ID Q2L2K0_BORA1 Unreviewed; 402 AA.
AC Q2L2K0;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Stearoyl-CoA desaturase {ECO:0000313|EMBL:CAJ49025.1};
DE EC=1.14.19.1 {ECO:0000313|EMBL:CAJ49025.1};
GN OrderedLocusNames=BAV1416 {ECO:0000313|EMBL:CAJ49025.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49025.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ49025.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ49025.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AM167904; CAJ49025.1; -; Genomic_DNA.
DR RefSeq; WP_012417097.1; NC_010645.1.
DR AlphaFoldDB; Q2L2K0; -.
DR STRING; 360910.BAV1416; -.
DR GeneID; 41393299; -.
DR KEGG; bav:BAV1416; -.
DR eggNOG; COG1398; Bacteria.
DR HOGENOM; CLU_062181_0_0_4; -.
DR OrthoDB; 9768289at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004768; F:stearoyl-CoA 9-desaturase activity; IEA:UniProtKB-EC.
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 InterPro; IPR002560; Transposase_DDE.
DR PANTHER; PTHR11351; ACYL-COA DESATURASE; 1.
DR PANTHER; PTHR11351:SF33; DELTA-9 FATTY ACID DESATURASE, DESA; 1.
DR Pfam; PF01610; DDE_Tnp_ISL3; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAJ49025.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..219
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
FT DOMAIN 290..400
FT /note="Transposase IS204/IS1001/IS1096/IS1165 DDE"
FT /evidence="ECO:0000259|Pfam:PF01610"
SQ SEQUENCE 402 AA; 45745 MW; E860C2116F2A181D CRC64;
MDYILSFLSG GLTQASWWQI VAFTLIVTHI TIVAVTVFLH RSQAHRGLDL HPAVMHFFRF
WLWMTTGMVT KEWVAIHRKH HAKCEKEGDP HSPMLFGIWK VLFRGAELYR QESTNKETMA
KFGHGTPDDW LERNLYAKHS LWGVLTMLAI DVALFGAIGL TVWAVQMAWI PFWAAGVVNG
VGHYWGYRNY NSPDTSTNVF PWGFIIGGEE LHNNHHAHGT SAKFSAKWYE IDVGWGYITV
LRWLGLAKVK KVAPKLTLDP DAKAIDLRTL QGVITHRYEV MARYADVIKK AAGEELNKLK
ASRRKGSADC NWTLLNRVRR TLTRNEEVLQ PAQLAEVDQV IAKNASLSTL VQMRRELGRI
WESSSASSEQ LLQDLQAWCQ RAQQSGIAGL EQFALHLRRY AA
//
