ID   DCHS_BOVIN              Reviewed;         658 AA.
AC   Q5EA83;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
GN   Name=HDC;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Catalyzes the biosynthesis of histamine from histidine.
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; histamine biosynthesis;
CC       histamine from L-histidine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; BT020686; AAX08703.1; -; mRNA.
DR   RefSeq; NP_001019722.1; NM_001024551.1.
DR   AlphaFoldDB; Q5EA83; -.
DR   SMR; Q5EA83; -.
DR   STRING; 9913.ENSBTAP00000013083; -.
DR   PaxDb; Q5EA83; -.
DR   PRIDE; Q5EA83; -.
DR   Ensembl; ENSBTAT00000013083; ENSBTAP00000013083; ENSBTAG00000009911.
DR   GeneID; 515950; -.
DR   KEGG; bta:515950; -.
DR   CTD; 3067; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009911; -.
DR   VGNC; VGNC:29784; HDC.
DR   eggNOG; KOG0628; Eukaryota.
DR   GeneTree; ENSGT00940000157938; -.
DR   HOGENOM; CLU_011856_3_0_1; -.
DR   InParanoid; Q5EA83; -.
DR   OMA; YKTPSRK; -.
DR   OrthoDB; 856958at2759; -.
DR   TreeFam; TF313863; -.
DR   Reactome; R-BTA-70921; Histidine catabolism.
DR   UniPathway; UPA00822; UER00786.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000009911; Expressed in aorta and 54 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0004398; F:histidine decarboxylase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0001694; P:histamine biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006548; P:histidine catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Catecholamine biosynthesis; Decarboxylase; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..658
FT                   /note="Histidine decarboxylase"
FT                   /id="PRO_0000146949"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         305
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   658 AA;  73912 MW;  F458FD059B4CB0C3 CRC64;
     MMEPEEYRER GKEMVDYICQ YLTTVRERRV TPDVRPGYLR AQLPESAPME PDSWDSIFGD
     IERIIMPGVV HWQSPHMHAY YPALTSWPSL LGDMLADAIN CLGFTWASSP ACTELEMNVM
     DWLAKMLGLP EHFLHHHPGS QGGGVLQSTV SESTLIALLA ARKNKILEMK ASEPEADESF
     LNARLVAYAS DQAHSSVEKA GLISLVKMKF LPVDENFSLR GEALQKAIKE DRERGLVPIF
     VCATLGTTGV CAFDCLSELG PICAREGLWL HIDAAYAGTA FLCPEFRGFL KGIEYADSFT
     FNPSKWMMVH FDCTGFWVKD KYKLQQTFSV DPVYLRHADS GVATDFMHWQ IPLSRRFRSI
     KLWFVIRSFG VKNLQAHVRH GTEMAKYFES LVRNDPFFEI PAKRHLGLVV FRLKGPNCLT
     ESVLKEIAKA GRLFLIPATI QDKLIIRFTV TSQFTTRDDI LRDWNLIQDA ATLILSQHCT
     SQPSPQGANL ILQTRGPRAL AKEMSFPSVN GAGDDPAHSR KIVMQPPRVG ASPVSRHLET
     LLDPLDDCFS EEAPDVTEHK LSSFLFSYLS VQNKRKAVRS LSCNSVPVSA QKQLTTEGSV
     KNGSSSRVRI FSRFPEEVMM LKKSAFKKLI KFYSVPNFPE CSSQCGLQLP CCPLQAMV