ID A0A0D2DXU4_9EURO Unreviewed; 560 AA.
AC A0A0D2DXU4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_00559 {ECO:0000313|EMBL:KIW47908.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47908.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW47908.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47908.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) 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; KN847332; KIW47908.1; -; Genomic_DNA.
DR RefSeq; XP_016268124.1; XM_016401071.1.
DR AlphaFoldDB; A0A0D2DXU4; -.
DR STRING; 215243.A0A0D2DXU4; -.
DR GeneID; 27352633; -.
DR VEuPathDB; FungiDB:PV06_00559; -.
DR HOGENOM; CLU_011856_3_1_1; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000053342; 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:UP000053342}.
FT MOD_RES 348
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 560 AA; 61631 MW; 9C480E3C7199A719 CRC64;
MFGRSLSGHC SSPTSLISGF SLTRYIHGAQ RLAMNSDEFR KAAHAAIEEI IAYNENVADY
PVLPTIKPGF LAPQLPRSAP EKPQAWSDIQ PDIASKIVPG LTHWQSPKFM AFFPAGVTYP
SMLGEMYSAA FTAPAFNWLC SPSCTELETV VMDWLAQAFD LPEEFLSTSP NAGGGTIQGS
ASEAVVTCMV AARERYLHGK CDAEGLKPDS EERADRIAYL RGRLIALSTD QTHSSTQKGA
LIAGTRYRAI PTKLENGLSL TGQGLEAALE QCKKEGLEPY YITLTMGTTS TCATDDFESL
APVLKSKPDL WVHIDAAYAG AALICPEFSS KYSPWMKIAD SYNMNMHKWL LVNFDASCLF
VQNRNHLTRA LSIEAAYYVN KHTDSGLVTD YRDWQIPLGR RFRALKIWFV MRTYGLEGMR
AHIRKTVAIG EVFAGLIRGR SDLFEIVAKP AFGLTCFRVK PSLLSPQGST ETDSTFNPRI
SAEQQREQDA NAVTKHIGEL INERGEVFLT CSSTAGKAFM RVVSGNPNAE EKYVRAAFDT
IVETTEEVLA ARGKKANGHI
//
