ID A0A1X6Z015_9RHOB Unreviewed; 382 AA.
AC A0A1X6Z015;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Alkane 1-monooxygenase 2 {ECO:0000313|EMBL:SLN36401.1};
DE EC=1.14.15.3 {ECO:0000313|EMBL:SLN36401.1};
GN Name=alkB2 {ECO:0000313|EMBL:SLN36401.1};
GN ORFNames=ROH8110_01862 {ECO:0000313|EMBL:SLN36401.1};
OS Roseovarius halotolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=505353 {ECO:0000313|EMBL:SLN36401.1, ECO:0000313|Proteomes:UP000193207};
RN [1] {ECO:0000313|EMBL:SLN36401.1, ECO:0000313|Proteomes:UP000193207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8110 {ECO:0000313|EMBL:SLN36401.1,
RC ECO:0000313|Proteomes:UP000193207};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFU01000002; SLN36401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6Z015; -.
DR OrthoDB; 4759734at2; -.
DR Proteomes; UP000193207; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0052869; F:arachidonic acid omega-hydroxylase activity; IEA:UniProtKB-EC.
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:SLN36401.1};
KW Oxidoreductase {ECO:0000313|EMBL:SLN36401.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193207};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 112..336
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 382 AA; 44259 MW; C5C2BE8B2AFA599A CRC64;
MIPSDQVAKF RNAAPFWMSL ILVPVAIFAA LYGGWTVILL PVVTWYLFSI LDAFLGLNLE
NADLETGEDQ LSWYKAITII WAPVQFALLF WMIWYVTGPG DAHLSPLETI VLFFGVGVIT
GTVGIVYSHE LMHQKDRGER FLGDALLSMV LYSHFRSEHL RVHHPYVGTS RDAVTARYNE
GFHRYFLRVL RESPISAFRS EKAMLARKGK HWSAPENPFW RYLGLQAFML LLALLVGGWT
GLLLFLWQAG AAIWQLELVN YVEHYALTRK HLGDGKYEHV KPHHSWNAAH KASNWLLINL
QRHSDHHYKP DRRFPLLQNY DESEAPQLPY GYPIMTMAAM IPPVWRRVMN PRVREWRKTY
YPEITDWAPY NKARLPMPRG SA
//
