ID   A0A1N6W5S0_9EURY        Unreviewed;       525 AA.
AC   A0A1N6W5S0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:SIQ85306.1};
GN   ORFNames=SAMN05421858_0607 {ECO:0000313|EMBL:SIQ85306.1};
OS   Haladaptatus litoreus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haladaptataceae; Haladaptatus.
OX   NCBI_TaxID=553468 {ECO:0000313|EMBL:SIQ85306.1, ECO:0000313|Proteomes:UP000186914};
RN   [1] {ECO:0000313|Proteomes:UP000186914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7737 {ECO:0000313|Proteomes:UP000186914};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) 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.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; FTNO01000001; SIQ85306.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N6W5S0; -.
DR   Proteomes; UP000186914; Unassembled WGS sequence.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.20.1650.10; PLP-dependent transferases; 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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000186914}.
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         341
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   525 AA;  57037 MW;  62F1E19431E7AF9F CRC64;
     MNKPPEERPA SSAKSSAEST DSADGEDSSD SMPSEESLFL GSEKGAETYR TTMEQTTDAI
     LDAFVENADP YSGTSPESLR EEFAEMEMIP DSGEGLESAL ESAEPVLRNS VGVSDRQCLA
     HLHCPPMISG LAAEAMLSAT NQSMDSWDQS PAATHLETRM VEELCDLFGY GDSGDGVFTS
     GGTQSNFMGL LLARERFAKE RFGTNVQRSG LPHRAKAMRI LCSEEAHFTA EQAAAHLGLG
     ENAVVTVESN DDREMCPDAL DQTLAELDER ELLPFALVGT AGTTDFGSID PLDELAERAE
     EHDLWFHVDA AYGGALALSD RHRDLLSGID RADSLSVDFH KLFYQPISCG AFLLRDGSQY
     EHIARNASYL NPEGASVPNL VAKSAQTTRR FDALKPFLSF RALGRDGFGM LVDETIALAE
     EVAELLASGS SFELVAEPTI NAVVFRYRPT SDMADERLSW LNEAIRESLL REGDAVVART
     EVDGVTALKF TLLNPRTTLT DVADILDAIE RRGSSLRAVS PEVKR
//