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Database: UniProt
Entry: A0A059DIH5_EUCGR
LinkDB: A0A059DIH5_EUCGR
Original site: A0A059DIH5_EUCGR 
ID   A0A059DIH5_EUCGR        Unreviewed;       564 AA.
AC   A0A059DIH5;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN   ORFNames=EUGRSUZ_A02497 {ECO:0000313|EMBL:KCW90352.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW90352.1};
RN   [1] {ECO:0000313|EMBL:KCW90352.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW90352.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC       {ECO:0000256|RuleBase:RU363097}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC         primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC         Evidence={ECO:0000256|RuleBase:RU363097};
CC   -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00005928, ECO:0000256|RuleBase:RU363097}.
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DR   EMBL; KK198753; KCW90352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059DIH5; -.
DR   STRING; 71139.A0A059DIH5; -.
DR   EnsemblPlants; KCW90352; KCW90352; EUGRSUZ_A02497.
DR   Gramene; KCW90352; KCW90352; EUGRSUZ_A02497.
DR   eggNOG; KOG1221; Eukaryota.
DR   InParanoid; A0A059DIH5; -.
DR   OMA; GMSSCVN; -.
DR   GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0102965; F:alcohol-forming long-chain fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080019; F:alcohol-forming very long-chain fatty acyl-CoA reductase activity; IBA:GO_Central.
DR   GO; GO:1903175; P:fatty alcohol biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0009556; P:microsporogenesis; IEA:EnsemblPlants.
DR   GO; GO:0010584; P:pollen exine formation; IEA:EnsemblPlants.
DR   GO; GO:0009635; P:response to herbicide; IEA:EnsemblPlants.
DR   GO; GO:0010345; P:suberin biosynthetic process; IBA:GO_Central.
DR   CDD; cd05236; FAR-N_SDR_e; 1.
DR   CDD; cd09071; FAR_C; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR026055; FAR.
DR   InterPro; IPR033640; FAR_C.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11011:SF45; FATTY ACYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF03015; Sterile; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU363097};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU363097}; NADP {ECO:0000256|RuleBase:RU363097};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363097}.
FT   DOMAIN          83..388
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   DOMAIN          489..559
FT                   /note="Fatty acyl-CoA reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03015"
SQ   SEQUENCE   564 AA;  62690 MW;  36C68925D5670C72 CRC64;
     MCCQGSGSAI KSTVLKETSA SVCTNQSSAL IDAGSLVTSP NGNSQAEICV NDLAPHAEHS
     HSLVEMDDGI GIVRFLRGKR FFITGATGFL AKVLVEKILR TVPDVGKIFL LMKAKDKDAA
     KARLSSEIIY SELFKNLQQT YGKSYEAFML SKLIPVVGDV SESNLGLGDE LVDFIANEVD
     IIVNSAANTK FDERYDVAIN INTKGPYHLM SFAKRCSQLK VFLQVSTAYV NGQRQGKIME
     KPFCVGDSIV TESYSAEPPT SLPQLDVESE IHLALESKKA LEDHAVAKKM KELGLNRAKK
     FGWQDTYVFT KAMGEMLIDD MRGEVPVIII RPSVIESTIK EPFPGWMEGN RMMDPIILYY
     GKGQLTGFLV DPNGVIDVVP ADIVVNATLA AIARHGMAGK SGVNIYQIAS SVVNPLVFQD
     LARLLYEHYN TSPCFDSKGR PIPVPSMKLF TSMDEFSAYL SGDASQISGL RAMTSDAKLS
     KKLEIVCRRS VEQIKKLANI YEPYAFYRGR FDNSNTERLM ERMSEEEKRR FGFDVGSIDW
     KDYIINVHIP GLRWHVMKER RTFI
//
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