GenomeNet

Database: UniProt
Entry: G1N155_MELGA
LinkDB: G1N155_MELGA
Original site: G1N155_MELGA 
ID   G1N155_MELGA            Unreviewed;       495 AA.
AC   G1N155;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE            EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000005203.2, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000005203.2, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA   Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA   Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA   Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA   Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA   Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA   Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA   Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA   Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000005203.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
CC       {ECO:0000256|RuleBase:RU363097}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 2 H(+) + 2 NADPH = (9Z)-octadecen-1-ol
CC         + CoA + 2 NADP(+); Xref=Rhea:RHEA:36323, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:73504;
CC         Evidence={ECO:0000256|ARBA:ARBA00036455};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36324;
CC         Evidence={ECO:0000256|ARBA:ARBA00036455};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 H(+) + 2 NADPH = (9Z,12Z)-
CC         octadecadien-1-ol + CoA + 2 NADP(+); Xref=Rhea:RHEA:36363,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73534;
CC         Evidence={ECO:0000256|ARBA:ARBA00036062};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36364;
CC         Evidence={ECO:0000256|ARBA:ARBA00036062};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 NADPH + octadecanoyl-CoA = CoA + 2 NADP(+) +
CC         octadecan-1-ol; Xref=Rhea:RHEA:36319, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32154, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.84;
CC         Evidence={ECO:0000256|ARBA:ARBA00000278};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36320;
CC         Evidence={ECO:0000256|ARBA:ARBA00000278};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + hexadecanoyl-CoA + 2 NADPH = CoA + hexadecan-1-ol + 2
CC         NADP(+); Xref=Rhea:RHEA:36315, ChEBI:CHEBI:15378, ChEBI:CHEBI:16125,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.84;
CC         Evidence={ECO:0000256|ARBA:ARBA00000203};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36316;
CC         Evidence={ECO:0000256|ARBA:ARBA00000203};
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|ARBA:ARBA00000233};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52717;
CC         Evidence={ECO:0000256|ARBA:ARBA00000233};
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC       {ECO:0000256|ARBA:ARBA00004549}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004549}.
CC   -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC       {ECO:0000256|RuleBase:RU363097}.
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DR   Ensembl; ENSMGAT00000005935.2; ENSMGAP00000005203.2; ENSMGAG00000005303.3.
DR   GeneTree; ENSGT00390000006367; -.
DR   HOGENOM; CLU_024661_0_0_1; -.
DR   InParanoid; G1N155; -.
DR   Proteomes; UP000001645; Chromosome 5.
DR   Bgee; ENSMGAG00000005303; Expressed in pectoralis major and 17 other cell types or tissues.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
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:SF45; FATTY ACYL-COA REDUCTASE 1; 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   Membrane {ECO:0000256|RuleBase:RU363097};
KW   NADP {ECO:0000256|RuleBase:RU363097};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU363097};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW   Transmembrane {ECO:0000256|RuleBase:RU363097};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   TRANSMEM        298..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   TRANSMEM        323..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363097"
FT   DOMAIN          15..284
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   REGION          404..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  55931 MW;  C867D5A21400B686 CRC64;
     MVSIPEYYEG KNVLLTGATG FMGKVLLEKL LRSCPKVKAV YVLVRPKAGQ TPETRIEEIT
     SCKLFDRLRE EQPYFKEKII VITSELTQPE LDLSNPVKEK LIECINIIFH CAATVRFNET
     LRDAVQLNVL STKQLLSLAQ QMTNLEVFMH VSTAYAYCNR KHIEEIVYPP PVDPKKLMDS
     LEWMDDSLVN DITPKLIGDR PNTYTYTKAL AEYVVQQEGA RLNTAIIRPS IVGASWKEPF
     PGWIDNFNGP SGLFIAAGKG ILRTMRASNG AVADLVPVDV VVNMTLAAAW YSGVNRKLVT
     HSVYVCVCIY MHIYTYIYIH IYMYMYVKQI VSLILVFLLP RIKYWKNVSL TNECMHAYIH
     TYVRTYIYIY XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXVRSLPR RRPSSPSAAG
     RPSAGTGSPR ATMASSGAEN TERPXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXSS
     SFPSFFFFPS SFLSF
//
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