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P48861 (DDC_MANSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aromatic-L-amino-acid decarboxylase

Short name=AADC
EC=4.1.1.28
Alternative name(s):
DOPA decarboxylase
Short name=DDC
Gene names
Name:Ddc
OrganismManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier7130 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.

Catalytic activity

L-dopa = dopamine + CO2.

5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the group II decarboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Aromatic-L-amino-acid decarboxylase
PRO_0000146948

Sites

Binding site821Substrate By similarity
Binding site1921Substrate By similarity

Amino acid modifications

Modified residue3031N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P48861 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 87538994956A7C77

FASTA50857,892
        10         20         30         40         50         60 
MNPGDFKDFA KAMTDYITEY LENIRDRQVV PSVKPGYLRP LVPEQAPQQA EPWTAVMADI 

        70         80         90        100        110        120 
ERVVMSGVTH WQSPRFHAYF PTANSYPSIV ADMLSGAIAC IGFTWIASPA CTELEVVMLD 

       130        140        150        160        170        180 
WLGQMLGLPD QFLARSGGEG GGVIQGTASE ATFVALLGAK SRMMHRVKEQ HPEWTETDIL 

       190        200        210        220        230        240 
GKLVGYCNQQ AHSSVERAGL LGGVKLRSLK PDSKRRLRGD TLREAIDEDI RNGLIPFYVV 

       250        260        270        280        290        300 
ATLGTTSSCA FDALDEIGDV CNASDIWLHV DAAYAGSAFI CPEYRHFMKG VEKADSFNFN 

       310        320        330        340        350        360 
PHKWMLVNFD CSAMWLKQPR WIVDAFNVDP LYLKHEQQGS APDYRHWQIP LGRRFRSLKL 

       370        380        390        400        410        420 
WFVLRLYGVE NLQKYIRKQI GFAHLFERLL TSDERFELFE EVTMGLVCFR LKGSNEINEE 

       430        440        450        460        470        480 
LLRRINGRGK IHLVPSKVDD VYFLRLAICS RFTEESDMHV SWEEIKDRLM MFLKSKGAVL 

       490        500 
IKIICSTTRR TKNILTYIKQ NIFRDVGL 

« Hide

References

[1]"Characterization of the dopa decarboxylase gene of Manduca sexta and its suppression by 20-hydroxyecdysone."
Hiruma K., Carter M.S., Riddiford L.M.
Dev. Biol. 169:195-209(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epidermis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03909 mRNA. Translation: AAC46604.1.

3D structure databases

ProteinModelPortalP48861.
SMRP48861. Positions 1-467.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.28. 3173.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR010977. Aromatic_deC.
IPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
PRINTSPR00800. YHDCRBOXLASE.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDDC_MANSE
AccessionPrimary (citable) accession number: P48861
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families