ID A0A1S3RW84_SALSA Unreviewed; 482 AA.
AC A0A1S3RW84;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=LOC106605416 {ECO:0000313|RefSeq:XP_014056524.1,
GN ECO:0000313|RefSeq:XP_014056525.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014056525.1};
RN [1] {ECO:0000313|RefSeq:XP_014056524.1, ECO:0000313|RefSeq:XP_014056525.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014056524.1,
RC ECO:0000313|RefSeq:XP_014056525.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine
CC (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
CC {ECO:0000256|ARBA:ARBA00037256}.
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 -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine
CC from L-tyrosine: step 2/2. {ECO:0000256|ARBA:ARBA00037889}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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_014056524.1; XM_014201049.1.
DR RefSeq; XP_014056525.1; XM_014201050.1.
DR Ensembl; ENSSSAT00000009683; ENSSSAP00000009065; ENSSSAG00000004522.
DR GeneID; 106605416; -.
DR KEGG; sasa:106605416; -.
DR OrthoDB; 47798at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR Bgee; ENSSSAG00000004522; Expressed in actinopterygian pyloric caecum and 9 other cell types or tissues.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
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 Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
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:UP000087266}.
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 482 AA; 54673 MW; C41FF98224572607 CRC64;
MDAAEFRRRG KEMVDLIADY LENIEQRPVY PDVEPGYLRS LIPEEAPEEP ETYEDVVKDI
ERVIMPGVTH WHSPYFYAYF PTANSFPAML ADMLSGAIGC IGFSWAASPA CTELETVMMD
WLGKMLKLPE DFIAGTHGQG GGVIQGTASE ATLVALLAAR SRAVRMILAS DPQRPETGIT
SKLVAYSSDQ AHCSVERAGM IAGVRMKKIP TEQSDKYAVQ GETLRRMIQE DKAAGLIPFY
FCATLGTTPS CAFDHITELG PICNAEKIWM HIDAAYAGSS FICPEFRPLL NGIEFADSFN
FNPHKWLLVN FDCSTMWVRK RSDLIGAFKM DPLYLKHDHQ ESGLVTDYRH WQIPLGRRFR
SLKMWFVFRM YGLKGLQDYI RKHVELAKEF ESLVRADQRF EISADVVLGL VCFRLKGSNE
VNETLLKRIN NGRKIHLVPC QLSGQFVLRF AVCARTTESR HIREAWRLIT QLAEEVMQEL
PH
//
