ID A0A0M6YFL0_9RHOB Unreviewed; 346 AA.
AC A0A0M6YFL0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alkane 1-monooxygenase 2 {ECO:0000313|EMBL:CTQ48455.1};
DE EC=1.14.15.3 {ECO:0000313|EMBL:CTQ48455.1};
GN Name=alkB2_1 {ECO:0000313|EMBL:CTQ48455.1};
GN ORFNames=JDO7802_00457 {ECO:0000313|EMBL:CTQ48455.1};
OS Jannaschia donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=420998 {ECO:0000313|EMBL:CTQ48455.1, ECO:0000313|Proteomes:UP000049222};
RN [1] {ECO:0000313|EMBL:CTQ48455.1, ECO:0000313|Proteomes:UP000049222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7802 {ECO:0000313|EMBL:CTQ48455.1,
RC ECO:0000313|Proteomes:UP000049222};
RA Noorani M.;
RL Submitted (JUL-2015) 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; CXSU01000005; CTQ48455.1; -; Genomic_DNA.
DR RefSeq; WP_055082179.1; NZ_CXSU01000005.1.
DR AlphaFoldDB; A0A0M6YFL0; -.
DR STRING; 420998.JDO7802_00457; -.
DR OrthoDB; 4759734at2; -.
DR Proteomes; UP000049222; 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:CTQ48455.1};
KW Oxidoreductase {ECO:0000313|EMBL:CTQ48455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049222};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..308
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 346 AA; 38504 MW; C56C8B83E07B601D CRC64;
MLALAPYIAA LGLSVGLLVA GAVWDGLWDF ASLVWMAMVV ACLDHILPEH SDAPDEAGAK
ALTVGLALIH FPLLAVAVWT LAQGGPVWNW IAYFAAAGLY FGQIMNSCAH ELIHAGGRVR
RALGRWIYVT LLFGHQTTAH PGVHHIHVAT PEDPNTARYG EAWWVFCFRA WHGSFWKGLA
VEKQRQRRKG RHGWNRRNPY WVYLGGGWLA MALAFGTLGW AGLAAYVALC LLSHSQLLIT
DYVLHYGMRR TWMGERYEPV GPQHSWNAPH TVTNLLTLHA PRHSDHHAHP TRGFEALRIG
ADAPVLPYSL PVMVTLALWP HLWRRVMNPR VDALPRSQTS MDTAAA
//
