ID   ALKMO_CAEEL             Reviewed;         505 AA.
AC   O17554;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Alkylglycerol monooxygenase {ECO:0000312|WormBase:BE10.2};
DE            EC=1.14.16.5 {ECO:0000250|UniProtKB:Q6ZNB7};
DE   AltName: Full=Transmembrane protein 195 homolog;
GN   Name=agmo-1 {ECO:0000312|WormBase:BE10.2};
GN   ORFNames=BE10.2 {ECO:0000312|WormBase:BE10.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Glyceryl-ether monooxygenase that cleaves the O-alkyl bond of
CC       ether lipids. {ECO:0000250|UniProtKB:Q6ZNB7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 1-O-(1,2-
CC         saturated-alkyl)-sn-glycerol + O2 = (6R)-L-erythro-6,7-
CC         dihydrobiopterin + a 1-(1-hydroxyalkyl)-sn-glycerol + H2O;
CC         Xref=Rhea:RHEA:36255, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:43120, ChEBI:CHEBI:59560, ChEBI:CHEBI:73418,
CC         ChEBI:CHEBI:83957; EC=1.14.16.5;
CC         Evidence={ECO:0000250|UniProtKB:Q6ZNB7};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q6ZNB7};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q6ZNB7}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q6ZNB7}.
CC   -!- SIMILARITY: Belongs to the sterol desaturase family. TMEM195 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z93372; CAB07547.2; -; Genomic_DNA.
DR   PIR; T18789; T18789.
DR   RefSeq; NP_499664.2; NM_067263.5.
DR   AlphaFoldDB; O17554; -.
DR   STRING; 6239.BE10.2; -.
DR   EPD; O17554; -.
DR   PaxDb; O17554; -.
DR   PRIDE; O17554; -.
DR   EnsemblMetazoa; BE10.2.1; BE10.2.1; WBGene00007210.
DR   EnsemblMetazoa; BE10.2.2; BE10.2.2; WBGene00007210.
DR   GeneID; 176695; -.
DR   KEGG; cel:CELE_BE10.2; -.
DR   UCSC; BE10.2; c. elegans.
DR   CTD; 176695; -.
DR   WormBase; BE10.2; CE30592; WBGene00007210; agmo-1.
DR   eggNOG; KOG0872; Eukaryota.
DR   GeneTree; ENSGT00440000033807; -.
DR   HOGENOM; CLU_033631_2_1_1; -.
DR   InParanoid; O17554; -.
DR   OMA; FMPTGWR; -.
DR   OrthoDB; 1446475at2759; -.
DR   PhylomeDB; O17554; -.
DR   Reactome; R-CEL-75109; Triglyceride biosynthesis.
DR   PRO; PR:O17554; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00007210; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050479; F:glyceryl-ether monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0006643; P:membrane lipid metabolic process; IBA:GO_Central.
DR   InterPro; IPR006694; Fatty_acid_hydroxylase.
DR   Pfam; PF04116; FA_hydroxylase; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Iron; Membrane; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..505
FT                   /note="Alkylglycerol monooxygenase"
FT                   /id="PRO_0000299305"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          130..262
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           145..149
FT                   /note="Histidine box-1"
FT   MOTIF           158..162
FT                   /note="Histidine box-2"
FT   MOTIF           234..238
FT                   /note="Histidine box-3"
SQ   SEQUENCE   505 AA;  58491 MW;  22C40C34FBA42820 CRC64;
     MNETAWLDRV FSNTSLGHRL LDRLTLTNLR HAFYLISPYE TTVESIDDVP NYNAEVSAWW
     LVFLTAEFFI LFISGHEDRF ALNDSITSIC AGMLSQCFKF GGRAVAIFLY VIVWDNWRIL
     ELPWDSPWTW IFCLFFQDFM YYLGHRAVHE AGFFWGLHTI HHSSEYYNFS TALRQAAIQD
     AGLAIYDCIQ AFFIPPSIFL VHRYFSEIFQ FIMHTSLVDT MGPLGLVFNT PSHHRVHHGR
     NPYCIDKNYG GVFIIWDKMF NTFEAERHDD PPIYGLVTNE NTFNQIYLQF HALWDILIFK
     GFTKDVKGEP MFPGVVNKLK ATVFPPGWFP GVPVTPFFHW MSMVNPAHGV PEPEKPVLRY
     SPPARILVKV YVASSFLLLL AIFFHFEYDR NHLSYLDCTV KIAYFVVTMQ CFGAFFDMKW
     YARYIEIARC CGVLIYYGVL MFDHIGAGTH RLFVISLHIM AIALWTTDVL VEKLSQCCSK
     NQSINPEKGD LERAPEIASI SKNVQ