ID A0A1B1MB68_STRLN Unreviewed; 336 AA.
AC A0A1B1MB68;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acyl-CoA desaturase {ECO:0000313|EMBL:QMV08833.1};
DE SubName: Full=Fatty acid desaturase (Membrane) {ECO:0000313|EMBL:ANS65774.1};
GN ORFNames=GJU35_26445 {ECO:0000313|EMBL:QMV08833.1}, SLCG_3308
GN {ECO:0000313|EMBL:AXG54463.1}, SLINC_3550
GN {ECO:0000313|EMBL:ANS65774.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS65774.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS65774.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS65774.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG54463.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG54463.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV08833.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV08833.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP016438; ANS65774.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG54463.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV08833.1; -; Genomic_DNA.
DR RefSeq; WP_067434112.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1MB68; -.
DR STRING; 1915.SLINC_3550; -.
DR KEGG; sls:SLINC_3550; -.
DR PATRIC; fig|1915.4.peg.3893; -.
DR OrthoDB; 19906at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd03505; Delta9-FADS-like; 1.
DR InterPro; IPR015876; Acyl-CoA_DS.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF3; STEAROYL-COA 9-DESATURASE; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR PRINTS; PR00075; FACDDSATRASE.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..277
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 336 AA; 38092 MW; F0C9A8BECDCCC20E CRC64;
MTSSSDVIED PSQAAVDADV PSATLGGEQK RSIEQITLLL FIIVPFLAVL AALPLAWGWG
VSWLDLGLLV FFYFLGCHGI TIGFHRYFTH GSFKAKRPLR IALAIMGSMA VEGPLVRWVA
DHRKHHKFSD AEGDPHSPWR FGETIPALMK GLWWAHIGWM FDEEQTPQDK YAPDLIKDRA
IRTISRQFIF WAMLSLALPA LIGGLVTMSW WGAFTGFFWG SLVRVCLLHH VTWSINSICH
AVGRRPFKSR DRSGNVWWLA VLSCGESWHN LHHADPTSAR HGVERGQVDS SARFIRWFEM
LGWAYDVRWP SRSRIDSRRI TGEDGSRRKK ETAEAA
//
