ID A0A0K0DJG5_ANGCA Unreviewed; 115 AA.
AC A0A0K0DJG5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=L-dopachrome isomerase {ECO:0000256|ARBA:ARBA00042730};
DE EC=5.3.2.1 {ECO:0000256|ARBA:ARBA00039086};
DE EC=5.3.3.12 {ECO:0000256|ARBA:ARBA00038932};
DE AltName: Full=L-dopachrome tautomerase {ECO:0000256|ARBA:ARBA00041631};
DE AltName: Full=Phenylpyruvate tautomerase {ECO:0000256|ARBA:ARBA00041912};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0001154601-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0001154601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate = enol-phenylpyruvate; Xref=Rhea:RHEA:17097,
CC ChEBI:CHEBI:16815, ChEBI:CHEBI:18005; EC=5.3.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC EC=5.3.3.12; Evidence={ECO:0000256|ARBA:ARBA00036823};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the MIF family. {ECO:0000256|ARBA:ARBA00005851}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0K0DJG5; -.
DR STRING; 6313.A0A0K0DJG5; -.
DR WBParaSite; ACAC_0001154601-mRNA-1; ACAC_0001154601-mRNA-1; ACAC_0001154601.
DR Proteomes; UP000035642; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR InterPro; IPR001398; Macrophage_inhib_fac.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR PANTHER; PTHR11954; D-DOPACHROME DECARBOXYLASE; 1.
DR PANTHER; PTHR11954:SF6; MACROPHAGE MIGRATION INHIBITORY FACTOR; 1.
DR Pfam; PF01187; MIF; 1.
DR SUPFAM; SSF55331; Tautomerase/MIF; 1.
PE 3: Inferred from homology;
KW Cytokine {ECO:0000256|ARBA:ARBA00022514};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000035642};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
SQ SEQUENCE 115 AA; 12351 MW; 412F4056E14DD9CE CRC64;
MPVFSLHTNV GRDKVTVELL KQISALVARI LHKPESYVAV HVVPDQQMTF AGTADPCGVG
VLKSIGGIGG KQNNEHAKAL FALIKDHLGI EGNRMYIEFV DLGASDIAHN SKTFG
//
