ID G3TUV0_LOXAF Unreviewed; 498 AA.
AC G3TUV0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Glutamate decarboxylase 1 {ECO:0008006|Google:ProtNLM};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019358.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000019358.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019358.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000019358.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019358.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; G3TUV0; -.
DR STRING; 9785.ENSLAFP00000019358; -.
DR Ensembl; ENSLAFT00000025589.1; ENSLAFP00000019358.1; ENSLAFG00000027361.1.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000164469; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; G3TUV0; -.
DR OMA; NIADICE; -.
DR TreeFam; TF314688; -.
DR Proteomes; UP000007646; 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:SF6; GLUTAMATE DECARBOXYLASE 1-LIKE; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT MOD_RES 309
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 498 AA; 56570 MW; 24FBA3ADD7B90BFE CRC64;
FSLDLLPSKN GKELTNYFLR QVVDVLLHYI KKTFDVKSKI LDFHHPHQLL EGLDGFSLEL
PDHPESLEQL LVDCTDTLKY GVKTGHPRFF NQLSSGLDMI GLAGEWLTAT ANTNMFTYEI
APVFTVMETI VLKKMYEIIG WKETEADGLF SPAIGGSISN LYGILVARYK QYPEIKTKGM
TALPHIVLFV SEQGHYSVKK AAAILGIGTD NVIEVKCDER GRMIPAELEK NIAQAKRKGQ
TPFFVSTTAG TTVYGAFDPL CDIADICEKH KLWMHVDAAW GGGLLLSRSH SYKLRGIERA
NSVTWNPHKL MGAPLQCSAI LIQEKDLLEA CNQMRAGYLF QPDKLYNVEF DTGDKTIQCG
QHIEFFLFWV MYSSSGTYGF EAQINKHMEL AKYFYKVLKE RDNFKLVFDA EPEFTNVCFW
YLPPRLKHIP KGFERDQELQ KIAPKIKALM IEEGSAMISY QPCGDKVNFF RMVFSNPATT
QTDVDYLIEE IERLGKDL
//
