ID F4SBA4_MELLP Unreviewed; 413 AA.
AC F4SBA4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MELLADRAFT_41048 {ECO:0000313|EMBL:EGF98077.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(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|RuleBase:RU361277}.
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DR EMBL; GL883186; EGF98077.1; -; Genomic_DNA.
DR RefSeq; XP_007418648.1; XM_007418586.1.
DR AlphaFoldDB; F4SBA4; -.
DR STRING; 747676.F4SBA4; -.
DR EnsemblFungi; EGF98077; EGF98077; MELLADRAFT_41048.
DR GeneID; 18927941; -.
DR KEGG; mlr:MELLADRAFT_41048; -.
DR VEuPathDB; FungiDB:MELLADRAFT_41048; -.
DR eggNOG; KOG0024; Eukaryota.
DR HOGENOM; CLU_026673_11_3_1; -.
DR InParanoid; F4SBA4; -.
DR OrthoDB; 948431at2759; -.
DR Proteomes; UP000001072; 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; cd08283; FDH_like_1; 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 PANTHER; PTHR42813:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G03930)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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:UP000001072};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..153
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 195..262
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT REGION 390..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45393 MW; 267F29B229E4494A CRC64;
MLALRWYGNK DVRLETVPVP AITEPNDVIC KVTGTTICGS DLHLYHKEIM QMQKGDILGH
EWMGIVDEVG SAIKNVKKGD RVVASFQIAC GDCSFCKEGL SSMCDRTNSS KLQEKLYGKP
FAGLFGYTHF AGGFAGGQAE YVRCPFGDTN LLKIPNSIPD EKALFLSDII PTSYHSVKCA
DVKEGKSVAI WGMGPIGLYA AKWCKLEGAR RVICIDRVPE RLAMASEILG CDVINYDVQT
DVVKAIYELE PEGVNCAIDA AAFRYTKGII HTVQRAIGLE TDSSEVVNEA IQAVRKFGTI
SLVADYAGWT NQFLIGALME KGITLRGTGQ APVQMYWKEL LKKVESGEFD PTIILSHRFS
IDEFPELYKS FDEKEMGILK TFVQTRFSNP PAPGTPSLSS LKSHDVKPSA VHA
//