DCHS_ACIBY
ID DCHS_ACIBY Reviewed; 383 AA.
AC B0VBU8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=ABAYE1098;
OS Acinetobacter baumannii (strain AYE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509173;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYE;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(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}.
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; CU459141; CAM86027.1; -; Genomic_DNA.
DR RefSeq; WP_000603880.1; NC_010410.1.
DR AlphaFoldDB; B0VBU8; -.
DR SMR; B0VBU8; -.
DR EnsemblBacteria; CAM86027; CAM86027; ABAYE1098.
DR KEGG; aby:ABAYE1098; -.
DR HOGENOM; CLU_028929_0_2_6; -.
DR OMA; EIDCEDF; -.
DR Proteomes; UP000002446; 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_1000130348"
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
