ID A0A0M2WHN1_9BURK Unreviewed; 536 AA.
AC A0A0M2WHN1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Putative FAD-linked oxidoreductase {ECO:0000313|EMBL:KKO62732.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KKO62732.1};
GN ORFNames=VM94_03736 {ECO:0000313|EMBL:KKO62732.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO62732.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO62732.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO62732.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-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:KKO62732.1}.
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DR EMBL; LBCO01000029; KKO62732.1; -; Genomic_DNA.
DR RefSeq; WP_046684838.1; NZ_VCCE02000001.1.
DR AlphaFoldDB; A0A0M2WHN1; -.
DR PATRIC; fig|1649647.5.peg.3825; -.
DR Proteomes; UP000034315; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR625650-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR625650-
KW 3}; Oxidoreductase {ECO:0000313|EMBL:KKO62732.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034315}.
FT DOMAIN 84..264
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 448
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 116..122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 197..200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 387
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 299
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 536 AA; 57305 MW; 4EF68CB7D4C82916 CRC64;
MQRWNGWGDE SITYALSGDA LAFLRERLGP GSGIVDATFD DACARVPASR LAPHPLIDTQ
PATRVRHALG QSLPDWFKLR HGRIGAVPDG VAFPDSALQV RQLLAYARQA CVAVIPHGGG
TSVAGHLTVA AGPRPVLSVS LARLCALGHL DREAQLATFG AGVYGPDLEA QLRAQGYTLG
HYPQSFEYST LGGWIATRSS GQQSLRYGRI EQLFAGGEVE TPAGTLRIPT FPASAAGIDL
REMVLGSEGR LGILTQATVR VSPLPPYEAF HAVFFADWGQ AQTAVRALAQ SRLPLCMLRL
SNAVETQTML TLAGHKKLVG LLERYLSLRG CGDGKCMLML GVSGEAGPAR AALRGALALA
RRHGGVHVGR HMGDKWKQGR FRNVYLRNGA WEHGYVIDTV ETAVDWPRVA PMMAALEQAG
ANALAAHGEQ VHAYTHLSHV YAQGASVYTT YVYRLASTFE ENMARWRSLK NAASAAIVAN
GGTISHQHGV GTDHAPWLAA EKGELGIAAM RALLRQFDPQ GMMNPGKLLP DAGSGL
//
