ID A0A1S3KCH4_LINUN Unreviewed; 477 AA.
AC A0A1S3KCH4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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};
GN Name=LOC106180504 {ECO:0000313|RefSeq:XP_013419956.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013419956.1};
RN [1] {ECO:0000313|RefSeq:XP_013419956.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013419956.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_013419956.1; XM_013564502.2.
DR AlphaFoldDB; A0A1S3KCH4; -.
DR STRING; 7574.A0A1S3KCH4; -.
DR EnsemblMetazoa; XM_013564502.2; XP_013419956.1; LOC106180504.
DR GeneID; 106180504; -.
DR KEGG; lak:106180504; -.
DR InParanoid; A0A1S3KCH4; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000085678; Unplaced.
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 GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06450; DOPA_deC_like; 1.
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 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; PF00282; Pyridoxal_deC; 1.
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, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 477 AA; 53509 MW; 1A5B0AE5574C3B94 CRC64;
MDAAEFRQRG KEMVDTVADY LENIQKRPVF PSVQPGYIRE LVPESAPETA ESWEDLVGDI
ERVVMPGVTH WHHPQFHAYF PTANSYAALC ADMLSDAIGC IGFSWASSPA CTELEMVMMD
WLGKMLDLPQ EFLFCSGGKG GGVIQGTASE ATLVALLAAR NQTIHREKEA NPALTEADIM
ARMVGYCSDQ AHSSVERAGL LGAVKIVKLS SDKKQSLRGE TLAQAVQKDK EKGLIPFFVC
GTLGTTPSCA FDNIEELGAV CNLEKIWLHI DAAYAGSAFI CPEFRYLLSG VQFADSFNFN
PHKWLRVTFD CSAMWIKDSS KLVDAFNVDP LYLKHDNQGK VPDYRHWQIP LGRRFRSLKL
WFVLRLHGIK GLQEYIRQHV KLAHEFEALV LADERFEIVA EVVLGLVCFR LKGANDINEQ
LLQRINQDGR IHLVPSKIGN TYFLRFAVCA PYAESKDVQF AWTVLTELAT ELLKEKK
//
