ID A0A0N1NFY6_9ACTN Unreviewed; 370 AA.
AC A0A0N1NFY6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Fatty acid desaturase {ECO:0000313|EMBL:KPI08267.1};
GN ORFNames=OK006_5653 {ECO:0000313|EMBL:KPI08267.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI08267.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI08267.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI08267.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC {ECO:0000256|ARBA:ARBA00009295}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI08267.1}.
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DR EMBL; LJCU01000222; KPI08267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NFY6; -.
DR PATRIC; fig|1592326.3.peg.6892; -.
DR Proteomes; UP000037912; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProt.
DR CDD; cd03506; Delta6-FADS-like; 1.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR012171; Fatty_acid_desaturase.
DR PANTHER; PTHR19353:SF19; DELTA(5) FATTY ACID DESATURASE C-RELATED; 1.
DR PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PIRSF; PIRSF015921; FA_sphinglp_des; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..344
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 40999 MW; 4097E57ED299708A CRC64;
MHAERNTVTT DMTIRGTGPA DHTDMAKPPP GGRGSDYAAL SREVKQSGLL KRRPGYYFVK
VGANLFLLAA GWAAFALIGQ SWWQLLTAAF LAVMFTQTGF IGHDAGHHQI AASKRVNNVL
GRVHADLLIG LSYGWWINKH NRHHSHPNHV DRDPDIADGA IAFTQDHARV RSGAYAWLAR
HQAWLFFPML LLEGLALHIA GVRALLDRTG TATSRAAKLA EAGLLTVHLG GYLAAVFLVL
SPVQAVCFLV VHQGLFGLYM GCSFAPNHKG MPVFAKDDKI DFLRRQVLTS RNIRGHRFTD
FALGGLNYQI EHHLFPSMPR PSLRHAQELV RTFCARHGIA YYETGLLNSY AQVLRHLHAV
GGPLRPEMEY
//
