ID F2STF0_TRIRC Unreviewed; 366 AA.
AC F2STF0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=TERG_05747 {ECO:0000313|EMBL:EGD89510.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD89510.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; GG700653; EGD89510.1; -; Genomic_DNA.
DR RefSeq; XP_003233879.1; XM_003233831.1.
DR AlphaFoldDB; F2STF0; -.
DR STRING; 559305.F2STF0; -.
DR GeneID; 10372437; -.
DR VEuPathDB; FungiDB:TERG_05747; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; F2STF0; -.
DR OMA; GPAWFVF; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF3; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G01980)-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 13..356
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 366 AA; 39263 MW; C51F09FE5C0CC936 CRC64;
MQDITFKGWV STSATSPLIY TTYEPKDFAS TDVDIAISHC GICGSDIHTL RSGWGPTNYP
CVAGHEIIGH IIRVGPEVAK LNSPSRDLRV GDRVGVGAQS GSCLRVDCEE CSSGLDNYCS
LMTGTYNGKY LDGSKSYGGY ADYWRGPAWF VFKIPDSLPS AVAAPLLCGG ATVFSPLLRG
GAGPGKHVGI IGIGGLGHMG LLFAKAMKCD KVVAISRTSS KKSDALVGLG ADVFIATDEE
KNWARTHSRT LDLIICTVSS GNMPIEKYLR LLKRGGEFIQ VGAPEDPFPG FRVGVMMGKG
LKIGASAIGS TEEIRAMLKL ASEQNIHPWV QERPMGNANQ VLVDMHEGKA RYRYVLVNGT
RSKTRL
//
