PALY_USTMA
ID PALY_USTMA Reviewed; 724 AA.
AC Q96V77; A0A0D1CF47; Q4PII5;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0000303|PubMed:11570515};
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:A0A4Y6HUI7};
GN Name=PAL1; ORFNames=UMAG_00078;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11570515; DOI=10.1007/s002940100230;
RA Kim S.-H., Virmani D., Wake K., MacDonald K., Kronstad J.W., Ellis B.E.;
RT "Cloning and disruption of a phenylalanine ammonia-lyase gene from Ustilago
RT maydis.";
RL Curr. Genet. 40:40-48(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to
CC form trans-cinnamic acid and a free ammonium ion (By similarity).
CC Facilitates the commitment step in phenylpropanoid pathways that
CC produce secondary metabolites such as lignins, coumarins and flavonoids
CC (By similarity). {ECO:0000250|UniProtKB:A0A4Y6HUI7,
CC ECO:0000250|UniProtKB:P11544}.
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:0000250|UniProtKB:A0A4Y6HUI7};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11544}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; AF306551; AAL09388.1; -; Genomic_DNA.
DR EMBL; CM003140; KIS71637.1; -; Genomic_DNA.
DR RefSeq; XP_011386045.1; XM_011387743.1.
DR AlphaFoldDB; Q96V77; -.
DR SMR; Q96V77; -.
DR STRING; 5270.UM00078P0; -.
DR PRIDE; Q96V77; -.
DR EnsemblFungi; KIS71637; KIS71637; UMAG_00078.
DR GeneID; 23561479; -.
DR KEGG; uma:UMAG_00078; -.
DR VEuPathDB; FungiDB:UMAG_00078; -.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_3_1_1; -.
DR InParanoid; Q96V77; -.
DR OMA; MYVHSIP; -.
DR OrthoDB; 923557at2759; -.
DR BioCyc; MetaCyc:MON-17190; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000000561; Chromosome 1.
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; ISS:UniProtKB.
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; 1.10.274.20; -; 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 3: Inferred from homology;
KW Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism;
KW Reference proteome.
FT CHAIN 1..724
FT /note="Phenylalanine ammonia-lyase"
FT /id="PRO_0000215433"
FT ACT_SITE 91
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 498
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 206
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 205..207
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT CONFLICT 61..64
FT /note="PVLD -> TRPR (in Ref. 1; AAL09388)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="R -> G (in Ref. 1; AAL09388)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="L -> H (in Ref. 1; AAL09388)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="R -> Q (in Ref. 1; AAL09388)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="I -> F (in Ref. 1; AAL09388)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="D -> N (in Ref. 1; AAL09388)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="I -> F (in Ref. 1; AAL09388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 79227 MW; 358870DC62DDD1E1 CRC64;
MAPTADVLPP VEASTRPGLL VQPSDTKLRK ASSFRTEQVV IDGYNLKIQG LVASARYGHV
PVLDPSAETR KRIDDSVQSL IAKLDRGESI YGINTGFGGS ADSRTANTRA LQLALLQMQQ
CGVLPVPSTF PTGEPSSAPF ALPLTDTESS LIMPEAWVRG AIVVRLSSLM RGHSGVRWEV
LDKMQKLFLQ NNVTPVVPVR SSISASGDLS PLSYVAGALA GQRGIYCFVT DGRGQRVKVT
ADEACRMHKI TPVQYEPKEA LGLLNGTAFS ASVAGLATYE AENLASLTQL TTAMAVEALK
GTDASFAPFI HEIARPHPGQ IKSAKFIRAL LSGSRLAEHL ENEKHVLFSE DNGTLRQDRY
TLRTASQWVG PGLEDIENAK RSVDIEINST TDNPMIDPYD GDGRIHHGGN FQAMAMTNAV
EKIRLALCAM GKMTFQQMTE LVNPAMNRGL PANLASTPDL SLNFHAKGID IALASVTSEL
MFLGNPVSTH VQSAEMANQA INSLALISGR QTLQAIECLS MIQAWSLYLL CQALDIRALQ
YKVAEQLPTL ILASLHSHFG EWMDETKQQE IAAQVLKSMS KRLDETSSKD LRDRLVETYQ
DASSVLVRYF SELPSGGGAD PLRNIVKWRA TGVADTEKIY RQVTIEFLDN PYACHASHLL
GKTKRAYEFV RKTLGVPMHG KENLNEFKGE FEQWNTTGGY VSVIYASIRD GELYNMLSEL
ERDL
