ID   F8C8E8_MYXFH            Unreviewed;       618 AA.
AC   F8C8E8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Oxidase, FAD binding protein {ECO:0000313|EMBL:AEI61994.1};
GN   OrderedLocusNames=LILAB_00290 {ECO:0000313|EMBL:AEI61994.1};
OS   Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI61994.1, ECO:0000313|Proteomes:UP000000488};
RN   [1] {ECO:0000313|EMBL:AEI61994.1, ECO:0000313|Proteomes:UP000000488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX   PubMed=21868801; DOI=10.1128/JB.05516-11;
RA   Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT   "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT   1.";
RL   J. Bacteriol. 193:5015-5016(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002830; AEI61994.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8C8E8; -.
DR   STRING; 483219.LILAB_00290; -.
DR   KEGG; mfu:LILAB_00290; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_2_2_7; -.
DR   UniPathway; UPA00781; -.
DR   Proteomes; UP000000488; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008611; P:ether lipid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 3.30.43.10; 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}.
FT   DOMAIN          148..330
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        524
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         249..255
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         262..265
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         314..320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            365
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   618 AA;  67735 MW;  FFE16C923DED83D6 CRC64;
     MALTEVSERF GGSPSTPASG DTRFTPPAAP ASKDEESLEG WGFADTRFVV KPDGNTVLTG
     TRYNISNVEL PELMPWFAGK LASPLGYDNR NEPHYPPEIP AAKQDAKLVA ALREFLKEEQ
     LTDDPKQRLR RGHGHTGGEI WAIRYRKLDR VPDLVVFPRG HDEVVRLVEV ATKHGACVIP
     FGGGTNVTEA LRIPLAEERF VIAVDMRQMN RILWVDPVNR MACIEAGATG RHLMEALAKF
     GFTMGHEPDS LEFSTLGGWI ATNASGMKKN RYGNIEDLVL DMQVVTAQGI VERPRQAPRE
     SVGVNPRQYM FGSEGNFGIV TTAVVKLFPL PEVQRYGSVI FPDLETGLSF LYALQQSGAV
     PASVRVMDNT QFHFGQALKP AKHGLAAKLK SEVEKAVVTK LKGFDPYKLA VATLVFEGSS
     EEVAFQEKTV YRIAAEHGGM KGGGANGERG YQLTFGIAYI RDLTFEHWAI AESFETSVPW
     SRAMDLYERV QRRVEKEHAA MGLPGKVFFT GRFTQVYQTG VVIYFYLGFY AKGVADPVAA
     YAALEHAARE EILAAGGSLS HHHGIGKIRR GFLPEVYSEG ALALNRKVKA AIDPDNVFGA
     SNSGINGPVA LTPDEEAH
//