ID A0A0P1IG60_9RHOB Unreviewed; 473 AA.
AC A0A0P1IG60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:CUK11178.1};
DE EC=4.1.1.15 {ECO:0000313|EMBL:CUK11178.1};
GN Name=gadB {ECO:0000313|EMBL:CUK11178.1};
GN ORFNames=PH7735_03544 {ECO:0000313|EMBL:CUK11178.1};
OS Shimia thalassica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUK11178.1, ECO:0000313|Proteomes:UP000051870};
RN [1] {ECO:0000313|Proteomes:UP000051870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7735 {ECO:0000313|Proteomes:UP000051870};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR EMBL; CYTW01000005; CUK11178.1; -; Genomic_DNA.
DR RefSeq; WP_058312713.1; NZ_CYTW01000005.1.
DR AlphaFoldDB; A0A0P1IG60; -.
DR STRING; 1715693.PH7735_03544; -.
DR GeneID; 83882521; -.
DR Proteomes; UP000051870; Unassembled WGS sequence.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 6.10.140.2150; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 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:UP000051870}.
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 473 AA; 51656 MW; 2582CF5C0BE1D078 CRC64;
MDHMRLPEQG RPEDEILDDL KQFSEDDPDY KHGRVWSLVY HLDQAHEDFT AAAYQQYSSA
NGLNPAAFKS LKRMETEIIS TVAGLLNGGP DTCGVVTAGG TESCLMAVKT YRDMARAKRR
VKTPNMIIPA TAHVAWFKAA GYFGVKARLL PMTKDFGTDI KKLKSMINRN TVMILGSAPE
YPHGTIDPIA EMGQIASEKG VPMHVDACVG AFILPFMEMN GIPLPEWDFR VPGVTSISAD
LHKYGYTAKG ASTILYRDLD TLKHQMFVYQ DWPGGVFASP ALLGTRPGGA YAAAWAVLQK
MGIDGYRELA AQTTAAVETL KAGINDTDGL RLLGNPQGPL LSYGSSDPKL NIFAVADQLE
AQGWNVNRVQ NPDGIHAMVT AKHNEVAETY VNDLKTAVAS VRSNPDLANS GSAATYGMMA
HVPLRGMVKT RVLDIFAEMY RAGGGHLDLD DSAKPSLLER GMARYVRWKS RRS
//