GenomeNet

Database: UniProt
Entry: A0A0P7XHE7_SCLFO
LinkDB: A0A0P7XHE7_SCLFO
Original site: A0A0P7XHE7_SCLFO 
ID   A0A0P7XHE7_SCLFO        Unreviewed;       549 AA.
AC   A0A0P7XHE7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
GN   ORFNames=Z043_104968 {ECO:0000313|EMBL:KPP75765.1};
OS   Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX   NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP75765.1, ECO:0000313|Proteomes:UP000034805};
RN   [1] {ECO:0000313|EMBL:KPP75765.1, ECO:0000313|Proteomes:UP000034805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aro1 {ECO:0000313|EMBL:KPP75765.1};
RA   Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT   "The genome of the Asian arowana (Scleropages formosus).";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter
CC       gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
CC       {ECO:0000256|ARBA:ARBA00037700}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00036502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC         Evidence={ECO:0000256|ARBA:ARBA00036502};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPP75765.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JARO02001337; KPP75765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7XHE7; -.
DR   STRING; 113540.ENSSFOP00015039350; -.
DR   Proteomes; UP000034805; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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:SF5; GLUTAMATE DECARBOXYLASE 1; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034805}.
FT   MOD_RES         360
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   549 AA;  62553 MW;  C3F86E261E80D8F6 CRC64;
     MTRFLQKNNS LEERSRIVSS FKEKHSSSKN LRSCENSDTE SRFRRAETDF SNLFARDLLP
     AKNGEEPTMQ FLLEVVDILT NYVRKTFDRS TKVLDFHHPH QLLEGMEGFN LELSEQPESL
     EQILVDCRDT LKYGVRTGHP RFFNQLSSGL DIIGLAGEWL TSTANTNMFT YEIAPVFVLM
     EQLTLKKMRE IIGWPNGEGD GIFSPGGAIS NMYSVMVARY KYFPEAKTKG MSAVPRLVLF
     TSEHSHYSIK KSGAALGFGV ENVILLKSDE RGRVIPADLE AKIIEAKQKG YVPLFVNATA
     GTTVYGAFDP IDEIADLCEK YNMWLHVDGA WGGGLLMSRK HRHKLSGIER ANSVTWNPHK
     MMGVPLQCSA ILVREKGLLQ GCNQMCAGYL FQPDKQYDVT YDTGDKAIQC GRHVDIFKFW
     LMWKAKGTIG FEQHINKCLE LSEYLYNKIK DREGFEMVFR GEPQHTNVCF WYVPPSLRGM
     PDCEERRERL HKVAPKIKAM MMESGTTMVG YQPQGDKVNF FRMVISNQAA TKSDIDFLIE
     EIERLGQDL
//
DBGET integrated database retrieval system