ID A0A1J0WFA7_9RHOB Unreviewed; 336 AA.
AC A0A1J0WFA7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Alkane 1-monooxygenase {ECO:0000313|EMBL:APE43004.1};
GN ORFNames=BOO69_05895 {ECO:0000313|EMBL:APE43004.1};
OS Sulfitobacter alexandrii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE43004.1, ECO:0000313|Proteomes:UP000181897};
RN [1] {ECO:0000313|EMBL:APE43004.1, ECO:0000313|Proteomes:UP000181897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM1-D1 {ECO:0000313|EMBL:APE43004.1,
RC ECO:0000313|Proteomes:UP000181897};
RA Yang Q., Zhang X., Tian X.;
RT "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT associated with marine dinoflagellate Alexandrium minutum in East China
RT Sea.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. AlkB
CC subfamily. {ECO:0000256|ARBA:ARBA00010823}.
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DR EMBL; CP018076; APE43004.1; -; Genomic_DNA.
DR RefSeq; WP_071971178.1; NZ_CP018076.1.
DR AlphaFoldDB; A0A1J0WFA7; -.
DR STRING; 1917485.BOO69_05895; -.
DR KEGG; suam:BOO69_05895; -.
DR OrthoDB; 4759734at2; -.
DR Proteomes; UP000181897; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd03512; Alkane-hydroxylase; 1.
DR InterPro; IPR033885; AlkB/XylM.
DR InterPro; IPR005804; FA_desaturase_dom.
DR PANTHER; PTHR38674; ALKANE 1-MONOOXYGENASE 1; 1.
DR PANTHER; PTHR38674:SF1; ALKANE 1-MONOOXYGENASE 1; 1.
DR Pfam; PF00487; FA_desaturase; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:APE43004.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000313|EMBL:APE43004.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..294
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 336 AA; 36854 MW; EB66C86F4993F73F CRC64;
MMWYAFASLL PAGLLTFACL FGGAWPVVSV LSITVFVFFM DKLPRSAQVS PATGRSLSLL
LAAVHFPLLA LGVWALGAGA HLDLVDRLLI FAGLGLFFGQ VSNSNAHELI HARSRLPRRI
GAAIYVSLLH GHHVSAHLRV HHVHAATDAD PNSAPLGMGF WRYCGHVLKG EFLAGLRAEN
RHRNRAVPPP ALWRHPYLYY VGGGAVALAC AFALAGLPGV AAHVGIALYA QWQLLLSDYV
QHYGLRRRLD TGKPEPVGPQ HSWNAPKWYS SAMMLNAPRH SDHHMRPSRA FPALEVTPDT
MPVLPHSLPV MAVVALVPPV WRRVMDRRAA RWQDVA
//
