ID H3DHQ4_TETNG Unreviewed; 577 AA.
AC H3DHQ4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000020048.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000020048.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU000382}.
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DR AlphaFoldDB; H3DHQ4; -.
DR STRING; 99883.ENSTNIP00000020048; -.
DR Ensembl; ENSTNIT00000020279.1; ENSTNIP00000020048.1; ENSTNIG00000016929.1.
DR GeneTree; ENSGT00940000155526; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; H3DHQ4; -.
DR OMA; FKSEPQH; -.
DR TreeFam; TF314688; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
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 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.
PE 3: Inferred from homology;
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:UP000007303}.
FT MOD_RES 388
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 577 AA; 64434 MW; 4652024C7B3F449A CRC64;
MAASAPSSSG GEAKPTLLPP PGSSYDAWCG VAHGCTRKLG MKICGFLQKN NSLEESARLT
RAHGAARNAQ SWERAETDFS NMFARDLLPA KNGEEPTLQF LLEVVEILTS YVRKTFDRST
KVDFHHPHQL LEGMEGFNLE LSDQPESLEQ ILVDCRDTLK YGVRTGHPRF FNQLSTGLDI
VGLAGEWLTS TANTNMFTYE IAPVFVLMEQ LTLKKMREIV GWPGGEGDGI FSPAGGAISN
MYSVMIARYK FFPVVKTKGM AAAPRLVLFT SEHSHYSIKK ASAAGFGTEN LILLNTDERG
RVIPADLEAK VLEAKQKGYV PMYVNATAGT TVYGAFDPIN EIADICEKYN MWLHVDGAWG
GGLLMSRKHR HKLSGVERAN SVTWNPHKMM GVPLQYSAIL VRERGLLQGC NSMCAGYLFQ
QDKQYDVTYD TGDKAIQCGR HVDIFKFWLM WKAKGTVGFE QHIDRCLELS AYLYQKIKNR
AGFEMVFSGE PQHTNVCFWY LPPSLRNLPD GKNRRERLHK VAPKIKALMM ESGTTMVGYQ
PQGDKVNFFR MVVSNPAATC SDIDFLVDEI ERLGNDL
//
