ID A0A0A0KH72_CUCSA Unreviewed; 717 AA.
AC A0A0A0KH72;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000256|ARBA:ARBA00012139, ECO:0000256|RuleBase:RU003955};
DE EC=4.3.1.24 {ECO:0000256|ARBA:ARBA00012139, ECO:0000256|RuleBase:RU003955};
GN ORFNames=Csa_6G445770 {ECO:0000313|EMBL:KGN48164.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN48164.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN48164.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
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 -!- 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|ARBA:ARBA00023537,
CC 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}.
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DR EMBL; CM002927; KGN48164.1; -; Genomic_DNA.
DR RefSeq; XP_004143356.2; XM_004143308.2.
DR AlphaFoldDB; A0A0A0KH72; -.
DR STRING; 3659.A0A0A0KH72; -.
DR EnsemblPlants; KGN48164; KGN48164; Csa_6G445770.
DR GeneID; 101222092; -.
DR Gramene; KGN48164; KGN48164; Csa_6G445770.
DR KEGG; csv:101222092; -.
DR eggNOG; KOG0222; Eukaryota.
DR OMA; VDIVSMM; -.
DR OrthoDB; 1030318at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000029981; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IBA:GO_Central.
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};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Phenylpropanoid metabolism {ECO:0000256|ARBA:ARBA00023051,
KW ECO:0000256|RuleBase:RU003955};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981}.
SQ SEQUENCE 717 AA; 78283 MW; 99122C8BED74D616 CRC64;
MAPAQLEQFA HQNGSMESFC TSHVVDPLNW GVAAEALKGS HLDEVKRMVD EYRRPVVKLG
GETLTISQVA AIATRDNDVV VKLAESARAG VKASSDWVME SMNKGTDSYG VTTGFGATSH
RRTKQGGALQ KELIRFLNAG IFGNGAESNH TLPHSATRAA MLVRINTLLQ GYSGIRFEIL
EAITNLLNEN VTPCLPLRGT ITASGDLVPL SYIAGLLTGR PNSKAIGPNG ETLDAEAAFK
QAGIPSSFFE LQPKEGLALV NGTAVGSGLA SIVLFEANIL AVLSEILSAI FAEVMQGKPE
FTDHLTHKLK HHPGQIEAAA IMEHILDGSS YMKAAKKLHE IDPLQKPKQD RYALRTSPQW
LGPLIEVIRF STKSIEREIN SVNDNPLIDV SRNKALHGGN FQGTPIGVSM DNTRLAIASI
GKLMFAQFSE LFNDFYNNGL PSNLSASRNP SLDYGFKGAE IAMASYCSEL QYLANPVTSH
VQSAEQHNQD VNSLGLISSR KTAEAIDILK LMSSTFLVAL CQAIDLRHLE ENLKSTVKSV
VSQVAKKVLT TSSIGTLHPS RFCEKDLLKV VDREYTFAYI DDPCSATYPL MQKLRQVLVD
HALTNGENEK NMNTSIFQKI TAFEEELKVA LPKEVENTRL AYESGNSKVA NQIKDCRSYP
LYKFVREDLG AKLLTGERVI SPGEECEKVF TALCQGKMID SILECLKEWN GAPIPIC
//
