ID A6W6Q0_KINRD Unreviewed; 554 AA.
AC A6W6Q0;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ABS02489.1};
GN OrderedLocusNames=Krad_1001 {ECO:0000313|EMBL:ABS02489.1};
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS02489.1, ECO:0000313|Proteomes:UP000001116};
RN [1] {ECO:0000313|Proteomes:UP000001116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC {ECO:0000313|Proteomes:UP000001116};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA Fliermans C., Richardson P.;
RT "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR EMBL; CP000750; ABS02489.1; -; Genomic_DNA.
DR AlphaFoldDB; A6W6Q0; -.
DR STRING; 266940.Krad_1001; -.
DR KEGG; kra:Krad_1001; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_2_0_11; -.
DR Proteomes; UP000001116; Chromosome.
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 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:UP000001116}.
FT DOMAIN 101..282
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 473
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 202..208
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 215..218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 266..272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 317
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 554 AA; 59804 MW; B7A2F1E375CD1B41 CRC64;
MVEHMKWWGW GQEGVAFHHE DKPNLAPFVK RVSGIDFDAP PAQVPELSEL EVPASRASQE
LREALVAALG AEHVHDDDHD RVVHTYGKSM RDLVRVRRGD FGRVPDLILY PGTEAEVEAV
LRIALDADAV LIPFGGGSNI VGSLEAPREE TRPVLSLDVG RMRAVLSLDE TAQTARIQAG
ALGPDLEAQL NARGWTIGHF PDSFKHSTLG GWIATRSSGM QSDRFGDIAD ITRAVRVVTP
KGLVATSEVP VQSVGPSVRE MVLGSEGRLG IITEATVQVH RVAEERVIQA YFFPDYASGL
KAMHDIAASD ASPSITRVSD ANETQFTLAT SKKGSPLGQL LNKGVQLYAS KRKGFDLSEM
CLSFIGFEGS SLGVRRNKAL VAEIVKKHGG FGVGSGPGTL YDQKKFDTPY IRDFILDRGA
YGDVSETSSS WTTLKSLHDN VVAAAGKAFA EVGVKGFVFC HLSHSYHSGA CQYFTFAFQP
PTDRDGLEAY DVVKGAIQQA FIDNGGTLSH HHAVGREHKR WVSEDLSPAG AEIVSTLFAG
VDPGRNLNPG AIVD
//
