ID D8SHP8_SELML Unreviewed; 679 AA.
AC D8SHP8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000256|RuleBase:RU003955};
DE EC=4.3.1.24 {ECO:0000256|RuleBase:RU003955};
GN Name=PAL3-2b {ECO:0000313|EMBL:EFJ16153.1};
GN ORFNames=SELMODRAFT_450484 {ECO:0000313|EMBL:EFJ16153.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ16153.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003955}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR EMBL; GL377620; EFJ16153.1; -; Genomic_DNA.
DR RefSeq; XP_002982908.1; XM_002982862.1.
DR AlphaFoldDB; D8SHP8; -.
DR STRING; 88036.D8SHP8; -.
DR EnsemblPlants; EFJ16153; EFJ16153; SELMODRAFT_450484.
DR GeneID; 9662334; -.
DR Gramene; EFJ16153; EFJ16153; SELMODRAFT_450484.
DR KEGG; smo:SELMODRAFT_450484; -.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_3_0_1; -.
DR InParanoid; D8SHP8; -.
DR OMA; NDPLSWG; -.
DR OrthoDB; 1030318at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000001514; 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:EFJ16153.1};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051,
KW ECO:0000256|RuleBase:RU003955};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
SQ SEQUENCE 679 AA; 72788 MW; 7D2B933BA484E131 CRC64;
MSGSHLEEVR EMAHTVYGAA KPSFPIEGTT LTIAQVAAVA KRGAQVRLDS AAAKKRVDES
SNWVLDNAMK GTDILGVTTG FGATSHRRIN QGVGLQRELI RVLNAGIFSD DDSTNVLPLA
FARGAMLVRT NTLLQGYSGI RWEILSAMEK LVNSGIVARI PLRGTITASG DLVPLSYIAG
LLSGRSNARA VLPDGKVVNS TEALKLVGVE QPFELQPKEG FAIVNGTAVG AAVASIACFD
ANVLALLAEI LSAMFCEAMQ GKPEFTDPLT HKLKHHPGQI EAAAIMEHVL AGSSYMKAAA
KLHETDSLKK PKQDRYALRT SPQWLGPQIE VIRHATHSIQ REINSVNDNP IIDVARDKAL
HGGNFQGTPI GVSMDNLRLA VAAIGKLMFA QFSELVNDFY NNGLPSNLSG GSNPSLDYGF
KGAEIAMASY TSELQYLANP VTTHVQSAEQ HNQDVNSLGL VSARKTVEAL NILKLMSSTY
LVALCQAIDL RHLEENLQAT VKQTVSHAVK NTLTTGAAGA LLPSRLCEKE LLSVVDNQHV
FTYIDDPASA GYPLMQKLRQ VLVEHALKNI GDEKETSSSV LHKIGLFEEE LKAALSVEVL
AAREAYESGN AVLPNRIFDC ASAPLYEFVR KGAGTALLMG TKSGTPGEDF TKVYDAICQG
KLVAPLLKCV DGWSGTPSF
//
