ID A0A094AGH5_9PEZI Unreviewed; 837 AA.
AC A0A094AGH5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE RecName: Full=Phenylalanine ammonia-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=V491_00300 {ECO:0000313|EMBL:KFY28746.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY28746.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY28746.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY28746.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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:KFY28746.1}.
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DR EMBL; JPJT01000137; KFY28746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094AGH5; -.
DR SMR; A0A094AGH5; -.
DR HOGENOM; CLU_014801_3_1_1; -.
DR Proteomes; UP000029338; 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:SF7; HISTIDINE AMMONIA-LYASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000029338}.
FT REGION 66..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 91193 MW; 57092FCC898CBA6B CRC64;
MQVMESTIKR NLDRKGSCQE LQIRGEDTKS IAMGNAWAVT QLDLNKIQEH QHSLSHESIG
PYLASSMDDP ISCKENGSAS ASSLTRSPAA SLNSDVSNLT SSVDDFSSRN EIESTFPISR
DPPHKDDRQL LKEGLSHSAI QIGQTQMLEE FKGSDKFVVL NGNNLDIPSL VAVARHGSRV
CIDDDPSMAE RIQASVDFLK QELDSGHSIY GITTGFGGSA NTNTDQFEKL QVALLQMQLC
GILPEHSNMP QQKPAARDSS LYYEAGLTTM SMPESWVRAA MVVRINTLMR GNSAVRLQVL
QSVEKLLQND IVPFIPLHGS ISASGDLSPL SYIAGAIEGN PDVYVWTGPS TNRILVASNE
VLEASGIELV RFGPKEGLGI LNGTAFSVGV AALAMYEANN LALMAQILTA MGVEALTGST
ESFEPFIAAV RPHPGQSEAA RNIAKALHGS KLVQEARDED TRSLRQDRYA LRTASQWLGP
SLEDLRLATE QLETELNSTT DNPLIDADSR RIFHGGNFQA ASVTSSTEKT RLALQMIGKL
IFAQSSELLN TKINNGLPPN LALDEPSLSY TLKGVDINMA AYMAELGFLA NPVSSHVQSA
EMGNQSLNSM ALVSARYTHK AIDIVTMMTS AYLYSLCQAV DLRALHEIYL TALHPKFDEI
TANYLKQATK CIEVKRWQDA IWSAFKEKLA LTVTEDSATR FMETARALQP ILLDIMASST
QSPDSGLRSN TPAVTMIQDC TDRLATSARD IFVQSRVSYA KQPDASPFLG AAASSMYNFV
RNELSIPLHK GIVDYPVAAG RDSKLDVKQL NTGSWVSKIY TAMRDGRVAK MLRNCIG
//