ID   A0A2U3N2Z5_9GAMM        Unreviewed;       510 AA.
AC   A0A2U3N2Z5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:SPL71919.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:SPL71919.1};
GN   Name=ddc {ECO:0000313|EMBL:SPL71919.1};
GN   ORFNames=KPC_3097 {ECO:0000313|EMBL:SPL71919.1};
OS   Acinetobacter stercoris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=2126983 {ECO:0000313|EMBL:SPL71919.1, ECO:0000313|Proteomes:UP000245974};
RN   [1] {ECO:0000313|Proteomes:UP000245974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPC-SM-21 {ECO:0000313|Proteomes:UP000245974};
RA   Blom J.;
RL   Submitted (MAR-2018) 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|RuleBase:RU000382}.
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DR   EMBL; OOGT01000190; SPL71919.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U3N2Z5; -.
DR   InParanoid; A0A2U3N2Z5; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000245974; Unassembled WGS sequence.
DR   GO; GO:0033983; F:diaminobutyrate 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   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   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   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}.
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   510 AA;  55907 MW;  2F99F28A1C66065E CRC64;
     MVDFAEHRKA LLCNDAQSIA DYESAMAEAV KAVSAWLQND KMYTGGSIKE LRSAISFNPS
     KQGIGLDKSV NRMTDLFLNK SLKVHHPHSL AHLHCPTMVA SQIAEVFINA TNQSMDSWDQ
     SPAGSLMEVQ LIDWLRQKVG YGKGEAGVFT SGGTQSNLMG VLLARDACIA KNYKDENGQE
     WSVQRDGIPA DALKKVKVIC SENAHFSVQK NMAMMGMGFQ SVVTVPVNDN AQMDVDALEK
     TMAHLQAEGK IVACVVATAG TTDAGAIDPL KQIREITSKY GAWMHIDAAW GGALILSNDH
     RSMLDGIELS DSVTLDFHKH YFQTISCGAF LLKDPANYRF MHYEAEYLNS AYDEEHGVPN
     LVSKSLQTTR RFDALKLWMT VEALGEELYG SMIDHGVELT REVTDYIKAT PGLELLVEPQ
     FASVLFRVVP EGYPAELLDT LNQNVADELF ARGEANIGVT KVGNVQSLKM TTLSPVATLE
     NVKNLLDLVL AEAERIKAPI QAGTYTPAID
//