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Database: UniProt
Entry: A0A162HVT5_9HYPO
LinkDB: A0A162HVT5_9HYPO
Original site: A0A162HVT5_9HYPO 
ID   A0A162HVT5_9HYPO        Unreviewed;       753 AA.
AC   A0A162HVT5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phenylalanine ammonia-lyase {ECO:0000313|EMBL:OAA44075.1};
GN   ORFNames=BBO_04431 {ECO:0000313|EMBL:OAA44075.1};
OS   Beauveria brongniartii RCEF 3172.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC   Beauveria brongniartii.
OX   NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA44075.1, ECO:0000313|Proteomes:UP000076863};
RN   [1] {ECO:0000313|EMBL:OAA44075.1, ECO:0000313|Proteomes:UP000076863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA44075.1,
RC   ECO:0000313|Proteomes:UP000076863};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA44075.1}.
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DR   EMBL; AZHA01000011; OAA44075.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162HVT5; -.
DR   OrthoDB; 1030318at2759; -.
DR   Proteomes; UP000076863; 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:OAA44075.1}.
FT   REGION          729..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  81579 MW;  CFA6A1BE7C2E3BAD CRC64;
     MAKINGVVPN GVDKQWPTPH TDNLLLSWNK LRQLVRDGSF EINGESLQVA AVVATARHGC
     RATVKKDPDV QSRIESSVAT LHDYLDKGYF LYGVNTGFGG SADTRTKDLY GLQRALMQHT
     QSAILTAEDK SDTQSSNEYL GSHSMPSAWT RATMLLRCNT NIRGHSAITA NTVETMIKLL
     HHDIMPIVPL RGSVSASGDL MPLSYVAGAI QGSPDIFVRV GCKISRHKIM TAEQALRGAG
     ITPVVLCPKE GLSLINGTSA AAAVATLGLW EANQLALVSQ MLTALSSEAL GANDEWAHPF
     IAAVRPHSGQ IEAAQNIRTF IKGSKLVYGL EQTKDRFKAG LAQERYALRS SPQWLSPLLE
     DLMSAEKQLT VEINSTTDNP VVNVADNDIH CGANFQATAV TSATEKIRLA LQSIGKMLFA
     QTSEMINHDL SNGLPPNLAA DDPSLSFCLK GIDVNTAAYT SELGFLANPV SNHVQSAEMH
     NQAINSLGLL SARKTMEAVE VLSLIVANCM YTGCQGADIR TMHKTFLIRL TDPIRDLIST
     LTGGKENTEV ERASESTTFF DRFWREFEDA WYRTAHLDAG ERCEKVSKTL VTVMVMHSTQ
     IGADGLSASK LEESRQALSA LTLETYTAHR GSFFRNPTTS RFLGDGTRAM YLFVREQLGV
     PMHRGLVEHP VAGAADGNMI DGRPKKTIGS WVAIIYEAIR AGSFSDAMLE FVGASTDVKW
     GANGKQYNNG AQANGSQNGH QSTNGQLDVN GSH
//
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