ID A0A2S5AB19_9SPHI Unreviewed; 359 AA.
AC A0A2S5AB19;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Alkane 1-monooxygenase {ECO:0000313|EMBL:POY39293.1};
GN ORFNames=C3K47_02005 {ECO:0000313|EMBL:POY39293.1};
OS Solitalea longa.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=2079460 {ECO:0000313|EMBL:POY39293.1, ECO:0000313|Proteomes:UP000236893};
RN [1] {ECO:0000313|EMBL:POY39293.1, ECO:0000313|Proteomes:UP000236893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AV {ECO:0000313|EMBL:POY39293.1,
RC ECO:0000313|Proteomes:UP000236893};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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}.
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:POY39293.1}.
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DR EMBL; PQVF01000001; POY39293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5AB19; -.
DR OrthoDB; 4759734at2; -.
DR Proteomes; UP000236893; Unassembled WGS sequence.
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:POY39293.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000313|EMBL:POY39293.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236893};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 31..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..327
FT /note="Fatty acid desaturase"
FT /evidence="ECO:0000259|Pfam:PF00487"
SQ SEQUENCE 359 AA; 41662 MW; AB02322AFA7E915F CRC64;
MQMIRKLGYF CAFSLPLLLI AGYYLGNEWL FMLPVFVFFI VPLIDILLGT DTSNIAEPLL
PSAATEFYYL FLLYFWTLIQ SVLLIWACYE ATFENWNLLQ WIGMILGMGI ITGGIGITVA
HELGHKKSNV ERFLSKVLLS EVCYTQFYIE HNRGHHVHVG TPSDPATSRK NESFYRFWKR
SVFEGFSHAW KIENERLAKK GQPIFCFSNE MLGLTLAPLA LAAVFTLVFC LIRGDFVWEV
PVFFFAQSIF AFSLLEGVNY IEHYGLMRKE LAPNKYEKVN TLHSWNSSQL LSNFFLFQLQ
RHSDHHIFPA RRYQVLDHHD ESPQLPTGYP GMLLLAMIPP IWFKVMNKKL EEWEGRSAK
//
