ID   DCHS_HUMAN              Reviewed;         662 AA.
AC   P19113; A1L4G0;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   01-MAY-2013, entry version 117.
DE   RecName: Full=Histidine decarboxylase;
DE            Short=HDC;
DE            EC=4.1.1.22;
GN   Name=HDC;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2216786; DOI=10.1093/nar/18.19.5891;
RA   Yamauchi K., Ruriko S., Ohkawara Y., Tanno Y., Maeyama K.,
RA   Watanabe T., Satoh K., Yoshizawa M., Shibahara S., Takishima T.;
RT   "Nucleotide sequence of the cDNA encoding L-histidine decarboxylase
RT   derived from human basophilic leukemia cell line, KU-812-F.";
RL   Nucleic Acids Res. 18:5891-5891(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1768863;
RA   Zahnow C.A., Yi H.F., McBride O.W., Joseph D.R.;
RT   "Cloning of the cDNA encoding human histidine decarboxylase from an
RT   erythroleukemia cell line and mapping of the gene locus to chromosome
RT   15.";
RL   DNA Seq. 1:395-400(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Leukemia;
RX   PubMed=1425659; DOI=10.1111/j.1432-1033.1992.tb17317.x;
RA   Mamune-Sato R., Yamauchi K., Tanno Y., Ohkawara Y., Ohtsu H.,
RA   Katayose D., Maeyama K., Watanabe T., Shibahara S., Takishima T.;
RT   "Functional analysis of alternatively spliced transcripts of the human
RT   histidine decarboxylase gene and its expression in human tissues and
RT   basophilic leukemia cells.";
RL   Eur. J. Biochem. 209:533-539(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8288622;
RA   Yatsunami K., Ohtsu H., Tsuchikawa M., Higuchi T., Ishibashi K.,
RA   Shida A., Shima Y., Nakagawa S., Yamauchi K., Yamamoto M., Hayashi N.,
RA   Watanabe T., Ichikawa A.;
RT   "Structure of the L-histidine decarboxylase gene.";
RL   J. Biol. Chem. 269:1554-1559(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-31.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-477 IN COMPLEX WITH
RP   HISTIDINE METHYL ESTER AND PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY,
RP   FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   MUTAGENESIS OF LYS-305; TYR-334 AND SER-354.
RX   PubMed=22767596; DOI=10.1074/jbc.M112.381897;
RA   Komori H., Nitta Y., Ueno H., Higuchi Y.;
RT   "Structural study reveals that Ser-354 determines substrate
RT   specificity on human histidine decarboxylase.";
RL   J. Biol. Chem. 287:29175-29183(2012).
RN   [7]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-49 AND LYS-285.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Catalyzes the biosynthesis of histamine from histidine.
CC   -!- CATALYTIC ACTIVITY: L-histidine = histamine + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.1 mM for histidine;
CC         Vmax=1880 nmol/min/mg enzyme;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; histamine biosynthesis;
CC       histamine from L-histidine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
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DR   EMBL; X54297; CAA38196.1; -; mRNA.
DR   EMBL; M60445; AAC41698.1; -; mRNA.
DR   EMBL; D16583; BAA04015.1; -; Genomic_DNA.
DR   EMBL; BC130527; AAI30528.1; -; mRNA.
DR   IPI; IPI00290368; -.
DR   PIR; A49882; A49882.
DR   RefSeq; NP_002103.2; NM_002112.3.
DR   UniGene; Hs.1481; -.
DR   PDB; 4E1O; X-ray; 1.80 A; A/B/C/D/E/F=2-477.
DR   PDBsum; 4E1O; -.
DR   ProteinModelPortal; P19113; -.
DR   STRING; 9606.ENSP00000267845; -.
DR   PhosphoSite; P19113; -.
DR   DMDM; 1352220; -.
DR   PaxDb; P19113; -.
DR   PRIDE; P19113; -.
DR   DNASU; 3067; -.
DR   Ensembl; ENST00000267845; ENSP00000267845; ENSG00000140287.
DR   GeneID; 3067; -.
DR   KEGG; hsa:3067; -.
DR   UCSC; uc001zxy.3; human.
DR   CTD; 3067; -.
DR   GeneCards; GC15M050534; -.
DR   HGNC; HGNC:4855; HDC.
DR   HPA; HPA038891; -.
DR   MIM; 142704; gene.
DR   neXtProt; NX_P19113; -.
DR   PharmGKB; PA29233; -.
DR   eggNOG; COG0076; -.
DR   HOGENOM; HOG000121941; -.
DR   HOVERGEN; HBG000944; -.
DR   InParanoid; P19113; -.
DR   KO; K01590; -.
DR   OMA; DVQPGYM; -.
DR   OrthoDB; EOG4DV5M4; -.
DR   BRENDA; 4.1.1.22; 2681.
DR   Reactome; REACT_111217; Metabolism.
DR   UniPathway; UPA00822; UER00786.
DR   DrugBank; DB00117; L-Histidine.
DR   DrugBank; DB00114; Pyridoxal Phosphate.
