ID A0A1L9T3Z6_9EURO Unreviewed; 939 AA.
AC A0A1L9T3Z6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=ASPSYDRAFT_61419 {ECO:0000313|EMBL:OJJ54071.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ54071.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the ADIP family.
CC {ECO:0000256|ARBA:ARBA00009291}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; KV878595; OJJ54071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9T3Z6; -.
DR STRING; 1036612.A0A1L9T3Z6; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_61419; -.
DR OrthoDB; 2726628at2759; -.
DR Proteomes; UP000184356; 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; IPR021622; Afadin/alpha-actinin-bd.
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 Pfam; PF11559; ADIP; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000184356};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 589..930
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 235..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 102835 MW; 4E9E12F56011A935 CRC64;
MEPQGDLHAA STYINNVLLA RGLVKTGRPI DFANPENEEG GVTDTMARII NLVNDLVLRR
DREAEHRENL ATTIRTLRAE DSHKTVEISE LSRSLALAEA QGRAFKTNMS SADATIRGLK
DQVQRMKTTV QQVRSQCAND IRKRDLELQK LKAHLADRQR GKRDGLGVTT ININPAASQS
SRARYLSGGE GVHDPGYSLK EETNEFLTQL CQTLSDENDS LILLARNTVN TLKEVQGLSS
TENSATENGY SYGAASTGPQ RSTHGGPAVT NLPASCDELS GEMEQVLEHL QTLLTNPSFV
PLEEVEVRDE EIKRLREGWE KMESRWRQAV TMMDGWHKRI AHGGGSIRAE ELRMGLKLDV
QVHSRHSGVR DSDVAMHSPI FEDQEDEENE DGDEDECEEE MTGAVPNRED TAPPPEEQPQ
PSPSRALKER TDNATLVAQP PRKGVIISGG DRKSPSKHRQ EEDDTMPIKA HQSDAVTRRP
SRRRAEPKGP RPGPSRMSVS QKLAAAESEA RAAEQSRREQ ESRKRSRGGK IARKRTGDRR
RSTLTTDELG ELMGFFQTTN LPHSPNWILS YESPAMPDTF TGWVAHDPKS PLTHEPFTPK
PFEETDIEVQ ISHCGICGSD VHTIRSGWAP ADYPCVVGHE IVGTAIRIGS AVPSSKHIKP
GDRVGIGAQC SACLRPDCEA CADNEESYCP KMVGTYNSRY PDGSKAYGGY ANRWRGPGHF
VFRIPEKLSS EEAAPLLCGG VTVFAPLRRF GAGPGKRVGI VGIGGLGHMG LLFAKAMGSD
AVVAISRSSA KKSDAVGPTP GSLGADDFIA TGEDKTWAKK HARSLDLIIC TVSGENMPLA
GYLRLLKRNG VFVQVGAPEE PLPPLRAFSL IQKGVKVTGS TIGSPEDIRV MLELAAENGV
KPWVQSRPME EVNLALADMH EGKARYRYVL ENAKKTGKL
//
