DHPAA_AEDAE
ID DHPAA_AEDAE Reviewed; 521 AA.
AC Q16S21;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=3,4-dihydroxyphenylacetaldehyde synthase {ECO:0000303|PubMed:21283636};
DE Short=DHPAA synthase;
DE EC=4.1.1.107 {ECO:0000269|PubMed:21283636};
GN ORFNames=AAEL010734 {ECO:0000312|EMBL:EAT37247.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [2]
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 -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CH477689; EAT37247.1; -; Genomic_DNA.
DR RefSeq; XP_001661057.1; XM_001661007.1.
DR AlphaFoldDB; Q16S21; -.
DR SMR; Q16S21; -.
DR STRING; 7159.AAEL018197-PA; -.
DR GeneID; 5573809; -.
DR KEGG; aag:5573809; -.
DR VEuPathDB; VectorBase:AAEL022306; -.
DR HOGENOM; CLU_011856_3_1_1; -.
DR InParanoid; Q16S21; -.
DR OMA; PAPSHCH; -.
DR PhylomeDB; Q16S21; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
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:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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 Catecholamine metabolism; Cuticle; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..521
FT /note="3,4-dihydroxyphenylacetaldehyde synthase"
FT /id="PRO_0000446129"
FT MOD_RES 306
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58909 MW; 61887FAE42C99624 CRC64;
MANMDIDEFK EFGKAAIDFV ADYLVNIRDR DVLPSVEPGY LHDLLPNEIP EKGDDWKTIM
EEFKRFIVPG LTHWQSPHFH AFYPSQTSYS SIVGETLAAG LGVVGFSWIC SPVCTELEVI
MMNWIGQLLN LPRCFLNCDE GNGGGVIQGS ASESIFIAVL VAREQAVRRL KNEHPELTEA
EIRGRLVAYT SDQSNSAVEK SGILGAIKMR LLPADDDCVL RGRTLKKAVE EDKANGLFPV
IMVATLGTTG TCAYDNLEEI GPYCNDNKLW LHVDAAYAGA SFCLPEYAWI KKGLEMADSL
NFNLHKWLFV NFDCCAMWFK DAAMITEAFS VDRIYLQHKF QGMSKAPDYR HWQIQLGRRF
RSLKVWITLK TMGAEKIREL IRFHISLAQK FEQYVRADPR FEVTSSTLAL VCFRLKGEDT
YSKQLLDNIV KRKKIYMIPA TYQGKFILRF MIAGIDPQAE DIDYAWNEVK SQTDLLLGVD
DNGNNVCSKK LIKEEIFEKD NPVGKITESL GGLVLANEKA Q