DR   GenomeRNAi; 3067; -.
DR   NextBio; 12133; -.
DR   ArrayExpress; P19113; -.
DR   Bgee; P19113; -.
DR   CleanEx; HS_HDC; -.
DR   Genevestigator; P19113; -.
DR   GermOnline; ENSG00000140287; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0004398; F:histidine decarboxylase activity; IDA: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; IDA:UniProtKB.
DR   GO; GO:0006548; P:histidine catabolic process; IDA: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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Catecholamine biosynthesis; Complete proteome;
KW   Decarboxylase; Lyase; Polymorphism; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    662       Histidine decarboxylase.
FT                                /FTId=PRO_0000146950.
FT   BINDING      81     81       Substrate; via amide nitrogen.
FT   BINDING     194    194       Substrate.
FT   MOD_RES     305    305       N6-(pyridoxal phosphate)lysine.
FT   VARIANT      31     31       T -> M (in dbSNP:rs17740607).
FT                                /FTId=VAR_048873.
FT   VARIANT      49     49       E -> V (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036470.
FT   VARIANT     285    285       E -> K (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036471.
FT   VARIANT     553    553       F -> L (in dbSNP:rs16963486).
FT                                /FTId=VAR_048874.
FT   VARIANT     644    644       E -> D (in dbSNP:rs2073440).
FT                                /FTId=VAR_033846.
FT   MUTAGEN     305    305       K->G: Loss of enzyme activity.
FT   MUTAGEN     334    334       Y->F: Loss of enzyme activity.
FT   MUTAGEN     354    354       S->G: Strongly decreases affinity for
FT                                histidine. Strongly increases affinity
FT                                for L-DOPA and confers enzyme activity
FT                                toward L-DOPA.
FT   CONFLICT    118    118       N -> M (in Ref. 3; no nucleotide entry).
FT   CONFLICT    148    148       S -> Q (in Ref. 1; CAA38196 and 3; no
FT                                nucleotide entry).
FT   CONFLICT    500    500       W -> M (in Ref. 3; no nucleotide entry).
FT   HELIX         4     23
FT   HELIX        25     27
FT   TURN         36     39
FT   HELIX        40     42
FT   HELIX        54     64
FT   HELIX        66     68
FT   STRAND       79     81
FT   HELIX        87     99
FT   TURN        106    108
FT   HELIX       110    127
FT   HELIX       131    133
FT   STRAND      143    148
FT   HELIX       150    172
FT   HELIX       178    182
FT   STRAND      185    190
FT   HELIX       195    204
FT   STRAND      207    211
FT   HELIX       221    233
FT   STRAND      237    246
FT   TURN        248    250
FT   HELIX       256    266
FT   STRAND      269    273
FT   HELIX       277    282
FT   HELIX       284    290
FT   HELIX       293    295
FT   STRAND      297    301
FT   HELIX       303    306
FT   STRAND      314    320
FT   HELIX       321    325
FT   TURN        326    328
FT   HELIX       333    335
FT   TURN        338    342
FT   HELIX       346    349
FT   STRAND      350    353
FT   HELIX       359    393
FT   STRAND      406    415
FT   HELIX       417    430
FT   STRAND      432    434
FT   STRAND      436    440
FT   STRAND      443    449
FT   HELIX       457    475
SQ   SEQUENCE   662 AA;  74141 MW;  D7611CFAAD60F469 CRC64;
     MMEPEEYRER GREMVDYICQ YLSTVRERRV TPDVQPGYLR AQLPESAPED PDSWDSIFGD
     IERIIMPGVV HWQSPHMHAY YPALTSWPSL LGDMLADAIN CLGFTWASSP ACTELEMNVM
     DWLAKMLGLP EHFLHHHPSS QGGGVLQSTV SESTLIALLA ARKNKILEMK TSEPDADESC
     LNARLVAYAS DQAHSSVEKA GLISLVKMKF LPVDDNFSLR GEALQKAIEE DKQRGLVPVF
     VCATLGTTGV CAFDCLSELG PICAREGLWL HIDAAYAGTA FLCPEFRGFL KGIEYADSFT
     FNPSKWMMVH FDCTGFWVKD KYKLQQTFSV NPIYLRHANS GVATDFMHWQ IPLSRRFRSV
     KLWFVIRSFG VKNLQAHVRH GTEMAKYFES LVRNDPSFEI PAKRHLGLVV FRLKGPNCLT
     ENVLKEIAKA GRLFLIPATI QDKLIIRFTV TSQFTTRDDI LRDWNLIRDA ATLILSQHCT
     SQPSPRVGNL ISQIRGARAW ACGTSLQSVS GAGDDPVQAR KIIKQPQRVG AGPMKRENGL
     HLETLLDPVD DCFSEEAPDA TKHKLSSFLF SYLSVQTKKK TVRSLSCNSV PVSAQKPLPT
     EASVKNGGSS RVRIFSRFPE DMMMLKKSAF KKLIKFYSVP SFPECSSQCG LQLPCCPLQA
     MV
//