ID   DCHS_VIBC1              Reviewed;         386 AA.
AC   A7MVI6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=VIBHAR_02100;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000789; ABU71065.1; -; Genomic_DNA.
DR   RefSeq; WP_012127831.1; NC_022269.1.
DR   AlphaFoldDB; A7MVI6; -.
DR   SMR; A7MVI6; -.
DR   EnsemblBacteria; ABU71065; ABU71065; VIBHAR_02100.
DR   KEGG; vha:VIBHAR_02100; -.
DR   PATRIC; fig|338187.25.peg.592; -.
DR   OMA; EIDCEDF; -.
DR   OrthoDB; 1478871at2; -.
DR   Proteomes; UP000008152; Chromosome I.
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..386
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_1000061290"
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;  43772 MW;  88E8CC17069F9326 CRC64;
     MKLSDEDLSR LNEFWLYCSK NQYFNVGYPE SADFDYSELE KFMKFSINNC GDWREESNYK
     LNSFDFEKDV MRYFSQLFNI PHQESWGYIS NGGTEGNLFS CYLARELFPT AYLYYSEETH
     YSVDKIARLL NIPSRKIPAL SNGEIDYQQL VTQIERDQQG NPIIFANIGS TMRGAIDDIG
     RIQNDLATLG LDRKDYYIHA DAALSGMILP FVDQPPPYSF QDGIDSITVS GHKMIGSPIP
     CGIVLAKQHM VDQISVEVDY ISSRDQTISG SRNGHSALFM WTAIKSHSLS DWQSKVKLCL
     DMADYTVQRL QKAGIEAWRN KNSNTVVFPC PSEPIWRKHS LATSGDVAHI VTMPHLNSTA
     QLDALIDDVI FDLSPEYGLG HVIGQN