ID   H6C924_EXODN            Unreviewed;       576 AA.
AC   H6C924;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000313|EMBL:EHY60601.1, ECO:0000313|EMBL:EHY60602.1};
GN   ORFNames=HMPREF1120_08555 {ECO:0000313|EMBL:EHY60602.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY60602.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY60602.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY60602.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; JH226136; EHY60601.1; -; Genomic_DNA.
DR   EMBL; JH226136; EHY60602.1; -; Genomic_DNA.
DR   RefSeq; XP_009161062.1; XM_009162814.1.
DR   RefSeq; XP_009161063.1; XM_009162815.1.
DR   STRING; 858893.H6C924; -.
DR   GeneID; 20313194; -.
DR   VEuPathDB; FungiDB:HMPREF1120_08555; -.
DR   eggNOG; KOG0628; Eukaryota.
DR   HOGENOM; CLU_011856_3_1_1; -.
DR   OMA; NPGFNWS; -.
DR   OrthoDB; 47798at2759; -.
DR   Proteomes; UP000007304; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT   MOD_RES         357
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   576 AA;  63135 MW;  9144E57596AEE9EC CRC64;
     MSRLGFLAYM LRRSIYRSPG FHKAFSISSI SHRLVSRSAR SAMDADEFRE AAHAAIEEII
     AYNQNIADYP VLPKVKPGFL APQLPKTAPE KPQPWSQIQP DIASKIVPGL THWQSPKFMA
     FFPAGVTYPS MLGELYSAAF TAPAFNWLCS PSCTELETVV MDWLARAFDL PQEFLSTSAT
     GGGGTIQGSA SEAVVTCMVA ARERYLHTKC DAEGLAPGSQ EREDRIAFLR GRLVALSSDQ
     AHSSTQKGAL IAGTRYRSIA AKLDNQLSLK AEALEAVLAQ CKAEGLEPYY ITLTLGTTST
     CAVDDFAGLA PILKAHPNLW VHVDAAYAGA ALVCPEYSSK YSPLMKIADS FNMNMHKWLL
     VNFDASCLFV QNRNHLTRAL SISAAYYANK HTDSGLVTDY RDWQIPLGRR FRALKIWFVM
     RNYGVEGLQN HIRKTVAIGE TFADLVRGRS DLFELVTEPA FALTCFRVKP SVLMEIQSTA
     ETEADFVPQT AAAQQHEQEA NAATKHIGEL INERGEVFLT CSSSAGKSFI RVVSGNPNAE
     EKYVRAAFDV IVKTTEEVLG NRRSADGKAV ADGHAG
//