ID A0A1V8TU45_9PEZI Unreviewed; 553 AA.
AC A0A1V8TU45;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A48_00250 {ECO:0000313|EMBL:OQO14868.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO14868.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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}.
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:OQO14868.1}.
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DR EMBL; NAJO01000001; OQO14868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TU45; -.
DR STRING; 1507870.A0A1V8TU45; -.
DR InParanoid; A0A1V8TU45; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000192596; 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:UP000192596}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 553 AA; 61087 MW; 36B886EE2D770988 CRC64;
MTQDLVNGNG HGPSSEVDGR TVPPLGLTGQ QFINAATNAV QDIEKYYSTI EDRPVLPSIS
PGYLQKLLPS HAPQDGEPWQ DIANDIEAKI MPGVTHWQHP KYMAFFSASS TYPGILGEMW
SAALTAPAFN WICSPVVTEL ETVVLDWLAQ ILALSKAFMS SGQGGGVIQG SASEAIVTCM
IAARERFVRR QLEGEGMTDE EESEDRACEI RSKLVALGSE QSHSSTKKGA VIAGTRYRSI
ATARKDDYAL TGASLRAKLE ELTTKGLQPY YLTITLGTTN TCAVDDFASI AEVAKDYPDL
WIHCDAAWAG AALVLPEYQH LSAQLSFVDS FDINMHKWLL TNFDASCLYV QKRKDLTDAL
SITPAYLKNQ FTDSGLVTDY RDWQIPLGRR FRALKVWFVL RTWGVSGLQQ HVQHHIHLGN
LFADLVRSRD DLFTMLTPPA YALTVFTVNA RRRQPVSIGH TTANGADPRS DQNSHVTITP
ATKTDDVAAA NEATKAVYSI IDERQEFFLT STFIDGVFAI RVVSANPLAE ERYIRQVFDQ
LVKVGEQVLE ETC
//
