ID A0A1B0ALP3_9MUSC Unreviewed; 827 AA.
AC A0A1B0ALP3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Fatty acyl-CoA reductase {ECO:0000256|RuleBase:RU363097};
DE EC=1.2.1.84 {ECO:0000256|RuleBase:RU363097};
OS Glossina palpalis gambiensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI000968-PA, ECO:0000313|Proteomes:UP000092460};
RN [1] {ECO:0000313|Proteomes:UP000092460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPPI000968-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI000968-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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}.
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DR EMBL; JXJN01000032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0ALP3; -.
DR STRING; 67801.A0A1B0ALP3; -.
DR EnsemblMetazoa; GPPI000968-RA; GPPI000968-PA; GPPI000968.
DR VEuPathDB; VectorBase:GPPI000968; -.
DR Proteomes; UP000092460; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011:SF24; FATTY ACYL-COA REDUCTASE; 1.
DR PANTHER; PTHR11011; MALE STERILITY PROTEIN 2-RELATED; 1.
DR Pfam; PF07993; NAD_binding_4; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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 Transmembrane {ECO:0000256|RuleBase:RU363097};
KW Transmembrane helix {ECO:0000256|RuleBase:RU363097}.
FT TRANSMEM 796..820
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363097"
FT DOMAIN 14..281
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT DOMAIN 394..638
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 827 AA; 94639 MW; ECAAE2B6A545E71B CRC64;
MSVTKFYVDQ EIFITGGSGF IGKALIEKIM RSFPEFSKIY VLLRSKVNKS ADERLQILLK
DPVFERVRRE QPQNFQKIFS IAGDCKELGL GISPDDRKRI ENVTMIFHSA ASVRFDDNFK
DAILLNTRGA FELIKIAEGL KKLKAFIHIS TTYSNPDRHV VEEKIYPPLA DWRTTIKLAE
HYDTKMLNIL FAKYSSHQPN TYTFTKHLAE HIVNDHRHKI PILLYRPSIV VSSIFEPVPG
WIDNFNGPIG LLIACGLGIL RTSHANPNVR ADIVPVDVCV QGLILAGYKL GNLIEATRED
QLLEVVNCSN ALIRTFCFGK IIELGRTIIR KNPLEKCMWL PSGSITDNVI WHYVRLQRRI
FMSCQALYKF YTTQWLFLND NFLALKNVIP PEDFKIYVLM RNKGGKTADQ RLRILLKDPV
FNRAQEEQPE SFKNIFAIAG DCKELGLGIS PVDRKRIENV TMIFHSAASV RFDDNFKDAI
LLNTRGAFEL IKIAEGLKKL KAFIHISTTY SNPDRHVVEE KIYPPLADWR TTIKLAEHYD
TKMLNILFAK YSSHQPNTYT FTKHLAEQIV NDSRDKIPIL LYRPSMVTSS LLEPVPGWLD
NFNGPIGLLV ACGAGVMMTN YSNPNIKADM VTIDVTVQGL LLAGYKIGNR FEPMTLDKPL
DVLHCSRANV KPVTYGALTE AGKRLVRQNP FEKFIWLPCG SVTTNPILHY TRNQRRIAMA
SQALQTFYTT QWLFSNEKFL ELESLISSED LDKLRLFQYM KAELDTLIWR GIGGCKEFLL
REPPNATQSA RLRLKFFFFM HYLAQFVGAV LIGRLMYFLY KKLCSTA
//
