DHAPP_DROME
ID DHAPP_DROME Reviewed; 510 AA.
AC P18486; Q9VIZ8; Q9VIZ9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=3,4-dihydroxyphenylacetaldehyde synthase;
DE Short=DHPAA synthase, isoform A;
DE EC=4.1.1.107 {ECO:0000269|PubMed:21283636};
DE AltName: Full=Alpha-methyldopa hypersensitive protein;
GN Name=amd; Synonyms=l(2)amd; ORFNames=CG10501;
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 [GENOMIC DNA].
RX PubMed=3021571; DOI=10.1093/genetics/114.2.453;
RA Marsh J.L., Erfle M.P., Leeds C.A.;
RT "Molecular localization, developmental expression and nucleotide sequence
RT of the alpha-methyldopa hypersensitive gene of Drosophila.";
RL Genetics 114:453-467(1986).
RN [2]
RP SEQUENCE REVISION.
RA Marsh J.L.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS A AND B).
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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21283636; DOI=10.1371/journal.pone.0016124;
RA Vavricka C., Han Q., Huang Y., Erickson S.M., Harich K., Christensen B.M.,
RA Li J.;
RT "From L-dopa to dihydroxyphenylacetaldehyde: a toxic biochemical pathway
RT plays a vital physiological function in insects.";
RL PLoS ONE 6:E16124-E16124(2011).
CC -!- FUNCTION: Catalyzes both the decarboxylation and deamination of L-dopa
CC to 3,4-dihydroxylphenylacetaldehyde (DHPAA) (PubMed:21283636). Probably
CC responsible for the protein cross-linking during the development of
CC flexible cuticles (PubMed:21283636). Participates in catecholamine
CC catabolism (PubMed:21283636). {ECO:0000269|PubMed:21283636}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + L-dopa + O2 = 3,4-dihydroxyphenylacetaldehyde +
CC CO2 + H2O2 + NH4(+); Xref=Rhea:RHEA:55524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57504; EC=4.1.1.107;
CC Evidence={ECO:0000269|PubMed:21283636};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55525;
CC Evidence={ECO:0000269|PubMed:21283636};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=The 2 isoforms are probably produced by alternative splicing.
CC {ECO:0000305};
CC Name=A;
CC IsoId=P18486-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P18486-2; Sequence=VSP_060031;
CC -!- DEVELOPMENTAL STAGE: Reaches a maximum in mid-embryogenesis.
CC {ECO:0000269|PubMed:3021571}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; X04695; CAA28400.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53760.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53759.2; -; Genomic_DNA.
DR EMBL; BT044421; ACH92486.1; -; mRNA.
DR PIR; A28569; A28569.
DR RefSeq; NP_476592.1; NM_057244.4. [P18486-1]
DR RefSeq; NP_724162.1; NM_165278.2. [P18486-2]
DR PDB; 6JRL; X-ray; 2.20 A; A=1-510.
DR PDBsum; 6JRL; -.
DR AlphaFoldDB; P18486; -.
DR SMR; P18486; -.
DR BioGRID; 61173; 1.
DR IntAct; P18486; 2.
DR STRING; 7227.FBpp0080697; -.
DR DNASU; 35188; -.
DR EnsemblMetazoa; FBtr0081153; FBpp0080697; FBgn0000075. [P18486-2]
DR EnsemblMetazoa; FBtr0081154; FBpp0080698; FBgn0000075. [P18486-1]
DR GeneID; 35188; -.
DR KEGG; dme:Dmel_CG10501; -.
DR UCSC; CG10501-RB; d. melanogaster.
DR CTD; 11700; -.
DR FlyBase; FBgn0000075; amd.
DR VEuPathDB; VectorBase:FBgn0000075; -.
DR eggNOG; KOG0628; Eukaryota.
DR HOGENOM; CLU_011856_3_0_1; -.
DR InParanoid; P18486; -.
DR OMA; PAPSHCH; -.
