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Database: UniProt
Entry: M3ZEY7_XIPMA
LinkDB: M3ZEY7_XIPMA
Original site: M3ZEY7_XIPMA 
ID   M3ZEY7_XIPMA            Unreviewed;       480 AA.
AC   M3ZEY7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000000779.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000000779.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000000779.1};
RG   Ensembl;
RL   Submitted (JUL-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_005811067.1; XM_005811010.1.
DR   AlphaFoldDB; M3ZEY7; -.
DR   STRING; 8083.ENSXMAP00000000779; -.
DR   Ensembl; ENSXMAT00000000782.2; ENSXMAP00000000779.1; ENSXMAG00000000755.2.
DR   GeneID; 102226428; -.
DR   KEGG; xma:102226428; -.
DR   CTD; 1644; -.
DR   eggNOG; KOG0628; Eukaryota.
DR   GeneTree; ENSGT00940000156004; -.
DR   HOGENOM; CLU_011856_3_0_1; -.
DR   InParanoid; M3ZEY7; -.
DR   OMA; NPGFNWS; -.
DR   OrthoDB; 47798at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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:0007420; P:brain development; IEA:Ensembl.
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:SF167; 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|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT   MOD_RES         303
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   480 AA;  54703 MW;  D64808947FB99108 CRC64;
     MDAAEFRRRG KEMVDYMADY LENIEQRPVY PDLEPGYLRS LIPTEAPLEP ESYEEIMHDV
     ERVIMPGITH WHSPNFFAYF PAASSYPAMV ADMLCGAIGC IGFSWAASPA CTELETVMLD
     WLGKMLHLPE SFIAGTHGHG GGVIQGTASE ATLMSLLAAR CKTIRRVLVT DSKKSESEIL
     SKLVAYTSDQ AHSSVERAAL IGAVMMRKVP TDEHYAVREE MLRKMVEEDK AAGLIPFYFC
     ATLGTTPSCA FDHIMELGPL CNKENMWMHI DAAYAGSAFI CPEFRPLLNG IEYADSFNFN
     PHKWLLVNFD CSAMWVKKRA DIIGAFKMEP LYLKHENQES GLVTDYRHWQ IPLGRRFRSL
     KLWFVFRMYG LKGLQAHIRK QVALAKEFES LVRADKRFEI CAEVVLGLVC FRLKGSNELN
     QNLLKKITKS RELHLVPCQL SGRFVLRFAI CARRTESRHI QQAWRHITQL AFELLQEQPH
//
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