ID K0SMF7_THAOC Unreviewed; 2387 AA.
AC K0SMF7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=alkylglycerone-phosphate synthase {ECO:0000256|ARBA:ARBA00012385};
DE EC=2.5.1.26 {ECO:0000256|ARBA:ARBA00012385};
DE AltName: Full=Alkylglycerone-phosphate synthase {ECO:0000256|ARBA:ARBA00031574};
GN ORFNames=THAOC_12956 {ECO:0000313|EMBL:EJK66139.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK66139.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK66139.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK66139.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
CC -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004670}.
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:EJK66139.1}.
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DR EMBL; AGNL01015242; EJK66139.1; -; Genomic_DNA.
DR EnsemblProtists; EJK66139; EJK66139; THAOC_12956.
DR eggNOG; KOG1221; Eukaryota.
DR eggNOG; KOG1233; Eukaryota.
DR eggNOG; KOG3730; Eukaryota.
DR OMA; FSKCVCE; -.
DR UniPathway; UPA00781; -.
DR Proteomes; UP000266841; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.80.10; -; 1.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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; PF00887; ACBP; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|PIRSR:PIRSR625650-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR625650-3};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 699..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 732..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..103
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT DOMAIN 1884..2073
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 119..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2358..2387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2266
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 1987..1993
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 2000..2003
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 2057..2063
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 2203
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 2108
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 2387 AA; 265106 MW; 888BEB3E2999888B CRC64;
MEVEQRQRLE NCFERVAALV RHASSPTDDP PSDTLRLNLY GYFKLSTSSV PSSGVPRPSF
FDPVGRAKHA AWKAAEDECQ FDRALSMERY IQAVIGSGTD VGREAGALWG EYLRRLGEQE
PDESHTPPTH AAKAGDDDDD KSSAVAGEDS DETGESLTRI PASRKTFDRM LASEQLEQGQ
SASRHRGSQR KLLSLLPRPL VPRGQLDIAL RDLLYAHMQC ALSVTYEFFL SDRGMLHRIL
SFFLPSFILQ MIGVFCARYH PERRRAWSVR KINERWREME RRSSSREGVK SAEKDVVVGL
SVRSLLDLYL SSKSYPAGSE ILLVPPVTIP AIVNIIEYHD LRLVGIDLPR IGGETRWGVD
VEALRQAVSD KTVALMLVHP FGCRIADLGT MRDLRKIANG HSLDIIEDCA QSYTGICTSK
KGHIQLGYLG SEEADVSLFS FGPIKTSTAL GGGLAVLRRR KGVAKSMRRM QESLYQPQRT
TSYYVRLLKC TFVQLASQST YCCGFIKILL DSVGIEYSWL VMKLTRGFDC RGGQQEVIRQ
IRRRPCPALL ALLNRRLQQS HLVYEEADKR RRRCESFSKV LARSEMSNLS TLKSVDGGDM
YNWIFPVFTS RPVHTSRSLI SMGFDAPCGM TQLRPLENCV RAKEVFDHIM YLPVTSQKCS
ESSRRKLVSV LQDACSDIAT EKSTAQKRSA TWKAKSKTML FILAILLERA VSVVGLFQFA
TVRLAIRVAK VILPWIFMSV AFVACSLLAL SRYMGPIYLS SSRTFAKYCD MVFRSPFDCE
VSRPEHKAFE RSQTVLSLDS TRIPTVLRSE DGGEPCVMLT GVTGFIGSLL LREILLHRDE
LSIGSAVVIV RPKRGRSAIQ RVERLLSQAM FSFLSEDEKK SLVIVVEGDV TQPYCGITPA
VIESSIQVSK ISHVLHCAAA VSFSQPLEDA ATSNITSSLN VQSLAKQLDA KFTYLSTAFV
HGDRTGTKSR PLPEAVFSLK PYDPDKLYES MLGSQSYASA AMNDLGFPNT YTFSKCVCEH
LLEMERDVET TIIRPSIVGP SVEEPYEGWA GERPSTIVAA ACLYLKFPYN MWCFGHKPVP
FVPVDVVCRV IISKSFGSDL MSEADVASYF RGQEEEKKEQ SPIDTGYRDS TRKSPAISTV
AWDSSSPERS TFSWVQYAFA ITHLGSVCGH VDRTVAYAGL LLSTKLFPWL GLSLATFRQL
HAILVRTPVD KVLEICKRLR LRSAFVRDLD ALSPVLDLPM LFFPFANRSF YFQSQIRAPD
DFNGERYMFS CAVAAHRFIE RIENQRKRSK HGRLEDGSSH PQRNCRNASI YVAGKCHAMP
ASDLWWALTQ PTGSLTIRFG AWVLSKIFRR TAREIGVDVA SYAVLARTLA STDAASVILA
PTHRSFYDFL ITSYISFALP ELGVGIPHIA AASDFQHVPI IGILAAWSNA FFLRRDGKGR
DTTLQQDLSR IISRSSPAFI EVFIEGKRSR SRAFLKPKTG FLRCLCENIE GSHLVLPSTI
NYEGLVDQMT LVEETSRVAK RGMGLFRLSQ WLRAVILNKV DIGRVYISAS PPIIVGAGTL
DVRGLGNAIQ ERQRSRTLVS EYHVEAASSV LGVPSHVIRE SMQDLGMIPW PPRGATEPLL
AIPSCQNVAW TTFFHFAHIY APYLAQTHQT WSEWLCPSSS KPKKSESSSV NVVVSILTQH
LEAADNEVVT VLKYLAANGF DSPTESHVFQ YLSDVKSPAM LLLLALKTKM VNRAGTIPLR
NMPRLEDPHL FRRQKVLKNN VPLENFAAWG FQDSYFVLNE SSDGAKIVTM KGSRYDISGK
QLPNLARFVE EELRITIDPM KAPKTCCDFV SVRRDAFDEG LATGILAVLG NDKDRFSTRA
VDRARHGTGH TQQDIFDLRF GNIRSRVPDA VVWPKSILEV EALVSFAVEE SLCLIPFGGG
TNVTHATHCP PREVDPRPMV SIDMKLMNGI LWVNEEDGLV HVEAGITGGE LIRRVEKLGF
TIGHIPDSYE FSTLGGWIAT KASGMKQNKY GNIEDIVKDV TVVGSKGILS TSHRISKTTA
GRSSAGLEPK SLALGSEGCF GIITSAVLKI SPIPEVKSYQ SVLLPSFGVG VEYMRALSKM
TMKPASVRLL DNDQFRLGQA LKERPSLFGT LREWLAHAIS SAGGNFSLNT VVCVTISFEG
SAAEVNLQQR LVRDFATVYE GMLAGPSVGK AGYDLTFAIA YLRDFALNYD IIGESFETFV
PWSCIKRLVA ATKDRVQFEH RHRALPGEPF ICSRITQLYD EGVCVYFYFC MQIKGVSNPS
VVFSEIEHIA REEILSNGGS LSHHHGLGKV RSSFVSQIYS QAYIDTLTAI KNSIDERNVF
GAANGIFGSK MYSSSIEHTN VSGKGPKNAR EGSRCGFTAA TGTTKTA
//
