DCHS_RHILO
ID DCHS_RHILO Reviewed; 369 AA.
AC Q98A07;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=mlr6209;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB52537.1; -; Genomic_DNA.
DR RefSeq; WP_010913856.1; NC_002678.2.
DR AlphaFoldDB; Q98A07; -.
DR SMR; Q98A07; -.
DR STRING; 266835.14025938; -.
DR EnsemblBacteria; BAB52537; BAB52537; BAB52537.
DR KEGG; mlo:mlr6209; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_028929_0_2_5; -.
DR OMA; EIDCEDF; -.
DR OrthoDB; 1478871at2; -.
DR BRENDA; 4.1.1.22; 3243.
DR Proteomes; UP000000552; 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 Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..369
FT /note="Histidine decarboxylase"
FT /id="PRO_0000146960"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00609"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00609"
SQ SEQUENCE 369 AA; 41034 MW; D95FEC59FA3BE8C8 CRC64;
MLEPQDQKKL DELFSSMQEA NGCFLGYPFA KDFDYEPLWR FMSLTGNNLG DPFEPGTYRV
NSHAFECDVV DFFARLFRAC SCEVWGYVTN GGTEGNIYGL YLARELYPNA VAYFSQDTHY
SVSKGVRLLR LEHSVVRSQS NGEINYDDLA QKATRYRTRP AVVVANIGTT MKEGKDDTLK
IRAVLHDVGI SAIYVHSDAA LCGPYAPLLN PKPAFDFADG ADSITLSGHK FLGAPMPCGV
VLSHKLHVQR VMRNIDYIGS SDTTLSGSRN AFTPIILWYA IRSLGIEGIK QTFQQCERLA
AYTADELNVR GVSAWRNPNA LTVVLPPVED SIKTKWQIAT QDVSHLVVTP GTTKQQADAL
IETISNRNR
