PALY_MAIZE
ID PALY_MAIZE Reviewed; 703 AA.
AC Q8VXG7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phenylalanine/tyrosine ammonia-lyase;
DE EC=4.3.1.25;
DE AltName: Full=Bifunctional phenylalanine ammonia-lyase;
DE Short=Bifunctional PAL;
GN Name=PAL1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9008393; DOI=10.1104/pp.113.1.175;
RA Roesler J., Krekel F., Amrhein N., Schmid J.;
RT "Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity.";
RL Plant Physiol. 113:175-179(1997).
CC -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine
CC and L-tyrosine to form trans-cinnamic acid and p-coumaric acid
CC respectively with similar efficiencies. Facilitates the commitment step
CC in phenylpropanoid pathways that produce lignins, coumarins and
CC flavonoids. {ECO:0000269|PubMed:9008393}.
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=4.3.1.25;
CC Evidence={ECO:0000269|PubMed:9008393};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine = (E)-4-coumarate + NH4(+); Xref=Rhea:RHEA:24906,
CC ChEBI:CHEBI:12876, ChEBI:CHEBI:28938, ChEBI:CHEBI:58315; EC=4.3.1.25;
CC Evidence={ECO:0000269|PubMed:9008393};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=658 uM for L-phenylalanine (at pH 7.7)
CC {ECO:0000269|PubMed:9008393};
CC KM=270 uM for L-phenylalanine (at pH 8.7)
CC {ECO:0000269|PubMed:9008393};
CC KM=41 uM for L-tyrosine (at pH 7.7) {ECO:0000269|PubMed:9008393};
CC KM=19 uM for L-tyrosine (at pH 8.7) {ECO:0000269|PubMed:9008393};
CC Note=kcat is 10.6 sec(-1) with L-phenylalanine as substrate and 0.92
CC sec(-1) with L-tyrosine as substrate (at pH 8.7).;
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:9008393};
CC Temperature dependence:
CC Optimum temperature is 55-60 degrees Celsius.
CC {ECO:0000269|PubMed:9008393};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; L77912; AAL40137.1; -; mRNA.
DR AlphaFoldDB; Q8VXG7; -.
DR SMR; Q8VXG7; -.
DR STRING; 4577.GRMZM2G074604_P01; -.
DR PaxDb; Q8VXG7; -.
DR PRIDE; Q8VXG7; -.
DR eggNOG; KOG0222; Eukaryota.
DR BRENDA; 4.3.1.24; 6752.
DR SABIO-RK; Q8VXG7; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q8VXG7; baseline and differential.
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; IDA:AgBase.
DR GO; GO:0052883; F:tyrosine 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:InterPro.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; TAS:AgBase.
DR GO; GO:0016598; P:protein arginylation; IDA:AgBase.
DR GO; GO:0046898; P:response to cycloheximide; IDA:AgBase.
DR GO; GO:0009739; P:response to gibberellin; IDA:AgBase.
DR CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.10.274.20; -; 1.
DR Gene3D; 1.10.275.10; -; 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 PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR01226; phe_am_lyase; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Phenylpropanoid metabolism; Reference proteome.
FT CHAIN 1..703
FT /note="Phenylalanine/tyrosine ammonia-lyase"
FT /id="PRO_0000418895"
FT REGION 608..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 190
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 189..191
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 703 AA; 74927 MW; 11374FD68516971E CRC64;
MAGNGAIVES DPLNWGAAAA ELAGSHLDEV KRMVAQARQP VVKIEGSTLR VGQVAAVASA
KDASGVAVEL DEEARPRVKA SSEWILDCIA HGGDIYGVTT GFGGTSHRRT KDGPALQVEL
LRHLNAGIFG TGSDGHTLPS EVTRAAMLVR INTLLQGYSG IRFEILEAIT KLLNTGVSPC
LPLRGTITAS GDLVPLSYIA GLITGRPNAQ AVTVDGRKVD AAEAFKIAGI EGGFFKLNPK
EGLAIVNGTS VGSALAATVM YDANVLAVLS EVLSAVFCEV MNGKPEYTDH LTHKLKHHPG
SIEAAAIMEH ILDGSSFMKQ AKKVNELDPL LKPKQDRYAL RTSPQWLGPQ IEVIRAATKS
IEREVNSVND NPVIDVHRGK ALHGGNFQGT PIGVSMDNAR LAIANIGKLM FAQFSELVNE
FYNNGLTSNL AGSRNPSLDY GFKGTEIAMA SYCSELQYLG NPITNHVQSA DEHNQDVNSL
GLVSARKTAE AIDILKLMSS TYIVALCQAV DLRHLEENIK ASVKNTVTQV AKKVLTMNPS
GELSSARFSE KELISAIDRE AVFTYAEDAA SASLPLMQKL RAVLVDHALS SGERGAGALR
VLQDHQVRGG APRGAAPGGG GRPRGVAEGT APVANRIADS RSFPLYRFVR EELGCVFLTG
ERLKSPGEEC NKVFVGISQG KLVDPMLECL KEWDGKPLPI NIK
