ID M1A3M4_SOLTU Unreviewed; 667 AA.
AC M1A3M4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=phenylalanine ammonia-lyase {ECO:0000256|ARBA:ARBA00012139};
DE EC=4.3.1.24 {ECO:0000256|ARBA:ARBA00012139};
GN Name=102605661 {ECO:0000313|EnsemblPlants:PGSC0003DMT400014003};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400014003, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400014003}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400014003};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- FUNCTION: This is a key enzyme of plant metabolism catalyzing the first
CC reaction in the biosynthesis from L-phenylalanine of a wide variety of
CC natural products based on the phenylpropane skeleton.
CC {ECO:0000256|ARBA:ARBA00002235}.
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005138}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238}.
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DR RefSeq; XP_006354305.1; XM_006354243.2.
DR AlphaFoldDB; M1A3M4; -.
DR SMR; M1A3M4; -.
DR STRING; 4113.M1A3M4; -.
DR PaxDb; 4113-PGSC0003DMT400014003; -.
DR EnsemblPlants; PGSC0003DMT400014003; PGSC0003DMT400014003; PGSC0003DMG400005492.
DR GeneID; 102605661; -.
DR Gramene; PGSC0003DMT400014003; PGSC0003DMT400014003; PGSC0003DMG400005492.
DR KEGG; sot:102605661; -.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_3_0_1; -.
DR InParanoid; M1A3M4; -.
DR OMA; WIIEGMN; -.
DR OrthoDB; 756923at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000011115; 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); 2.
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; IPR023144; Phe_NH3-lyase_shielding_dom_sf.
DR PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR PANTHER; PTHR10362:SF52; PHENYLALANINE AMMONIA-LYASE; 1.
DR Pfam; PF00221; Lyase_aromatic; 2.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 3: Inferred from homology;
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115}.
SQ SEQUENCE 667 AA; 73689 MW; 5627FD6C6E0F94B1 CRC64;
MDYSQDFSIK SDDQQRYDPL CWNMAEDTLK GSHHDEVKKM VDVFRKPVIR LGGGEMLTIG
NVAAIATRSG MESVKVELSE AARAGVKASS DWIIEGMNKG TDSNGVTTGF GATSHRRTKQ
GAALQKELIR FLNAGVFGNE MMYSHTKLPQ SATRSAMLVR INTLLKGYSG IRFEILETMT
KFLNNNITPC LPVHTSCSDL VPLSYIAGLL MGRPNSKATK PNGELLNAVQ AFHEVGIDTG
FFELQPKEGI ALVNGTCVGS GLASIVLYET NILVVLSEVL SAFFVEAMHG QHILNGSNSY
VMEIDEKRNK HDCYVLGKSP HWLGPQIEVI REATTMIERE INSVDDNPLI DVSRNKALHG
GNFQGISIGV SMDNTRLALA SIGKLIFAQF SDLVSNGLPS NLSGSRSSSL DYGFKGAEIS
MASYCSELQF LANPVTNHVQ SAEQHNQDVN SLALISSRKT SEAVDILKLM SSTYLVALCQ
AIDLRHLEEN LEAAVKNAVS LVSQNGELDH LSIRFCEKDL LKVVDSEYVF AYADDPCNAN
YPLIQKLRQI LMDHARDEEK ILSNSIFQKI SAFEEELKVV LSEEIESARC DFDNCKSSIP
NRIKECKSYP LYKFVREELE INFLTGEKVK SPGEEINKVL ISMNEGMLID PLLNCLKDWN
GVPLPFC
//
