ID A0A0D2U386_GOSRA Unreviewed; 721 AA.
AC A0A0D2U386;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=B456_009G416300 {ECO:0000313|EMBL:KJB62426.1}, Gorai_013615
GN {ECO:0000313|EMBL:MBA0596808.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB62426.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB62426.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
RN [2] {ECO:0000313|EMBL:MBA0596808.1, ECO:0000313|Proteomes:UP000593578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8 {ECO:0000313|EMBL:MBA0596808.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0596808.1};
RX PubMed=30476109;
RA Grover C.E., Arick M.A. 2nd, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Frelichowski J.E., Scheffler J.A., Scheffler B.E.,
RA Wendel J.F.;
RT "Insights into the Evolution of the New World Diploid Cottons (Gossypium,
RT Subgenus Houzingenia) Based on Genome Sequencing.";
RL Genome Biol. Evol. 11:53-71(2019).
RN [3] {ECO:0000313|EMBL:MBA0596808.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=8 {ECO:0000313|EMBL:MBA0596808.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:MBA0596808.1};
RA Grover C.E., Arick M.A. II, Thrash A., Conover J.L., Sanders W.S.,
RA Peterson D.G., Scheffler J.A., Scheffler B.E., Wendel J.F.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM001748; KJB62426.1; -; Genomic_DNA.
DR EMBL; JABEZZ010000009; MBA0596808.1; -; Genomic_DNA.
DR RefSeq; XP_012443197.1; XM_012587743.1.
DR RefSeq; XP_012443198.1; XM_012587744.1.
DR AlphaFoldDB; A0A0D2U386; -.
DR STRING; 29730.A0A0D2U386; -.
DR EnsemblPlants; KJB62426; KJB62426; B456_009G416300.
DR GeneID; 105768043; -.
DR Gramene; KJB62426; KJB62426; B456_009G416300.
DR KEGG; gra:105768043; -.
DR eggNOG; KOG0222; Eukaryota.
DR OMA; GNFHGDY; -.
DR OrthoDB; 1030318at2759; -.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000032304; Chromosome 9.
DR Proteomes; UP000593578; Unassembled WGS sequence.
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; 1.20.200.10; 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:UP000032304}.
SQ SEQUENCE 721 AA; 78341 MW; 1B68E13131EACEF6 CRC64;
MDMITQNAQQ SSSLESFCTT TTTAKGGVVD PLNWGVAAKS LQGSHLDEVK RMVAEYRRSL
VKLGGETLTI SQVAAIATRD LGVKVELSED ARAGVKASAD WVLDGMNKGT DSYGVTTGFG
ATSHRRTKQG AALQKELIRF LNAGIFGNGI ESCHTLPHSA TRAAMLVRIN TLLQGYSGIR
FEILEAITKL LNHNVTPCLP LRGTITASGD LVPLSYIAGL LTGRPNSKAV GPNGEPLDAQ
EAFHVAGIDS GFFVLQPKEG LALVNGTAVG SGLASMVLFE ANILAVLSEI LSAIFAEVMN
GKPEFTDHLT HKLKHHPGQI EAAAIMEHIL EGSSYVKAAK KLHEMDPLQK PKQDRYALRT
SPQWLGPQIE VIRFATKSIE REINSVNDNP LIDVSRNKAL HGGNFQGTPI GVSMDNARLA
IAAIGKLMFA QFSELVNDFY NNGLPSNLSG GRNPSLDYGF KGAEIAMASY CSELQYLANP
VTNHVQSAEQ HNQDVNSLGL ISSRKTAEAV DILKLMSSTF LVALCQAIDL RHVEENLRNT
VKNTVSQIAK KTLTTGANGE LHPSRFCEKD LLKAVDREYV FAYIDDPCSA TYPLMQKLRQ
VLVEHALTNG ESEKNTSTSI FQKITDFEEE LQAVLPKEVE SARVTLENGN AAIPNMIKDC
RSYPLYKFVR EELGTGLLTG EKVKSPGEEF DKVFTAMCQG KIIDPMLECL KEWNGAPLPI
C
//