DR OrthoDB; 856958at2759; -.
DR PhylomeDB; P18486; -.
DR BRENDA; 4.1.1.107; 1994.
DR SignaLink; P18486; -.
DR BioGRID-ORCS; 35188; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35188; -.
DR PRO; PR:P18486; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000075; Expressed in embryonic/larval foregut (Drosophila) and 30 other tissues.
DR ExpressionAtlas; P18486; baseline and differential.
DR Genevisible; P18486; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IDA:FlyBase.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:FlyBase.
DR GO; GO:0019239; F:deaminase activity; IDA:FlyBase.
DR GO; GO:0036468; F:L-dopa decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR GO; GO:0042424; P:catecholamine catabolic process; IDA:UniProtKB.
DR GO; GO:0006584; P:catecholamine metabolic process; IMP:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0040003; P:chitin-based cuticle development; IMP:UniProtKB.
DR GO; GO:0042335; P:cuticle development; 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.
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 3D-structure; Alternative splicing; Catecholamine metabolism; Cuticle;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..510
FT /note="3,4-dihydroxyphenylacetaldehyde synthase"
FT /id="PRO_0000147010"
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..101
FT /note="MDAKEFREFGKAAIDYIADYLENIRDDDVLPNVEPGYLLDLLPTEMPEEPEA
FT WKDVLGDISRVIKPGLTHWQSPHMHAYYPTSTSYPSIVGEMLASGFGVI -> MDFDEF
FT REFGHASIEFLINYLSGIRERDVLPSTAPYAVINQLPKEIPEQPDHWREVLKDLENIIL
FT PGLTHWQSPYFNAFYPSSSSAGSIIGELLIAGIGVL (in isoform B)"
FT /id="VSP_060031"
FT CONFLICT 71..72
FT /note="WQ -> SE (in Ref. 1; CAA28400)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="G -> E (in Ref. 1; CAA28400)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="R -> A (in Ref. 1; CAA28400)"
FT /evidence="ECO:0000305"
FT CONFLICT 477..478
FT /note="EQ -> DE (in Ref. 1; CAA28400)"
FT /evidence="ECO:0000305"
FT CONFLICT 493..494
FT /note="QH -> HD (in Ref. 1; CAA28400)"
FT /evidence="ECO:0000305"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 109..125
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 148..168
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 235..244
FT /evidence="ECO:0007829|PDB:6JRL"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 359..394
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 417..430
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:6JRL"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:6JRL"
FT HELIX 457..477
FT /evidence="ECO:0007829|PDB:6JRL"
SQ SEQUENCE 510 AA; 57021 MW; 94464F49896E7654 CRC64;
MDAKEFREFG KAAIDYIADY LENIRDDDVL PNVEPGYLLD LLPTEMPEEP EAWKDVLGDI
SRVIKPGLTH WQSPHMHAYY PTSTSYPSIV GEMLASGFGV IGFSWICSPA CTELEVVVMD
WLAKFLKLPA HFQHASDGPG GGVIQGSASE AVLVAVLAAR EQAVANYRES HPELSESEVR
GRLVAYSSDQ SNSCIEKAGV LAAMPIRLLP AGEDFVLRGD TLRGAIEEDV AAGRIPVICV
ATLGTTGTCA YDDIESLSAV CEEFKVWLHV DAAYAGGAFA LEECSDLRKG LDRVDSLNFN
LHKFMLVNFD CSAMWLRDAN KVVDSFNVDR IYLKHKHEGQ SQIPDFRHWQ IPLGRRFRAL
KVWITFRTLG AEGLRNHVRK HIELAKQFEQ LVLKDSRFEL VAPRALGLVC FRPKGDNEIT
TQLLQRLMDR KKIYMVKAEH AGRQFLRFVV CGMDTKASDI DFAWQEIESQ LTDLQAEQSL
VARKSGNVGD LAQHFQIHLS TENATHEKSQ
