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Database: UniProt
Entry: A0A0Q6W489_9BURK
LinkDB: A0A0Q6W489_9BURK
Original site: A0A0Q6W489_9BURK 
ID   A0A0Q6W489_9BURK        Unreviewed;       534 AA.
AC   A0A0Q6W489;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KQV79805.1};
GN   ORFNames=ASD15_17405 {ECO:0000313|EMBL:KQV79805.1};
OS   Massilia sp. Root351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV79805.1, ECO:0000313|Proteomes:UP000051876};
RN   [1] {ECO:0000313|EMBL:KQV79805.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV79805.1,
RC   ECO:0000313|Proteomes:UP000051876};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV79805.1, ECO:0000313|Proteomes:UP000051876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root351 {ECO:0000313|EMBL:KQV79805.1,
RC   ECO:0000313|Proteomes:UP000051876};
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:KQV79805.1}.
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DR   EMBL; LMDJ01000033; KQV79805.1; -; Genomic_DNA.
DR   RefSeq; WP_057157924.1; NZ_LMDJ01000033.1.
DR   AlphaFoldDB; A0A0Q6W489; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000051876; 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|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR625650-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR625650-
KW   3}; Reference proteome {ECO:0000313|Proteomes:UP000051876}.
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   534 AA;  57842 MW;  14E6679E78483F38 CRC64;
     MRRWNGWGDD AVNFALEADA LAFLAQRIGA GKGRQDATFE QACATLAPSR LPCHQLIDTS
     APVRLRNALG QSLPDWLKLR YGRIGTAPDG VAYPESPEQV RELLQYAQRY NVAVVPHGGG
     TSVAGHLTAG EGAQPTLAVN LTRLCRMAHL DRASQLATFG AGVYGPDLEA QLRAHGYTLG
     HFPQSFEYST LGGWVVTRSS GQQSLRYGRI EQMFAGGSLE TPVGRLEIPT FPASAAGTDL
     REIVLGSEGR IGILTEAVVR VSPLPEYEAF HAVFFADWTH AETAVRELAQ ARLGLSMLRL
     SNALETTTML ALAGHKRLIG LLEGWLSLRG CKEGKCMLML GASGAKPQAR AAISAALRMA
     RRHGGVHVGR KMGDKWKQNR FRNVYLRNAA WEHGYVIDTV ETAVDWPLVE PTMRAVEAAA
     AEALAGHGEQ VHAYTHLSHL YAQGASVYST FVYRLAGDYD EDLARWRSLK QAVSHAIVDC
     GGTISHQHGV GSDHAPYLAE EKGAAGIAAM QAIFRHFDPQ GIMNPGKLLP KAQT
//
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