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Database: UniProt
Entry: H9GNM5_ANOCA
LinkDB: H9GNM5_ANOCA
Original site: H9GNM5_ANOCA 
ID   H9GNM5_ANOCA            Unreviewed;       418 AA.
AC   H9GNM5;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000016555.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000016555.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000016555.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000016555.3}
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   AlphaFoldDB; H9GNM5; -.
DR   STRING; 28377.ENSACAP00000016555; -.
DR   Ensembl; ENSACAT00000016881.3; ENSACAP00000016555.3; ENSACAG00000016649.3.
DR   eggNOG; KOG0629; Eukaryota.
DR   GeneTree; ENSGT00940000155526; -.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   TreeFam; TF314688; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000016649; Expressed in testis and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IBA:GO_Central.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
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; 2.
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:UP000001646}.
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   418 AA;  47289 MW;  7F4C9BDE13D9A5B3 CRC64;
     GMEGFNLELS DNPESLEQIL VDCRDTLKYG VRTGHPRFFN QLSTGLDIIG LAGEWLTSTA
     NTNMFTYEIA PVFVLMEQIT LRKMREIIGW TDKDGDGIFS PGGAISNMYS IMAARYKYYP
     EVKTKGMAAV PKLVLFTSEH SHYSIKKAGA ALGFGTENGY APLYVNATAG TTVYGAFDPI
     HEIADICEKY NLWLHVDAAW GGGLLMSSKH RHKLNGIERA NSVTWNPHKM MGVLLQCSAI
     LLREKGILQG CNQMCAGYLF QQDKQYDITY DTGDKAIQCG RHVDIFKFWL MWKAKGTVGF
     ETQINKCLEL SEYLYNKIKN REEFEMVFKG EPEHTNVCFW YIPPSLRGMP DSEERREKLH
     RVAPKIKALM MESGTTMVGY QPHADKVNFF RMVVSNPAAT KSDIDFLVEE IERLGQDL
//
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