ID   A0A0Q7JV72_9ACTN        Unreviewed;       524 AA.
AC   A0A0Q7JV72;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Alkyldihydroxyacetonephosphate synthase {ECO:0000313|EMBL:KQX62180.1};
GN   ORFNames=ASD06_15360 {ECO:0000313|EMBL:KQX62180.1};
OS   Angustibacter sp. Root456.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX   NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX62180.1, ECO:0000313|Proteomes:UP000051170};
RN   [1] {ECO:0000313|EMBL:KQX62180.1, ECO:0000313|Proteomes:UP000051170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root456 {ECO:0000313|EMBL:KQX62180.1,
RC   ECO:0000313|Proteomes:UP000051170};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX62180.1, ECO:0000313|Proteomes:UP000051170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root456 {ECO:0000313|EMBL:KQX62180.1,
RC   ECO:0000313|Proteomes:UP000051170};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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:KQX62180.1}.
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DR   EMBL; LMER01000020; KQX62180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7JV72; -.
DR   STRING; 1736539.ASD06_15360; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000051170; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
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   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR625650-3};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR625650-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051170}.
FT   DOMAIN          93..274
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        442
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         125..131
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         207..210
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         258..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            309
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   524 AA;  54160 MW;  4166F272A9E93A5D CRC64;
     MPFARWGAID HATPLTPQAR ALVRQALGIE HPPAAATTLR DVGLPRPQLP SGFLSDLREL
     LGPGGVATDD ASRALHARGR STSDLLRLRA GDLGDAPDAV LRPGTAEQVQ AALARCGAAR
     VAVVPFGGGT SVVGGLSARR DGFAGLVALD LRGLRRLVAL DTVSRTAELE AGLLGPEAEA
     LLAAEGFTLG HFPQSFEHAS IGGFAATRSS GQASAGYGRF DDLVVALRAA TPRGPLELGR
     APASAAGPDL RQLLLGSEGA FGVITSVTVR VRPAPQASRY EGWRFATFPD AVTAARALAQ
     DGPLPTVLRV SDEAETAIGL ATPESVGAEF GSGALLVAGY EGTAADVERR AADVATVLTT
     LGGTCLGPEP GEAWRRGRYA GGYLRDALLD EGALVETLET AAFWSQLPVL YDAVRGALAD
     ALGRSIVLCH LSHVYATGGS LYFTVAAPQT HDPLRQWDCA KRAASEAVLS SGGTISHHHG
     IGRDHRDDLP REIGDVGVGV LRAVKDYLDP DGVLNPGALV GEGT
//