ID A0A0L0V6B7_9BASI Unreviewed; 682 AA.
AC A0A0L0V6B7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phenylalanine ammonia-lyase {ECO:0000313|EMBL:KNE94736.1};
GN ORFNames=PSTG_11924 {ECO:0000313|EMBL:KNE94736.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE94736.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNE94736.1}.
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DR EMBL; AJIL01000110; KNE94736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0V6B7; -.
DR STRING; 1165861.A0A0L0V6B7; -.
DR OrthoDB; 1406325at2759; -.
DR Proteomes; UP000054564; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016841; F:ammonia-lyase activity; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
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, ECO:0000313|EMBL:KNE94736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054564}.
SQ SEQUENCE 682 AA; 74589 MW; 32B4B02BC4BDAFDF CRC64;
MSRPHAALCH ALITPLLLDP VPNNSETVTV IIDGYSLTIQ DLIRATTRIP KYEISKDPKT
SSKIASSLKF MLDRANQSTY GVTTGFGAAA TTRTHEVGAL QVSIIEHLLC GLTGVKNVTR
LTIGENPSIP IHHNIMAESV VRTAILIRVN SLSRGHSAVR FELLESLVEL LNRNITPIVP
LRGTISASGD LTPLAYVAGA VCGHPDVYVI DRSNPTEPKI MNSQECMKKH NLAPLVLGPK
EGLAIANGTA FSAGLGSIVI YETHILALLS QVLTAMTVET LVGQIGAFHP FIHKTARPHS
GQIEVAENVY KFLKESKLVE NEDQEEGDDD FEREKSNQIL RQDRYPLRTA PQWIGPQLED
ILVAHQTISV ELNSTTDNPL VDIENGKLHH GGNFQATSIA TSMEKTRLSI AAIGKIMFAQ
LTELNNSNMN KGLPSCLNGS EPSINYHTKG LDTHCAAYCS ELQFLASPVT THVQSAEGHN
QSINSLAFIS ARKTAESIEI LKMLMASHLY CLCQALDLRV IEIRLKESLV EIFKETLQSS
FGDLKISVDE VVDKFMNRRE TSPSLDSSDR VKECIEVTIP LIVKQFESDA QSIPVGSVTQ
YMSTSTRLIL NKLEELSTGT LPTSQYLGSS RVIYDFVRVE LDVQFRVGDV AGGVHTSIGS
SVDRILCCLS TPSFLNVLLS LF
//
