ID C1GCH9_PARBD Unreviewed; 428 AA.
AC C1GCH9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=PADG_04701 {ECO:0000313|EMBL:EEH48622.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH48622.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH48622.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH48622.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; KN275961; EEH48622.2; -; Genomic_DNA.
DR RefSeq; XP_010760107.1; XM_010761805.1.
DR AlphaFoldDB; C1GCH9; -.
DR SMR; C1GCH9; -.
DR STRING; 502780.C1GCH9; -.
DR GeneID; 22583760; -.
DR KEGG; pbn:PADG_04701; -.
DR VEuPathDB; FungiDB:PADG_04701; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_3_1; -.
DR InParanoid; C1GCH9; -.
DR OMA; CCRNFGT; -.
DR OrthoDB; 2786308at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08286; FDH_like_ADH2; 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; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42813:SF4; NADP-DEPENDENT ISOPROPANOL DEHYDROGENASE; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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:UP000001628};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 81..426
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 29..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 45525 MW; 936390ADDD1042DF CRC64;
MKLTSPRTFL PGTGMRKYHT TGLMRTLSSR PSHSIISSSS VSTPGNKYTR PPVSGVNSFN
HPTFTTKRFA SMKALVYQSQ GKVALEDRPC PTIQSSTDAI VKLKHTTICG TDLHIIKGDV
PTATPGRILG HEGVGTVVEV GTSVTSVKPG DTVLISCITA CGGCSYCRRE MSSHCTSGGW
ILGHTIDGTQ AEYVRIPHAA SSLYKLPSTV SLSDAVMLSD AMPTGLECGT LNGKVKPGSS
VVVIGAGAVG MSVMMTSMLY SPALLVVVDL DDTRLAMARS FGAHQTVNGK NQTEAVEKLM
KLTEGQGFDA VIEAVGVPGT FQLCQELVAP GGVIANVGVH GKKVDLHLEK LWDRNICITT
RLVDAVTTPM LLKLFKAGKL DLSKLSTHLE LIDILVSRTE FSFGECEKAY NVFGAAAQHN
AMKVLINM
//
