYLVA LCQAVDLRHL
     EENMQVSVKN VVSQAAKKTL FTDAQGCLLP SRFCEKDLLK VVDNQPPFSY VDDATSASYP
     LMQKLRQCLV SHALSSENEE ERCSVFRRIS VFEEQVKTDL EATVPKVREQ FDNGVAAIPN
     RISDCRSYPL YDFVRSLGTK LLVGTETRSP GQDIELVKDF CPFDCKLENV ELVVLTSIF
//
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