ID   DOPD_CHICK              Reviewed;         118 AA.
AC   Q5ZMG0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=D-dopachrome decarboxylase;
DE            EC=4.1.1.84 {ECO:0000250|UniProtKB:P30046};
DE   AltName: Full=D-dopachrome tautomerase;
GN   Name=DDT; ORFNames=RCJMB04_2c16;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Tautomerization of D-dopachrome with decarboxylation to give
CC       5,6-dihydroxyindole (DHI). {ECO:0000250|UniProtKB:P30046}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-dopachrome + H(+) = 5,6-dihydroxyindole + CO2;
CC         Xref=Rhea:RHEA:18441, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:27404, ChEBI:CHEBI:58782; EC=4.1.1.84;
CC         Evidence={ECO:0000250|UniProtKB:P30046};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18442;
CC         Evidence={ECO:0000250|UniProtKB:P30046};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P30046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30046}.
CC   -!- SIMILARITY: Belongs to the MIF family. {ECO:0000305}.
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DR   EMBL; AJ719424; CAG31083.1; -; mRNA.
DR   RefSeq; NP_001025838.1; NM_001030667.1.
DR   AlphaFoldDB; Q5ZMG0; -.
DR   SMR; Q5ZMG0; -.
DR   STRING; 9031.ENSGALP00000010251; -.
DR   PaxDb; Q5ZMG0; -.
DR   PRIDE; Q5ZMG0; -.
DR   GeneID; 416937; -.
DR   KEGG; gga:416937; -.
DR   CTD; 100037417; -.
DR   VEuPathDB; HostDB:geneid_416937; -.
DR   eggNOG; KOG1759; Eukaryota.
DR   InParanoid; Q5ZMG0; -.
DR   OrthoDB; 1515400at2759; -.
DR   PhylomeDB; Q5ZMG0; -.
DR   PRO; PR:Q5ZMG0; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0033981; F:D-dopachrome decarboxylase activity; ISS:UniProtKB.
DR   GO; GO:0050178; F:phenylpyruvate tautomerase activity; IBA:GO_Central.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.429.10; -; 1.
DR   InterPro; IPR001398; Macrophage_inhib_fac.
DR   InterPro; IPR019829; Macrophage_inhib_fac_CS.
DR   InterPro; IPR014347; Tautomerase/MIF_sf.
DR   PANTHER; PTHR11954; PTHR11954; 1.
DR   Pfam; PF01187; MIF; 1.
DR   SUPFAM; SSF55331; SSF55331; 1.
DR   PROSITE; PS01158; MIF; 1.
PE   3: Inferred from homology;
KW   Acetylation; Cytoplasm; Lyase; Melanin biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O35215"
FT   CHAIN           2..118
FT                   /note="D-dopachrome decarboxylase"
FT                   /id="PRO_0000337234"
FT   MOD_RES         2
FT                   /note="N-acetylproline"
FT                   /evidence="ECO:0000250|UniProtKB:O35215"
SQ   SEQUENCE   118 AA;  12835 MW;  5F7A61E65C09A4A8 CRC64;
     MPFVELETNL PAERLPPGLP LKLCEATATI LGKPAERVNV TVRSGMPMVL AGSAEPCAQL
     LVSSIGVVGS AQQNQGHSAR FFDFLTTELG LGPERIVIRF YPLEPWQIGK NRTVMTFL