ID   DCHS_VIBA7              Reviewed;         386 AA.
AC   Q56581; Q6W4S7;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
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}; Synonyms=angH;
OS   Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum).
OG   Plasmid pJM1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=882102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 68554 / 775;
RX   PubMed=7752899; DOI=10.1111/j.1365-2958.1995.tb02223.x;
RA   Tolmasky M.E., Actis L.A., Crosa J.H.;
RT   "A histidine decarboxylase gene encoded by the Vibrio anguillarum plasmid
RT   pJM1 is essential for virulence: histamine is a precursor in the
RT   biosynthesis of anguibactin.";
RL   Mol. Microbiol. 15:87-95(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 68554 / 775;
RX   PubMed=13129954; DOI=10.1128/jb.185.19.5822-5830.2003;
RA   Di Lorenzo M., Stork M., Tolmasky M.E., Actis L.A., Farrell D., Welch T.J.,
RA   Crosa L.M., Wertheimer A.M., Chen Q., Salinas P., Waldbeser L., Crosa J.H.;
RT   "Complete sequence of virulence plasmid pJM1 from the marine fish pathogen
RT   Vibrio anguillarum strain 775.";
RL   J. Bacteriol. 185:5822-5830(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 68554 / 775;
RX   PubMed=21576332; DOI=10.1128/iai.05138-11;
RA   Naka H., Dias G.M., Thompson C.C., Dubay C., Thompson F.L., Crosa J.H.;
RT   "Complete genome sequence of the marine fish pathogen Vibrio anguillarum
RT   harboring the pJM1 virulence plasmid and genomic comparison with other
RT   virulent strains of V. anguillarum and V. ordalii.";
RL   Infect. Immun. 79:2889-2900(2011).
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   -!- PATHWAY: Siderophore biosynthesis; anguibactin biosynthesis.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR12533.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY312585; AAR12533.1; ALT_INIT; Genomic_DNA.
DR   PIR; S60898; S49218.
DR   RefSeq; NP_943559.1; NC_005250.1.
DR   RefSeq; WP_020977926.1; NC_005250.1.
DR   AlphaFoldDB; Q56581; -.
DR   SMR; Q56581; -.
DR   eggNOG; COG0076; Bacteria.
DR   BRENDA; 4.1.1.22; 6625.
DR   UniPathway; UPA00016; -.
DR   Proteomes; UP000006800; Plasmid pJM1.
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; Plasmid; Pyridoxal phosphate.
FT   CHAIN           1..386
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146961"
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   386 AA;  44260 MW;  4FFBDBC84BE25831 CRC64;
     MKLSNEDLCK LNKFWLYCEE NQYFNVGYPE SAAFDYSILE KFMKFSINNC GDWREESNYK
     LNSFEFEKEV MRFFSQLFKI PYNDSWGYIS NGGTEGNMFS CYLAREIFPT AYIYYSEETH
     YSVDKIVRLL NIPARKIRSL PSGEIDYQNL VDQIQKDKQK NPIIFANIGT TMRGATDNIQ
     RIQQDLASIG LERNDYYIHA DAALSGMIMP FVEQPHPYSF EDGIDSISVS GHKMIGSPIP
     CGIVLAKRHM VDQISVEVDY ISSRDQTISG SRNGHSALFM WTAIKSHSFV DWQGKVNQCL
     NMAEYTVQRF QEVGINAWRN KNSNTVVFPC PSEPVWRKHS LANSGSVAHI ITMPHLDGPD
     KLDPLIEDVI YDLLPNYNIL NVSGQN