ID B7P0R9_IXOSC Unreviewed; 624 AA.
AC B7P0R9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 08-NOV-2023, entry version 84.
DE RecName: Full=Alkylglycerone-phosphate synthase {ECO:0000256|ARBA:ARBA00012385, ECO:0000256|RuleBase:RU363113};
DE Short=Alkyl-DHAP synthase {ECO:0000256|RuleBase:RU363113};
DE EC=2.5.1.26 {ECO:0000256|ARBA:ARBA00012385, ECO:0000256|RuleBase:RU363113};
GN Name=8023161 {ECO:0000313|EnsemblMetazoa:ISCW016253-PA};
GN ORFNames=IscW_ISCW016253 {ECO:0000313|EMBL:EEC00199.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC00199.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC00199.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW016253-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW016253-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Catalyzes the exchange of an acyl for a long-chain alkyl
CC group and the formation of the ether bond in the biosynthesis of ether
CC phospholipids. {ECO:0000256|RuleBase:RU363113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol =
CC 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+);
CC Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26;
CC Evidence={ECO:0000256|RuleBase:RU363113};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR625650-3,
CC ECO:0000256|RuleBase:RU363113};
CC -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004670, ECO:0000256|RuleBase:RU363113}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU363113}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275,
CC ECO:0000256|RuleBase:RU363113}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000,
CC ECO:0000256|RuleBase:RU363113}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABJB010349922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010534028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB011010841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS612847; EEC00199.1; -; Genomic_DNA.
DR RefSeq; XP_002399350.1; XM_002399309.1.
DR AlphaFoldDB; B7P0R9; -.
DR STRING; 6945.B7P0R9; -.
DR PaxDb; 6945-B7P0R9; -.
DR EnsemblMetazoa; ISCW016253-RA; ISCW016253-PA; ISCW016253.
DR GeneID; 8023161; -.
DR KEGG; isc:IscW_ISCW016253; -.
DR VEuPathDB; VectorBase:ISCI016253; -.
DR VEuPathDB; VectorBase:ISCP_023135; -.
DR VEuPathDB; VectorBase:ISCW016253; -.
DR HOGENOM; CLU_017779_2_2_1; -.
DR InParanoid; B7P0R9; -.
DR OMA; GTISHQH; -.
DR OrthoDB; 2898095at2759; -.
DR UniPathway; UPA00781; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.160.650; -; 1.
DR Gene3D; 3.30.300.330; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.3450; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR46568; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR PANTHER; PTHR46568:SF1; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW FAD {ECO:0000256|PIRSR:PIRSR625650-3, ECO:0000256|RuleBase:RU363113};
KW Flavoprotein {ECO:0000256|RuleBase:RU363113};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU363113};
KW Lipid metabolism {ECO:0000256|RuleBase:RU363113};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|RuleBase:RU363113};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7P0R9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Transferase {ECO:0000256|RuleBase:RU363113, ECO:0000313|EMBL:EEC00199.1}.
FT DOMAIN 167..349
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 543
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 199..205
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 281..284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 333..339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 384
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 624 AA; 68827 MW; 7E7111A0EF9E8EBF CRC64;
MAATERLNTI KKHLQGSDPG DSGAGDGSNA TENGSCPAAS FSAQTTIPRR RQDLLKWNGW
GYKDSKFVVD GTTHHVSFTG DRYKIGNKTL PHFKSWVESA LGVDLSVLLP AKQPPSDQDL
PSPVVNEAFV DAVRRQGIVY SSDGQDRLFR AHGHTMREIF TLREGCFPRI PDLVVWPTCH
EDVVFLVSMA SQHNVVLIPF GGGTSVSGGL ECPSNEARMI VSLDTSQMNR ILWVDKMNLT
ANIEAGIIGQ DLERKLAEHG LCTGHEPDSY EFSSLGGWVA TRASGMKKSV YGNIEDLVVH
VRLVTPSGVL ERSCQVPRLS GGPDVHHFVL GSEGTLGVVT QVTIRVRPLP ECQRYGSIVF
PTFEPGVACL REVTRQQIRP ASIRLMDNTQ FIFGQALKPE ANSLLAPLWD GFKRFYVTRV
KGFEVDKMCV ATLLFEGSKQ EVDMQEKRVY EIAAKFGGLA AGEENGLRGY MLTFVIAYIR
DLGLDFSVVA ESFETSVPWD RVVDLCRNVK DVIVRECHSH GVSLPPLASC RVTQTYDAGA
CVYFYFAFNY TGVQDPVHVY EEIEAAAREE ILACGGSISH HHGVGKIRKR WLEQTISSTG
MQMLRAVKQS VDPQNIFANG NLML
//
