ID F1L026_ASCSU Unreviewed; 652 AA.
AC F1L026;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000256|ARBA:ARBA00040968};
DE EC=4.1.1.28 {ECO:0000256|ARBA:ARBA00038886};
DE AltName: Full=DOPA decarboxylase {ECO:0000256|ARBA:ARBA00041275};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY43480.1};
RN [1] {ECO:0000313|EMBL:ADY43480.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
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DR EMBL; JI168850; ADY43480.1; -; mRNA.
DR AlphaFoldDB; F1L026; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.640.10; 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 PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 2: Evidence at transcript level;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..652
FT /note="Aromatic-L-amino-acid decarboxylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003268238"
FT TRANSMEM 185..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 228..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 617
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 652 AA; 73554 MW; 236DFAAA76205A99 CRC64;
MTYHIWQLSV ILSFIPTVVP GKVKIGQFNC PVKLFVDKDS KSNFTTNIIT FFNKVSKNGY
QIIYADGANM CSRADIQFVL KTLTTTQITI ILNEHINRPC EVAIERGVIL QFFKIEDFIT
VHFINQGFRM PNIRFHDNEV DEIERFLNDV CMSIESNVRR RRQVRRTNDR REDEENSGTT
ATLNLWVIVL IAVIICLGFI IIITLFYVDH RKNLKRIAAL GKELMESTRS KTRTNLPPEM
MKKQQMDDED KKEKELRKID KAKKEGVDKV DEKNDESSKT LVLNARHVPL FVRDVFDIAN
FCLGYGGTEE VVKRDTKTIV SGTISKDNIG PNETSSSPVA IIDELETSIL PMFQQFPKMR
SHSFFPGVQS LADILIEFGC NLLAARGFIT DGSPGMLELE MVATSWVGKA LGLPSCFLPG
RKTRGGGLLL TTTTEGMFTA ILAARQKKLR EILNANATGC GKEKSHANEE DFLLNNMVAY
GCSEAHLSFD FGCRLAKVED KLISPDAEYT MNVDELEHEI MVDRLESSLL PSVLFQHAGV
IEDVKNKRTP VFINATFGSA HSCSLDKLDE ITKIAKKYNI WVHVDASYAG NYLVCPSYRS
LINGLENANS ISVNLHKCLT QSSHTTFFWT TDLRAVKDSI PQSQNMLKML HC
//
