ID J2XUB8_9PSED Unreviewed; 531 AA.
AC J2XUB8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:EJN28270.1};
GN ORFNames=PMI37_03690 {ECO:0000313|EMBL:EJN28270.1};
OS Pseudomonas sp. GM80.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144339 {ECO:0000313|EMBL:EJN28270.1, ECO:0000313|Proteomes:UP000007301};
RN [1] {ECO:0000313|EMBL:EJN28270.1, ECO:0000313|Proteomes:UP000007301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM80 {ECO:0000313|EMBL:EJN28270.1,
RC ECO:0000313|Proteomes:UP000007301};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJN28270.1}.
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DR EMBL; AKJD01000109; EJN28270.1; -; Genomic_DNA.
DR RefSeq; WP_008083406.1; NZ_AKJD01000109.1.
DR AlphaFoldDB; J2XUB8; -.
DR PATRIC; fig|1144339.3.peg.3530; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000007301; 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}.
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 248..254
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 531 AA; 58081 MW; 63FD1D41B3DDE57A CRC64;
MRRWNGWGDA TTVVELPAQG AEFLHERLGE GRALPDATLE AALARVPASR LSAHTLYSID
AHDRMLHARG QSLPDWLALR EGALGNYPDA VAFPETAEHI RQLLALAHEQ DLCLIPYGGG
TSVAGHINPP DSARPVVTVS LARMNRLIDL DEQSLLATFG PGASGPQVES QLRARGYTLG
HFPQSWELST LGGWVASRSS GQQSLRYGRI EQLFAGGTLE TFAGPLEIPT FPASAAGPDL
REVVLGCEGR FGIISEVKVR VSALPADERF YGVFLPSWTK ALQAIRQLAQ ARVPLSMLRL
SNAVETETQL ALAGHPQQIA WLEKYLKLRG AAEGKCLLTF GVTGNRRQNA LSLTQARQHL
KAFGGVFTGT LLGKKWAQNR FRFPYLRENL WNAGYVVDTL ETATDWSNVD NLLNLIENSL
REALAAEGER VHVFTHLSHV YGEGSSIYTT YVFRPAADYP ATLARWKALK HAASQTIVDN
HGTISHQHGV GKDHAPYLLR EKGALAMDTL QALSKYFDPA GRLNPGTLLP E
//
