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Database: UniProt
Entry: Q0RM07_FRAAA
LinkDB: Q0RM07_FRAAA
Original site: Q0RM07_FRAAA 
ID   Q0RM07_FRAAA            Unreviewed;       595 AA.
AC   Q0RM07;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   OrderedLocusNames=FRAAL2801 {ECO:0000313|EMBL:CAJ61445.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ61445.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ61445.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR   EMBL; CT573213; CAJ61445.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0RM07; -.
DR   STRING; 326424.FRAAL2801; -.
DR   KEGG; fal:FRAAL2801; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_2_0_11; -.
DR   Proteomes; UP000000657; 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:UP000000657}.
FT   DOMAIN          117..298
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        489
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         218..224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         231..234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         282..288
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         428
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            333
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   595 AA;  63116 MW;  170B7F61F559B651 CRC64;
     MSTESVRTPV VVEEPALVEH MKWWGWGRES VSFSHSDKPD LAPFVRTNIG LDITRPPAQP
     PAFADLTIPD PTLPEPLRAA LTAAVGAEHV HTDAHMRVVH AYGKSLRDLV RIRNADLGRL
     PDAVVYPDGE EAVRAVLAAA LDADAVVIPF GGGSNISGSL EAPRGETRPV ISVDLGRLDR
     VLEIDADARL ARIQAGALGP HLEEQLNAQG WTLGHFPDSF SHSTLGGWIA TRSSGMQSDK
     YGDIAEITRA VRVVTPAGVL ATRPVPSQST GPSVREMILG SEGRLGIITE ATVQVHRVPE
     ERVILGYFFP TWDDALVAMR EIAESEASPT VTRVSDANET RFSFATRRKG SLASGLVSAG
     LKQYLRRVRN YDLEQMCLSF IGFEGTPAHV KAQRKLVGEI VGRHGGLCVG TGPGQLYDQK
     KFDTPYIRDF LLGQGAVADV SETSASWSQL GPLYRGVVAR ANKAFAEIGV DGWIMCHLSH
     SYHSGACLYF TFAYSSPVTL EAIEGYDTVK SAIQQGFLDL AGTLSHHHAV GVEHAPWLGD
     DISPAGVRLL TALFDGIDPG HNLNPGKIIP GAGAGAGAGA GAGAGAGAGG GPVGE
//
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