ID S3NJG6_9GAMM Unreviewed; 388 AA.
AC S3NJG6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Stearoyl-CoA desaturase (Delta-9 desaturase) {ECO:0000313|EMBL:EPF79797.1};
GN ORFNames=F945_00685 {ECO:0000313|EMBL:EPF79797.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF79797.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF79797.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF79797.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EPF79797.1}.
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DR EMBL; ATGI01000006; EPF79797.1; -; Genomic_DNA.
DR RefSeq; WP_016655116.1; NZ_KE340351.1.
DR AlphaFoldDB; S3NJG6; -.
DR STRING; 632955.GCA_000829675_02914; -.
DR PATRIC; fig|421052.3.peg.675; -.
DR eggNOG; COG1398; Bacteria.
DR HOGENOM; CLU_027359_1_3_6; -.
DR OrthoDB; 19906at2; -.
DR Proteomes; UP000014568; Unassembled WGS sequence.
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:SF31; DESATURASE 1, ISOFORM A-RELATED; 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:UP000014568};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..263
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 388 AA; 44859 MW; A3FCD161FA47FB9B CRC64;
MNPPLPKAPI NWIAIFALVF LPVAALITIP VYAYYNDFSL AAWLSMFVLL GVSSLGITAG
YHRLWAHKAY EATLPLKIIL MIAGTFAVQN SILFWSSGHR THHRHVDDID KDPYSINNGF
WYAHMGWMLR NYPAAEPNFK NAPDLLNDKL VMFQHKYYVP LVIIIHVAIL GTVGWAVGDL
WGVVLLGGLV RLILSHHVTF FINSLCHMWG KRPYTDENTA RDNFWLAIAT WGEGYHNYHH
IFQYDYRNGV KWWQYDPTKW LIWSCSKVGL AKNLRRIPSF NIKKAELAMR FKYAEQDLAV
YGHDVNADLN AMKQKVAQEY EAFTHTLNDW AKLKEQELQV KKAAVAEKIH NMDLKLTVDF
QLVEQKLSFH RERLETLMRS IKKNAVSS
//
