ID L0M2J5_ENTBF Unreviewed; 487 AA.
AC L0M2J5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=PLP-dependent enzyme, glutamate decarboxylase {ECO:0000313|EMBL:AGB78154.1};
GN OrderedLocusNames=D782_2172 {ECO:0000313|EMBL:AGB78154.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB78154.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB78154.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB78154.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
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.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP003938; AGB78154.1; -; Genomic_DNA.
DR AlphaFoldDB; L0M2J5; -.
DR STRING; 693444.D782_2172; -.
DR KEGG; ebf:D782_2172; -.
DR PATRIC; fig|693444.3.peg.2094; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_6; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000011002; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino 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; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
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:UP000011002}.
FT MOD_RES 307
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 487 AA; 53130 MW; 77121ACC104297D3 CRC64;
MSENNPILSG SAQSIAAYQD AIEQSSKAVV EWLKQPEMYQ GKTVDQLRER IHLNFTAEGL
GNQATIARAV EYFLKDSLSV HHAQCVAHLH CPSLVISQAA EVLINATNQS MDSWDQSPSA
TIIEMKLIEW LREQVGYPAG DAGVFTSGGT QSNLMGLMLA RDAFFARQGH SIQQNGLTGD
LSKIKVFCSE SAHFSVQKNM ALMGLGYRSV TQVKTDAFSR MDMADLKAKL AQAKANGEQV
MAIVATAGTT DAGAIDPLVE ITELAAAENI WVHVDAAWGG ALLLSEKYRH YLNGLESADS
VTLDFHKQFF QTISCGAFLL KDARHYELMR YQAAYLNSDF DEEHGVPNLV SKSLQTTRRF
DALKLWMGLE ALGKKQYAEI IDNGVTLAQQ VAEFVSAQPH LELVMQPQLA SVLFRFRPES
GDAAFVALLN QRIGDVLLAS GAANVGVTEA DGVTCLKLTL LNPTVCLEDV KVLLASVKET
AETLLTR
//
