ID   DCHS_ACIB5              Reviewed;         383 AA.
AC   B7I459;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=AB57_2808;
OS   Acinetobacter baumannii (strain AB0057).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=480119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB0057;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
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; CP001182; ACJ42158.1; -; Genomic_DNA.
DR   RefSeq; WP_000603880.1; NC_011586.2.
DR   AlphaFoldDB; B7I459; -.
DR   SMR; B7I459; -.
DR   KEGG; abn:AB57_2808; -.
DR   HOGENOM; CLU_028929_0_2_6; -.
DR   OMA; EIDCEDF; -.
DR   Proteomes; UP000007094; Chromosome.
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_1000130345"
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;  43737 MW;  5EB08FFE2F17C0DF CRC64;
     MILSPADQER IETFWNYCLK HQYFNIGYPE SADFDYSALF RFFKFSINNC GDWKDYSNYA
     LNSFDFEKDV MAYFAEIFQI PFEESWGYVT NGGTEGNMFG CYLARELFSD STLYYSKDTH
     YSVGKIAKLL QMKSCVIESL DNGEIDYDDL IHKIKTNKES HPIIFANIGT TMTGAIDDIE
     MIQERLAQIG IMRRDYYIHA DAALSGMILP FVDHPQAFSF AHGIDSICVS GHKMIGSPIP
     CGIVVAKRQN VERISVDVDY ISTRDQTISG SRNGHTVLLM WAAIRSQTNL QRRQRIQHCL
     KMAQYAVDRF QAVGIPAWRN PNSITVVFPC PSEHIWKKHY LATSGNMAHL ITTAHHRDTR
     QIDSLIDDVI FDLQGASKRT VGF