DCHS_PSEE4
ID DCHS_PSEE4 Reviewed; 403 AA.
AC Q1IAK7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=PSEEN2506;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK15310.1; -; Genomic_DNA.
DR RefSeq; WP_011533709.1; NC_008027.1.
DR AlphaFoldDB; Q1IAK7; -.
DR SMR; Q1IAK7; -.
DR STRING; 384676.PSEEN2506; -.
DR EnsemblBacteria; CAK15310; CAK15310; PSEEN2506.
DR KEGG; pen:PSEEN2506; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_028929_0_2_6; -.
DR OMA; EIDCEDF; -.
DR OrthoDB; 1478871at2; -.
DR Proteomes; UP000000658; 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..403
FT /note="Histidine decarboxylase"
FT /id="PRO_1000061289"
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 403 AA; 45223 MW; ED52E465C2C35489 CRC64;
MTLSSADQAR LDQFWEHCLK NQYFNIGYPE NADFNYAQLH RFLRFSINNC GDWAEPGNYL
LNSFDFEKDV MAYFAELFSI PLEESWGYVT NGGTEGNMFG CYLARELFPT GTLYYSKDTH
YSVAKIVKLL RIDCRAVESL PNGEIDYDDL MAKIAADQEQ HPIIFVNVGT TMRGAIDNIA
TIQQRLEEVG IPREDYYLHA DAALSGMILP FVDNPQPFNF ADGVDSICVS GHKMIGSPIP
CGIVVAKREN VERISVDVDY IRANDKTISG SRNGHTPMMM WAALRSHSPA QWRRRVRHSL
NSAQYAVDRL QAAGIDAWRH DNSITVVFPC PSSRIARKYC LATSGDTAHL ITTPHHQDKS
MIDALIDEVI AEHQPNEWRA GLGLAGLDGV PPERVAASHF DVI
