ID A0A2T4BU50_TRILO Unreviewed; 211 AA.
AC A0A2T4BU50;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=M440DRAFT_1363143 {ECO:0000313|EMBL:PTB72840.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB72840.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB72840.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB72840.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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; KZ679140; PTB72840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4BU50; -.
DR STRING; 983965.A0A2T4BU50; -.
DR Proteomes; UP000240760; 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:UP000240760};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 131..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 22667 MW; EDE424C0B586B376 CRC64;
MIYAELKTNI ENQQHFLTTL SNHLAARYNR HPSSTVVSLH HSQGLLFGGS PGPAYVLAVM
ALACEVQPAT NKRNAAVLQK HLEVMLGVPS ARGMVYFVPV AEEWLAWGGV TVTGRIAEAV
AGVEGKEVQD RRRLKSLSLR RSTPAEVPSP SSQSTSPSKN QKGASESSNA RIQAGDAETE
GNGRGVRKKK SIIHTLFRTS RVDDGDPGSQ G
//
