ID   DDC_ACIBA               Reviewed;         510 AA.
AC   Q43908;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=L-2,4-diaminobutyrate decarboxylase;
DE            Short=DABA decarboxylase;
DE            Short=DABA-DC;
DE            EC=4.1.1.86;
GN   Name=ddc;
OS   Acinetobacter baumannii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 19606 / DSM 30007 / CCUG 19096 / CIP 70.34 / JCM 6841 / LMG
RC   1041 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX   PubMed=8772175; DOI=10.1007/s002030050366;
RA   Ikai H., Yamamoto S.;
RT   "Sequence analysis of the gene encoding a novel L-2,4-diaminobutyrate
RT   decarboxylase of Acinetobacter baumannii: similarity to the group II amino
RT   acid decarboxylases.";
RL   Arch. Microbiol. 166:128-131(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-2,4-diaminobutanoate = CO2 + propane-1,3-diamine;
CC         Xref=Rhea:RHEA:15689, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57484, ChEBI:CHEBI:58761; EC=4.1.1.86;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; 1,3-diaminopropane
CC       biosynthesis; 1,3-diaminopropane from L-aspartate 4-semialdehyde: step
CC       2/2.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; D55724; BAA09538.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q43908; -.
DR   SMR; Q43908; -.
DR   STRING; 470.IX87_08925; -.
DR   KEGG; ag:BAA09538; -.
DR   eggNOG; COG0076; Bacteria.
DR   BRENDA; 4.1.1.86; 98.
DR   UniPathway; UPA00010; UER00732.
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   Gene3D; 3.40.640.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..510
FT                   /note="L-2,4-diaminobutyrate decarboxylase"
FT                   /id="PRO_0000147003"
FT   MOD_RES         319
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   510 AA;  56244 MW;  900DF52FD1941B70 CRC64;
     MVDFAEHRKA LLCNDAQSIA DYESAMGEAV KAVSAWLQNE KMYTGGSIKE LRSAISFQPS
     KEGMGVQQSL QRMIELFLNK SLKVHHPHSL AHLHCPTMVM SQIAEVLINA TNQSMDSWDQ
     SPAGSLMEVQ LIDWLRQKVG YGSGQAGVFT SGGTQSNLMG VLLARDWCIA KNWKDENGNP
     WSVQRDGIPA EAMKNVKVIC SENAHFSVQK NMAMMGMGFQ SVVTVPVNEN AQMDVDALEK
     TMAHLQAEGK VVACVVATAG TTDAGAIHPL KKIREITNKY GSWMHIDAAW GGALILSNTY
     RAMLDGIELS DSITLDFHKH YFQSISCGAF LLKDEANYRF MHYEAEYLNS AYDEEHGVPN
     LVSKSLQTTR RFDALKLWMT IESLGEELYG SMIDHGVKLT REVADYIKAT EGLELLVEPQ
     FASVLFRVVP EGYPVEFIDS LNQNVADELF ARGEANIGVT KVGNVQSLKM TTLSPVVTVD
     NVKNLLAQVL AEAERIKDAI ASGNYVPPID