ID M9LS54_PSEA3 Unreviewed; 815 AA.
AC M9LS54;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PANT_20d00029 {ECO:0000313|EMBL:GAC76266.1};
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:GAC76266.1, 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr) (TC
CC 2.A.96) family. {ECO:0000256|ARBA:ARBA00005587}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533}.
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DR EMBL; DF196786; GAC76266.1; -; Genomic_DNA.
DR AlphaFoldDB; M9LS54; -.
DR STRING; 1151754.M9LS54; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IPR000791; Gpr1/Fun34/SatP-like.
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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF01184; Gpr1_Fun34_YaaH; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT MOD_RES 625
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 815 AA; 87462 MW; 97698161F603AA21 CRC64;
MAVNNYKHPN LKEQWGLAED PNASDHIVTS RGQKLTRTVT AGGHDVDSSQ PGFPIYHRRI
ANPFPLVCIA TGASVLMLGF ILVRNRSITN PSIYMAMALP LGMFGNFAAC MFAFAEGSTY
LATISGTLAG LLGGTALQFL PWTGIQATYL AGGAAGLNEY YKAEAMVYFI ALIPIFLIFV
ASARTSGPVA GAALLITVAL ALLGAAYIGG AEDFMVAKAS GAIFIIIGIM LFYAALSVML
AEEGWKILPG TPTPTAPAYA GTRRHNCLAS QPHPSIYSTF ICASRSRNMD IEGFRKAGYA
AVDRICDYYA SLAERPVSAQ VQPGFLSASI PTSAPETGEA WERIDNDYHS VIMPGITHCF
EGALADLYCA SISNPGFNWS VSPSVTELEI LMVDWVGRML GLDDAFLSTS GTGGGIILGS
ASEVALTVAI AARERCIDRL TPQHPMPTVH TGTNGVGSLD ADQDVASAGQ SAAEVGADAT
LVANTRLAQW RGGLTSRLVM YGTTQTHTIA AKAALILGLD FRALPVSAES SYSLSGATLA
AAIAEDVALG RVPFMLIATI GTTSSGAVDN LTEIVEVVAK HPTLWLHIDA AYAGVCLSLP
ELRAEMHLDA INSAAVDSFS TNLHKWGLVQ FDCSPLHVRD RGDLSRALGI TPTYLRTKQA
DAGNVLDLRN LQISLGRRFR SLKVWFVLRS YGLEGFRKHL RTTMQLANHF ESLLRADDAG
LLEIVALPRW ALVVFRMNPK GEGVDVEQLN KAFWDDLEAQ SAHFVLTQTS LPEVGFCIRF
VVGSPQTQRH HVEHTWKLVA QTARSTWARF KTSCT
//
