ID C9SUY2_VERA1 Unreviewed; 340 AA.
AC C9SUY2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=VDBG_08707 {ECO:0000313|EMBL:EEY22597.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(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; DS985226; EEY22597.1; -; Genomic_DNA.
DR RefSeq; XP_003000911.1; XM_003000865.1.
DR AlphaFoldDB; C9SUY2; -.
DR STRING; 526221.C9SUY2; -.
DR GeneID; 9534299; -.
DR KEGG; val:VDBG_08707; -.
DR eggNOG; ENOG502S2ZV; Eukaryota.
DR HOGENOM; CLU_038298_2_1_1; -.
DR OMA; EDCAGWK; -.
DR OrthoDB; 2718868at2759; -.
DR Proteomes; UP000008698; 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:UP000008698};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 340 AA; 37167 MW; AD3C286770B4CCD1 CRC64;
MSSSLTVDNT KSLSSPIAQT RRPSNAAQLT FAKRKEAQRE EKVTSLQSLM NDGHWVSSRS
VSRPLPVDPT RESTKVKSQP TPAQSRSRYF EDAFQAGREV SLAKDRIRSE AVIMAEVCTN
VIRPVSSIVV TLQHGACMLF GGSFDSAYTM SISGLPIEFA PTKNRRIAAL LQKYMEESLG
VLPRRGYLRF VPLPEENVAW DGKTVASELA ETQGLEDEHG VATILQHKTS RRLSAKVKES
RVRSAPASLT RQSMSSLKSR STKTNSAPDR IDLIASHSMD SGPPMPLMAT VCEGGESRAG
GMTSNADKDD CKGEELWKSP KVGKRKSFVA SFFGRSKLGV
//
