ID   B0VVA4_ACIBS            Unreviewed;       510 AA.
AC   B0VVA4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:CAQ15851.1};
DE            EC=4.1.1.86 {ECO:0000313|EMBL:CAQ15851.1};
GN   Name=ddc {ECO:0000313|EMBL:CAQ15851.1};
GN   OrderedLocusNames=ABSDF1093.4 {ECO:0000313|EMBL:CAQ15851.1};
OS   Acinetobacter baumannii (strain SDF).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509170 {ECO:0000313|EMBL:CAQ15851.1, ECO:0000313|Proteomes:UP000001741};
RN   [1] {ECO:0000313|EMBL:CAQ15851.1, ECO:0000313|Proteomes:UP000001741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDF {ECO:0000313|EMBL:CAQ15851.1,
RC   ECO:0000313|Proteomes:UP000001741};
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAQ15851.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VVA4; -.
DR   KEGG; abm:ABSDF1093.4; -.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000001741; Chromosome.
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;  56180 MW;  9393E74F27CF4FB7 CRC64;
     MVDFAEHRKA LLCNDAQSIA DYESAMGEAV KAVSAWLQNE KMYTGGSIKE LRSAISFQPS
     KEGMGVQQSL QRMIELFLNK SLKVHHPHSL AHLHCPTMVM SQIAEVLINA TNQSMDSWDQ
     SPAGSLMEVQ LIDWLRQKVG YGSGQAGVFT SGGTQSNLMG VLLARDWCIA KNWKDENGNP
     WSGQRDGIPA EAMKNVKVIC SENAHFSVQK NMAMMGMGFQ SVVTVPVNEN AQMDVDALEK
     TMAHLQAEGK VVACVVATAG TTDAGAIDPL KKIREITNKY GSWMHIDAAW GGALILSNDY
     RAMLDGIELS DSITLDFHKH YFQSISCGAF LLKDEANYRF MHYEAEYLNS AYDEEHGVPN
     LVSKSLQTTR RFDALKLWMT IESLGEELYG SMIDHGVKLT REVADYIKAT DGLELLVEPQ
     FASVLFRVVP EGYPVEFIDS LNQNVADELF ARGEANIGVT KVGNVQSLKM TTLSPVVTVD
     NVKNLLAQVL AEAERIKDAI ASGNYVPPID
//