ID M9M0D4_PSEA3 Unreviewed; 726 AA.
AC M9M0D4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phenylalanine and histidine ammonia-lyase {ECO:0000313|EMBL:GAC73305.1};
GN ORFNames=PANT_9c00054 {ECO:0000313|EMBL:GAC73305.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC73305.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR EMBL; DF196775; GAC73305.1; -; Genomic_DNA.
DR AlphaFoldDB; M9M0D4; -.
DR STRING; 1151754.M9M0D4; -.
DR OrthoDB; 1030318at2759; -.
DR Proteomes; UP000011976; 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:GAC73305.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976}.
SQ SEQUENCE 726 AA; 79285 MW; F96DD32AB6070B06 CRC64;
MAPTADVLPA AEASTRPGLL VQPSDTKLRK ASSFRTEQVV IDGNNLKIQG LVASARYGHI
PILDNSPAVR KRIDDSVNSL IAKLDRGESI YGINTGFGGS ADSRTANTRA LQLALLQMQQ
CGVLPVPSTF PTGEPSSAPF ALPLTDTETS LVMPEAWVRG AIVVRLSSLM RGHSGVRWEV
LDKMQKLFLQ NNVTPVVPVR SSISASGDLS PLSYVAGALA GQRGIYCWVT DKKSGQRVKV
TADEACRMHG IEPVLYEPKE ALGLLNGTAF SASVAGLATY EAEKLAQLTQ LTTAMAVEAL
KGTDASFAPF IHEVARPHPG QIKSARYIRA LLSGSKLAEH LENEKHVLFS EDNGTLRQDR
YTLRTASQWV GPGLEDIENA KRSVDIEINS TTDNPMIDPY DADGRIHHGG NFQAMAMTNA
VEKIRLALCA MGKMTFQQMT ELVNPAMNRG LPANLASTPD LSLNFHAKGI DIALASVTSE
LMFLGNPVST HVQSAEMANQ AINSLALISG RQTLQAVECL SMIQAWSLYL LCQALDIRAL
QYKVAEQLPA MVLASINSHF GEWMDEAKQA EIALLVFKSM SKRLDETSSK DLRDRLVETY
QDASSVLVKY FSELPSGGGA DPLRNIVKWR AAGVAETEKI YRDVTVEFLD NPYACHASHL
LGKTKRAYEF VRKTLGVPMH GKENLYEFKG EFSQWNTTGG YVSVIYASIR DGELYDMLAE
LEKEIY
//
