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PAL2_ORYSI
ID   PAL2_ORYSI              Reviewed;         713 AA.
AC   A2X7F7; P53443; Q6K6P7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=ZB8; ORFNames=OsI_008000;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. IR36;
RX   PubMed=8534851; DOI=10.1007/bf00020983;
RA   Zhu Q., Dabi T., Beeche A., Yamamoto R., Lawton M.A., Lamb C.;
RT   "Cloning and properties of a rice gene encoding phenylalanine ammonia-
RT   lyase.";
RL   Plant Mol. Biol. 29:535-550(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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:0000250|UniProtKB:P24481}.
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:P24481};
CC   -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC       trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P24481}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA61198.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA61198.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; X87946; CAA61198.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM000127; EAY86767.1; -; Genomic_DNA.
DR   PIR; S66313; S66313.
DR   AlphaFoldDB; A2X7F7; -.
DR   SMR; A2X7F7; -.
DR   STRING; 39946.A2X7F7; -.
DR   PRIDE; A2X7F7; -.
DR   EnsemblPlants; BGIOSGA005998-TA; BGIOSGA005998-PA; BGIOSGA005998.
DR   Gramene; BGIOSGA005998-TA; BGIOSGA005998-PA; BGIOSGA005998.
DR   HOGENOM; CLU_014801_3_0_1; -.
DR   OMA; CNEMIDP; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000007015; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.10.274.20; -; 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..713
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000300256"
FT   ACT_SITE        106
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         200
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        199..201
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   713 AA;  76937 MW;  00394D799E57673F CRC64;
     MECENGRVSA NGMSGLCVAA PRADPLNWGK ATEEMTGSHL DEVKRMVAEY RQPLVKIEGA
     SLRIAQVAAV AAAGEARVEL DESARERVKA SSDWVMNSMM NGTDSYGVTT GFGATSHRRT
     KEGGALQREL IRFLNAGAFG TGTDGHVLPA EATRAAMLVR INTLLQGYSG IRFEILEAIA
     KLLNANVTPC LPLRGTITAS GDLVPLSYIA GLVTGRENAV AVAPDGSKVN AAEAFKIAGI
     QGGFFELQPK EGLAMVNGTA VGSGLASTVL FEANILAILA EVLSAVFCEV MNGKPEYTDH
     LTHKLKHHPG QIEAAAIMEH ILEGSSYMKH AKKLGELDPL MKPKQDRYAL RTSPQWLGPQ
     IEVIRAATKS IEREINSVND NPLIDVSRGK ALHGGNFQGT PIGVSMDNTR LAIAAIGKLM
     FAQFSELVND FYNNGLPSNL SGGRNPSLDY GFKGAEIAMA SYCSELQFLG NPVTNHVQSA
     EQHNQDVNSL GLISSRKTAE AIDILKLMSS TFLIALCQAV DLRHIEENVK SAVKSCVMTV
     AKKTLSTNST GDLHVARFCE KDLLKEIDRE AVFAYADDPC SHNYPLMKKL RNVLVERALA
     NGAAEFNADT SVFAKVAQFE EELRATLPGA IEAARAAVEN GTAAIPSRIT ECRSYPLYRF
     VREELGTKYL TGEKTRSPGE ELNKVLVAIN EGKHIDPLLE CLKEWNGEPL PIC
 
 
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