GenomeNet

Database: UniProt
Entry: A0A158NEI5_ATTCE
LinkDB: A0A158NEI5_ATTCE
Original site: A0A158NEI5_ATTCE 
ID   A0A158NEI5_ATTCE        Unreviewed;       304 AA.
AC   A0A158NEI5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
GN   Name=105619025 {ECO:0000313|EnsemblMetazoa:XP_012055943.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012055943.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012055943.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
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|RuleBase:RU363097}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ADTU01013404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012055943.1; XM_012200553.1.
DR   AlphaFoldDB; A0A158NEI5; -.
DR   EnsemblMetazoa; XM_012200553.1; XP_012055943.1; LOC105619025.
DR   GeneID; 105619025; -.
DR   KEGG; acep:105619025; -.
DR   eggNOG; KOG1221; Eukaryota.
DR   InParanoid; A0A158NEI5; -.
DR   OMA; FANCDED; -.
DR   OrthoDB; 1434498at2759; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
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; IEA:InterPro.
DR   GO; GO:1901568; P:fatty acid derivative metabolic process; IEA:UniProt.
DR   CDD; cd05236; FAR-N_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR026055; FAR.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11011:SF12; FATTY ACYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU363097};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU363097};
KW   NADP {ECO:0000256|RuleBase:RU363097};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT   DOMAIN          21..291
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
SQ   SEQUENCE   304 AA;  34436 MW;  FD54A8196146E7CD CRC64;
     MEEKIAKSEI ISFYKDKTIF ITGASGFMGK VLLEKLLFTC SNLNKIYILI RSKKGRNIET
     RLDEMFKLPV FQRIRNEKPY LFKKVIPISG DVCLPNLGLT NQQCELLINE VHIVFHFAAT
     LRLEAKLKDA IEMNTTGTKK LLDLAKRMKH LVSLVHLSTA FCHVDQKELG ERCYDSPDDP
     QDVMRLVQWL DDEDINLITP KLLHPHPNTY TYSKRLAETL VSNEYPNLPC CIARPSIVIP
     SYLEPIPGWV DNLNGPTGLL VGAGKGVIRS MHCNGNYHAE VVPVDLAINA VITISYKIAV
     YKQK
//
DBGET integrated database retrieval system