ID   GADL1_XENTR             Reviewed;         511 AA.
AC   Q28D99;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Acidic amino acid decarboxylase GADL1;
DE   AltName: Full=Aspartate 1-decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.11 {ECO:0000250|UniProtKB:Q80WP8};
DE   AltName: Full=Cysteine sulfinic acid decarboxylase;
DE            Short=CSADC;
DE            EC=4.1.1.29 {ECO:0000250|UniProtKB:Q80WP8};
DE   AltName: Full=Glutamate decarboxylase-like protein 1;
DE   Flags: Fragment;
GN   Name=gadl1; ORFNames=TGas121d14.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-
CC       alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine,
CC       hypotaurine and taurine, respectively. The preferred substrate is L-
CC       aspartate. Does not exhibit any decarboxylation activity toward
CC       glutamate. {ECO:0000250|UniProtKB:Q80WP8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57966; EC=4.1.1.11;
CC         Evidence={ECO:0000250|UniProtKB:Q80WP8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-sulfino-L-alanine + H(+) = CO2 + hypotaurine;
CC         Xref=Rhea:RHEA:16877, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57853, ChEBI:CHEBI:61085; EC=4.1.1.29;
CC         Evidence={ECO:0000250|UniProtKB:Q80WP8};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q80WP8};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q80WP8}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ83832.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR855620; CAJ83832.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001039075.1; NM_001045610.1.
DR   AlphaFoldDB; Q28D99; -.
DR   SMR; Q28D99; -.
DR   PaxDb; Q28D99; -.
DR   GeneID; 733871; -.
DR   KEGG; xtr:733871; -.
DR   CTD; 339896; -.
DR   Xenbase; XB-GENE-5721903; gadl1.
DR   eggNOG; KOG0629; Eukaryota.
DR   InParanoid; Q28D99; -.
DR   OrthoDB; 810772at2759; -.
DR   Reactome; R-XTR-1614558; Degradation of cysteine and homocysteine.
DR   Reactome; R-XTR-8963693; Aspartate and asparagine metabolism.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004782; F:sulfinoalanine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR039025; GADL1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR45677:SF1; PTHR45677:SF1; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           <1..511
FT                   /note="Acidic amino acid decarboxylase GADL1"
FT                   /id="PRO_0000312226"
FT   MOD_RES         323
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80WP8"
FT   NON_TER         1
SQ   SEQUENCE   511 AA;  58815 MW;  D454A94A9FA8CC26 CRC64;
     HDIDKNKQET RPMKRNAVLV DGVVLNGPII DSSSGEKFVE DVYRILMNEL VYKASDINQK
     VCEWQEPEQL KKLLDLNIKD NGEPHEKLLQ LCKNVIKYSV KTSHPRFFNQ LYAGMDHYSL
     AARFITEALN PSVYTYEVSP VFILTEEAIL KKMIEFLGWK EGDGIFSPGG SVSNMYAVNL
     ARYKYCPDIK QKGLSSAPRL VMFTSEECHY SMKKAAAFLG IGTENVYFVK TDDRGKMIPE
     ELENQIQRAK KEGAVPFLVS ATSGTTVLGA FDPLDDIANI CEKHKLWFHV DASWGGSALM
     SQKYRKRLHG IHRADSVAWN PHKMLMAGIQ CCALLVRDNS GLLKRCHSAE ATYLFQQDKF
     YDVQYDTGDK SIQCSRRADA FKFWMMWKAL GTTGLEERIN RALALTRYLA SEIKKRDGFE
     LLWEPEYANT CFWYIPPSFR NMEKGPEYWR KFSNVAPTIK ERMMKKGSMM VGYQPHRDKV
     NFFRHIVISP QVSREDMDFV LDEIERLGRD L