GADL1_BOVIN
ID GADL1_BOVIN Reviewed; 521 AA.
AC A6QM00;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 77.
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;
GN Name=GADL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=23038267; DOI=10.1074/jbc.m112.393728;
RA Liu P., Ge X., Ding H., Jiang H., Christensen B.M., Li J.;
RT "Role of glutamate decarboxylase-like protein 1 (GADL1) in taurine
RT biosynthesis.";
RL J. Biol. Chem. 287:40898-40906(2012).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-cysteate = CO2 + taurine; Xref=Rhea:RHEA:25221,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58090,
CC ChEBI:CHEBI:507393; 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 -!- TISSUE SPECIFICITY: Expressed at highest levels in skeletal muscles.
CC Also detected heart, spleen and rumen. {ECO:0000269|PubMed:23038267}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI48147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC148146; AAI48147.1; ALT_INIT; mRNA.
DR RefSeq; NP_001095751.2; NM_001102281.2.
DR RefSeq; XP_010815825.1; XM_010817523.2.
DR AlphaFoldDB; A6QM00; -.
DR SMR; A6QM00; -.
DR STRING; 9913.ENSBTAP00000009385; -.
DR PaxDb; A6QM00; -.
DR Ensembl; ENSBTAT00000009385; ENSBTAP00000009385; ENSBTAG00000007131.
DR GeneID; 614548; -.
DR KEGG; bta:614548; -.
DR CTD; 339896; -.
DR VEuPathDB; HostDB:ENSBTAG00000007131; -.
DR VGNC; VGNC:29210; GADL1.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000158391; -.
DR InParanoid; A6QM00; -.
DR OMA; DESDMLY; -.
DR OrthoDB; 810772at2759; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000007131; Expressed in infraspinatus muscle and 64 other tissues.
DR ExpressionAtlas; A6QM00; baseline.
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..521
FT /note="Acidic amino acid decarboxylase GADL1"
FT /id="PRO_0000312223"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q80WP8"
SQ SEQUENCE 521 AA; 59380 MW; E9A0F16C479295DB CRC64;
MSLLPDRERA PDGDISPQEM VPSRKNVVLV DGVILNGPAT DVKAGEKFVE DACRLIMEEV
VLKATDINEK VCEWRPPEEL KRLLDLELRD AGEPHHRLLQ RCQDVIRYSV KTNHPRFFNQ
LYAGLDYYSL VARFMTEALN PSVYTYEVSP VFLLVEEAVL KKMIEFIGWK EGDGIFNPGG
SVSNMYAMNL ARYKYCPDIK EKGLSGLPRL ILFTSAECHY SMKKSASFLG IGTENVCFVE
TDGRGKMIPE ELEKRVQEAK KEGAAPFLVC ATSGTTVLGA FDPLDEIADI CERHGLWLHV
DASWGGSALM SRKHRRLLQG IHRADSVAWN PHKMLMAGIQ CCAFLVKDKS DLLKRCYSAN
ASYLFQQDKF YDVSYDTGDK SIQCSRRPDA FKFWLAWKAL GTLGLEERVN RALALSRYLV
EEIKKREGFK LLMEPEYANI CFWYIPPSLR QMEEGPEFWA KLHLVAPAIK ERMMKKGSLM
LGYQPHQGKV NFFRQVVISP QVSREDMDFL LDEIDLLGKD M
