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Database: UniProt
Entry: A0A1C4VDF5_MICVI
LinkDB: A0A1C4VDF5_MICVI
Original site: A0A1C4VDF5_MICVI 
ID   A0A1C4VDF5_MICVI        Unreviewed;       349 AA.
AC   A0A1C4VDF5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Fatty acid desaturase {ECO:0000313|EMBL:SCE81759.1};
GN   ORFNames=GA0074695_1350 {ECO:0000313|EMBL:SCE81759.1};
OS   Micromonospora viridifaciens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1881 {ECO:0000313|EMBL:SCE81759.1, ECO:0000313|Proteomes:UP000198242};
RN   [1] {ECO:0000313|EMBL:SCE81759.1, ECO:0000313|Proteomes:UP000198242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43909 {ECO:0000313|EMBL:SCE81759.1,
RC   ECO:0000313|Proteomes:UP000198242};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295}.
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DR   EMBL; LT607411; SCE81759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4VDF5; -.
DR   OrthoDB; 104711at2; -.
DR   Proteomes; UP000198242; Chromosome i.
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        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..326
FT                   /note="Fatty acid desaturase"
FT                   /evidence="ECO:0000259|Pfam:PF00487"
SQ   SEQUENCE   349 AA;  38135 MW;  68D6E6854D7265AC CRC64;
     MTSSTLTAPP ERRGSDYARL SRRVAEAGLF ARRPGWYAAR IGLTLGAFLA GWAVVVAVGD
     SWAQMLLAVG MAVATTQVAF LGHDAGHRQM FRRRGPSELA GLIAGNLAVG LSYGWWVDKH
     NRHHANPNHT DEDPDVGAGA LVWTYEQAAA TRGVGRWLAR RQAWLFFPLL LLEGLALHVA
     SVQALAGREG GRWRTPVRHR AVEAVLLVAH AVGYLGLLFA VMSPGKALLF AAVHQGLWGL
     YMGCAFAPNH KGMPMPSAED DLDFLRKQVL TSRNVRGGRF VDVALGALNY QIEHHLFPNM
     PRANLRRARP IVQAYCAEQG IPYAETGLIE SYRQALAHLH EVGRPLRAG
//
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