ID E9G3A7_DAPPU Unreviewed; 369 AA.
AC E9G3A7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=DAPPUDRAFT_309058 {ECO:0000313|EMBL:EFX85742.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX85742.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX85742.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
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; GL732531; EFX85742.1; -; Genomic_DNA.
DR AlphaFoldDB; E9G3A7; -.
DR STRING; 6669.E9G3A7; -.
DR EnsemblMetazoa; EFX85742; EFX85742; DAPPUDRAFT_309058.
DR KEGG; dpx:DAPPUDRAFT_309058; -.
DR eggNOG; KOG1759; Eukaryota.
DR HOGENOM; CLU_750654_0_0_1; -.
DR InParanoid; E9G3A7; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050178; F:phenylpyruvate tautomerase activity; IBA:GO_Central.
DR Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR InterPro; IPR001398; Macrophage_inhib_fac.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR11954; D-DOPACHROME DECARBOXYLASE; 1.
DR PANTHER; PTHR11954:SF6; MACROPHAGE MIGRATION INHIBITORY FACTOR; 1.
DR Pfam; PF01187; MIF; 1.
DR Pfam; PF02892; zf-BED; 2.
DR SMART; SM00614; ZnF_BED; 2.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR SUPFAM; SSF55331; Tautomerase/MIF; 1.
DR PROSITE; PS50808; ZF_BED; 2.
PE 3: Inferred from homology;
KW Cytokine {ECO:0000256|ARBA:ARBA00022514};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00027}.
FT DOMAIN 35..83
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT DOMAIN 184..232
FT /note="BED-type"
FT /evidence="ECO:0000259|PROSITE:PS50808"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41156 MW; 922046FA01D7648C CRC64;
MAYQGAGHSG NEESPSKEDA SSDGPPRKKG RKHREKVSWV WQYFIEEGNF AICQFCEASL
STASTTTLKY HLNHLHQDLI AEGEPNLNQP KPRIQVVSIP SKSPLKNSVN VTKNPPLPKH
FLKETTALIS KMLGKPSSNI RVVQLIQDDE AGNIENRRKK HSPSSKDYSS AVSSNRNKTK
KHREKVSWVW QHFRKEGNMA TCEFCQASLS AASTTTLKYH LNHLHKDLLT NETSSNMDST
NPASQTEIIE IEPEIIMVPE IAKMPHLKIT TNISKSSVPS DFLDETSALL SKMLDKPENC
SIVTVVPERL MLWGGEKGPC AIARLRGVGK LGDSDNANLK VQLGEHIEKF LGVPPCRMLI
HNDINTAYF
//
