ID   DCHS_ACIBT              Reviewed;         383 AA.
AC   A3M7A4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Histidine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00609};
DE            Short=HDC {ECO:0000255|HAMAP-Rule:MF_00609};
DE            EC=4.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00609};
GN   Name=hdc {ECO:0000255|HAMAP-Rule:MF_00609}; OrderedLocusNames=A1S_2379;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-histidine = CO2 + histamine; Xref=Rhea:RHEA:20840,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:58432; EC=4.1.1.22; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00609};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00609};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00609}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00609}.
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DR   EMBL; CP000521; ABO12798.2; -; Genomic_DNA.
DR   RefSeq; WP_000603867.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M7A4; -.
DR   SMR; A3M7A4; -.
DR   DNASU; 4918294; -.
DR   KEGG; acb:A1S_2379; -.
DR   HOGENOM; CLU_028929_0_2_6; -.
DR   GO; GO:0004398; F:histidine decarboxylase activity; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00609; Pyridoxal_decarbox; 1.
DR   InterPro; IPR023523; Hist_deCOase_bac.
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   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..383
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_1000130347"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00609"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00609"
SQ   SEQUENCE   383 AA;  43756 MW;  B2780676014ED90B CRC64;
     MILSPADQER IETFWNYCLK HQYFNIGYPE SADFDYSALF RFFKFSINNC GDWKDYSNYA
     LNSFDFEKDV MAYFAEIFQI PFEESWGYVT NGGTEGNMFG CYLARELFPD STLYYSKDTH
     YSVGKIAKLL QMKSCVIESL DNGEIDYDDL IHKIKTNKES HPIIFANIGT TMTGAIDDIE
     MIQERLAQIG IMRRDYYIHA DAALSGMILP FVDHPQAFSF AHGIDSICVS GHKMIGSPIP
     CGIVVAKRQN VERISVDVDY ISTRDQTISG SRNGHTVLLM WAAIRSQTNL QRRHRIQHCL
     KMAQYAVDRF QAVGIPAWRN PNSITVVFPC PSEHIWKKHY LATSGNMAHL ITTAHHRDTR
     QIDSLIDDVI FDLQGASKRT VGF