ID A0A0A0KIE0_CUCSA Unreviewed; 705 AA.
AC A0A0A0KIE0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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_6G446290 {ECO:0000313|EMBL:KGN48167.1};
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:KGN48167.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN48167.1, 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; KGN48167.1; -; Genomic_DNA.
DR RefSeq; XP_004143260.2; XM_004143212.2.
DR AlphaFoldDB; A0A0A0KIE0; -.
DR STRING; 3659.A0A0A0KIE0; -.
DR EnsemblPlants; KGN48167; KGN48167; Csa_6G446290.
DR GeneID; 101219091; -.
DR Gramene; KGN48167; KGN48167; Csa_6G446290.
DR KEGG; csv:101219091; -.
DR OMA; NASSYWV; -.
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 705 AA; 77172 MW; B0E81D2D460987F6 CRC64;
MALVETISKS SIHDPLNWGV AADSLKGSHF DEVKRMVEEY QRTLVKLDGE TLTVSQVAAI
ATRNSDVIVE LSESTRVGVK ASSDWIMESL NKGTDSYGIT TGFGATSHRR TKQGGALQKE
LIRFLNAGIS ESGTESSHTL SHSATRAAML VRTNTLLQGY SGIRFEILEA IIKLLNHNIT
PCLPLRGTVT ASGDLVPLSY IAGLLIGRPN SKAIGPNGEN LDAKEAFIHA GITSGFFEFQ
PKEGFALVNS TAVGSGLASI VLFEANILAV LSEILSAIFA EVMQGKPEFT DHLTHKLKHH
PGQIEAAAIM EHILDGSSYM KTAKKLHEMD PLQKPKQDRY ALRTAPQWLG PLIEVIRFST
KSIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN TRLAIASIGK LMFAQFSELV
NDFYNNGLPS NLSASRNPSL DYGFKGAEIA MASYCSELQY LANPVTTHVQ SAEQHNQDIN
SLGLISSRKT AEAIDILKLM SSTFLVALCQ AIDLRHLEEN LKSAVKSTII LVAQKVLITS
TNGALDPSRL FEKNLLKVVD REYTFAYIDD PCSATYPLMQ GLRQVFVEHT LANSDDENNA
DTPIFQKIAI FEAELKAILS NKVESTRLAY ESGNALIKNQ IEECRSYPLY RFVREELGIK
LLTGEKVISP GEECEKVFAA LCKGKMINSI LECLKEWNGA PIPIC
//
