ID   DDC_HAEIN               Reviewed;         511 AA.
AC   P71362;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 120.
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; OrderedLocusNames=HI_0946.1;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   White O., Clayton R.A., Kerlavage A.R., Fleischmann R.D.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9514614; DOI=10.1248/bpb.21.170;
RA   Ikai H., Yamamoto S.;
RT   "Two genes involved in the 1,3-diaminopropane production pathway in
RT   Haemophilus influenzae.";
RL   Biol. Pharm. Bull. 21:170-173(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L42023; AAC22607.1; -; Genomic_DNA.
DR   PIR; JC5880; JC5880.
DR   RefSeq; NP_439107.1; NC_000907.1.
DR   RefSeq; WP_005693296.1; NC_000907.1.
DR   AlphaFoldDB; P71362; -.
DR   SMR; P71362; -.
DR   STRING; 71421.HI_0946.1; -.
DR   EnsemblBacteria; AAC22607; AAC22607; HI_0946.1.
DR   KEGG; hin:HI_0946.1; -.
DR   PATRIC; fig|71421.8.peg.988; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   OMA; RHATYHA; -.
DR   PhylomeDB; P71362; -.
DR   BioCyc; HINF71421:G1GJ1-987-MON; -.
DR   UniPathway; UPA00010; UER00732.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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   Gene3D; 3.90.1150.10; -; 1.
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   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; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..511
FT                   /note="L-2,4-diaminobutyrate decarboxylase"
FT                   /id="PRO_0000147004"
FT   MOD_RES         320
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  56638 MW;  42832FA4AC4F297A CRC64;
     MSNLKQHKQA LFCNDNEAIN DYETAMHNAV QAVSAWLKNE KMYTGGSIKQ MRALISGFNP
     TKEGMGVQKS LDHLVEIFLN PSLKVHHPHS LAHLHCPTMV TSQIAEVLIN ATNQSMDSWD
     QSPAGSIMEE HLINWLRQKA GYGEGTSGVF TSGGTQSNLM GVLLARDWAI ANHWKNEDGS
     EWSVQRDGIP AEAMQKVKVI CSENAHFSVQ KNMAMMGMGF QSVVTVPSNA NAQMDLIALK
     QTLAQLKADG KITACIVATA GTTDAGAIDD LKAIRKLADE YQAWLHVDAA WGGALLLSKD
     YRYFLDGIEL TDSITLDFHK HFFQTISCGA FLLKDPENYR FIDYKADYLN SEYDEAHGVP
     NLVAKSLQTT RRFDALKLWF TLEALGEDLY ASMIDHGVKL TKEVEQYIND TPDLEMLVPS
     QFASVLFRVV PKDYPAEFID ALNQNVADEL FARGEANIGV TKVGDKQSLK MTTLSPIATL
     ENVKALLTQV LTEANRIKDD IKNGTYTPPI D