SCYD_COLOR
ID SCYD_COLOR Reviewed; 188 AA.
AC Q00455; A0A484FJW6; N4VLA3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Scytalone dehydratase;
DE EC=4.2.1.94;
GN Name=SCD1 {ECO:0000303|PubMed:8953707}; ORFNames=Cob_03011, Cob_v008979;
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=8953707; DOI=10.1128/aem.62.12.4340-4344.1996;
RA Kubo Y., Takano Y., Endo N., Yasuda N., Tajima S., Furusawa I.;
RT "Cloning and structural analysis of the melanin biosynthesis gene SCD1
RT encoding scytalone dehydratase in Colletotrichum lagenarium.";
RL Appl. Environ. Microbiol. 62:4340-4344(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422;
RX PubMed=30893003; DOI=10.1094/mpmi-12-18-0352-a;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
CC -!- FUNCTION: Scytalone dehydratase; part of the gene cluster that mediates
CC the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green
CC pigment and a structural component of the conidial wall
CC (PubMed:8953707). Within the pathway, catalyzes the dehydration of
CC scytalone as well as of vermelone (PubMed:8953707).
CC {ECO:0000269|PubMed:8953707}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=scytalone = 1,3,8-trihydroxynaphthalene + H2O;
CC Xref=Rhea:RHEA:24396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16945,
CC ChEBI:CHEBI:18393; EC=4.2.1.94;
CC Evidence={ECO:0000269|PubMed:8953707};
CC -!- ACTIVITY REGULATION: Carpropamid acts as an efficient inhibitor of
CC scytalone dehydratase activity. {ECO:0000269|PubMed:8953707}.
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000269|PubMed:8953707}.
CC -!- SUBUNIT: Homotrimer (By similarity). Each subunit contains an active
CC site, located in the central part of the hydrophobic core of the
CC monomer, which functions independently (By similarity).
CC {ECO:0000250|UniProtKB:P56221}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:O14434}.
CC -!- DISRUPTION PHENOTYPE: Forms reddish-brown colonies and accumulated
CC reddish pigments in the culture medium (PubMed:8953707).
CC {ECO:0000269|PubMed:8953707}.
CC -!- SIMILARITY: Belongs to the scytalone dehydratase family. {ECO:0000305}.
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DR EMBL; D86079; BAA13009.1; -; Genomic_DNA.
DR EMBL; KB725656; ENH88853.1; -; Genomic_DNA.
DR EMBL; AMCV02000025; TDZ18313.1; -; Genomic_DNA.
DR AlphaFoldDB; Q00455; -.
DR SMR; Q00455; -.
DR STRING; 1213857.Q00455; -.
DR EnsemblFungi; ENH88853; ENH88853; Cob_03011.
DR eggNOG; ENOG502SNND; Eukaryota.
DR HOGENOM; CLU_101889_0_0_1; -.
DR OrthoDB; 1377897at2759; -.
DR UniPathway; UPA00785; -.
DR PHI-base; PHI:58; -.
DR Proteomes; UP000014480; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030411; F:scytalone dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR004235; Scytalone_dehydratase.
DR Pfam; PF02982; Scytalone_dh; 1.
DR PIRSF; PIRSF024851; SCD1; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Endosome; Lyase; Melanin biosynthesis; Reference proteome.
FT CHAIN 1..188
FT /note="Scytalone dehydratase"
FT /id="PRO_0000097638"
FT ACT_SITE 82
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT ACT_SITE 107
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P56221"
SQ SEQUENCE 188 AA; 21687 MW; A58F3EB940321EFA CRC64;
MASPAGNITF EDYLGLNAAL FEWADSYDSK DWDRLRKCIA PELRIDYRSF LDKIWEAMPA
EEFIAMISDK SVLGNPLLKT QHFIGGSRWE KVSDTEVIGH HQLRVPHQKY TDASRTEVAV
KGHAHSYNMH WYRKVNGVWK FAGLNPEIRW SEYDFDAVFA DGRDSYGTED QKTDVKVVEK
EIKFAAAH
