ID C6HDN3_AJECH Unreviewed; 125 AA.
AC C6HDN3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 41.
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};
GN ORFNames=HCDG_04314 {ECO:0000313|EMBL:EER41667.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER41667.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; GG692423; EER41667.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HDN3; -.
DR STRING; 544712.C6HDN3; -.
DR VEuPathDB; FungiDB:HCDG_04314; -.
DR HOGENOM; CLU_129906_1_0_1; -.
DR OMA; YINFFDM; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:GOC.
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 Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
SQ SEQUENCE 125 AA; 13770 MW; BA422B5D83A4B64B CRC64;
MPFLELLTNA TLSREQSKEL ALSLSKTASE ILRKPEALIS VRVQANEVLT FAGTHDPCFQ
LRITSLGNLK PDNNILFSKA FADFLKIKIG VENDRGYIVF SDPGYKGTTG AELWGSKHLS
NASQK
//
