DCHS_DROME
ID DCHS_DROME Reviewed; 847 AA.
AC Q05733; Q9V5I3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histidine decarboxylase;
DE Short=HDC;
DE EC=4.1.1.22 {ECO:0000305|PubMed:8096176};
GN Name=Hdc; ORFNames=CG3454;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=8096176; DOI=10.1002/j.1460-2075.1993.tb05732.x;
RA Burg M.G., Sarthy P.V., Koliantz G., Pak W.L.;
RT "Genetic and molecular identification of a Drosophila histidine
RT decarboxylase gene required in photoreceptor transmitter synthesis.";
RL EMBO J. 12:911-919(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC -!- FUNCTION: Required in photoreceptor transmitter synthesis
CC (PubMed:8096176). Catlayzes the conversion of L-histidine to histamine
CC (Probable). {ECO:0000269|PubMed:8096176, ECO:0000305|PubMed:8096176}.
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 Evidence={ECO:0000305|PubMed:8096176};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20841;
CC Evidence={ECO:0000305|PubMed:8096176};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Localized primarily to the photoreceptors, in the
CC eye. {ECO:0000269|PubMed:8096176}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X70644; CAA49989.1; -; mRNA.
DR EMBL; AE013599; AAF58823.1; -; Genomic_DNA.
DR PIR; S36337; S36337.
DR RefSeq; NP_001260855.1; NM_001273926.1.
DR RefSeq; NP_001286274.1; NM_001299345.1.
DR RefSeq; NP_523679.2; NM_078955.3.
DR AlphaFoldDB; Q05733; -.
DR SMR; Q05733; -.
DR BioGRID; 61897; 2.
DR IntAct; Q05733; 2.
DR STRING; 7227.FBpp0304256; -.
DR PaxDb; Q05733; -.
DR EnsemblMetazoa; FBtr0088333; FBpp0087422; FBgn0005619.
DR EnsemblMetazoa; FBtr0331923; FBpp0304256; FBgn0005619.
DR EnsemblMetazoa; FBtr0345474; FBpp0311591; FBgn0005619.
DR GeneID; 36076; -.
DR KEGG; dme:Dmel_CG3454; -.
DR CTD; 3067; -.
DR FlyBase; FBgn0005619; Hdc.
DR VEuPathDB; VectorBase:FBgn0005619; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000157938; -.
DR HOGENOM; CLU_011856_2_0_1; -.
DR InParanoid; Q05733; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; Q05733; -.
DR BRENDA; 4.1.1.22; 1994.
DR Reactome; R-DME-70921; Histidine catabolism.
DR ChiTaRS; Hdc; fly.
DR GenomeRNAi; 36076; -.
DR PRO; PR:Q05733; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0005619; Expressed in head capsule and 5 other tissues.
DR ExpressionAtlas; Q05733; baseline and differential.
DR Genevisible; Q05733; DM.
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; IMP:FlyBase.
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; IBA:GO_Central.
DR GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
DR GO; GO:0043052; P:thermotaxis; IMP:FlyBase.
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 1: Evidence at protein level;
KW Catecholamine biosynthesis; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..847
FT /note="Histidine decarboxylase"
FT /id="PRO_0000146953"
FT REGION 575..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 304
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 214
FT /note="D -> E (in Ref. 1; CAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="I -> T (in Ref. 1; CAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="P -> A (in Ref. 1; CAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="P -> H (in Ref. 1; CAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="Q -> H (in Ref. 1; CAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="I -> M (in Ref. 1; CAA49989)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="Q -> R (in Ref. 1; CAA49989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 94036 MW; C04F32F01C176951 CRC64;
MDFKEYRQRG KEMVDYIADY LENIRERRVF PDVSPGYMRQ LLPESAPIEG EPWPKIFSDV
ERIVMPGITH WQSPHMHAYF PALNSMPSLL GDMLADAINC LGFTWASSPA CTELEIIVMN
WLGKMIGLPD AFLHLSSQSQ GGGVLQTTAS EATLVCLLAG RTRAIQRFHE RHPGYQDAEI
NARLVAYCSD QAHSSVEKAA LIGLVRMRYI EADDDLAMRG KLLREAIEDD IKQGLVPFWV
CATLGTTGSC SFDNLEEIGI VCAEHHLWLH VDAAYAGSAF ICPEFRTWLR GIERADSIAF
NPSKWLMVHF DATALWVRDS TAVHRTFNVE PLYLQHENSG VAVDFMHWQI PLSRRFRALK
VWFVLRSYGI KGLQRHIREG VRLAQKFEAL VLADHRFELP AKRHLGLVVF RIRGDNEITE
KLLKRLNHRG NLHCIPSSLK GQYVIRFTIT STHTTLDDIV KDWMEIRQVA STVLEEMNIT
ISNRVYLKET KEKNEAFGSS LLLSNSPLSP KVVNGSFAAI FDADEFLAKT YAGVRIAHQE
SPSMRRRVRG ILMSGKQFSL DSHMDVVVQT TLDAGNGATR TSTTNSYGHT TSAAQANSER
QASIQEDNEE SPEETELLSL CRTSNVPSPE HAHSLSTPSR SCSSSSHSLI HSLTQSSPRS
SPVNQFRPIT LCAVPSQSQL SMPLAMPLPN RNVTVSVDSL LNPVTTCNVY HGKRFLEPLE
NLAQTSASFS SSIFRLPTPI ATPTRESPED PDWPAKTFSQ LLLERYSSQS QSLGNNSSTE
SSSLSGGATP TPTPMSSLDE LVTPLLLSFA SPSQPMLSAH GIGEGQREQG SDSDATVCST
TSSMESL
