ID B7UHI4_ECO27 Unreviewed; 484 AA.
AC B7UHI4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Predicted FAD containing dehydrogenase {ECO:0000313|EMBL:CAS10583.1};
GN Name=ygcU {ECO:0000313|EMBL:CAS10583.1};
GN OrderedLocusNames=E2348C_3035 {ECO:0000313|EMBL:CAS10583.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS10583.1, ECO:0000313|Proteomes:UP000008205};
RN [1] {ECO:0000313|EMBL:CAS10583.1, ECO:0000313|Proteomes:UP000008205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX PubMed=18952797; DOI=10.1128/JB.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR EMBL; FM180568; CAS10583.1; -; Genomic_DNA.
DR RefSeq; WP_000059425.1; NC_011601.1.
DR AlphaFoldDB; B7UHI4; -.
DR KEGG; ecg:E2348C_3035; -.
DR HOGENOM; CLU_017779_2_3_6; -.
DR Proteomes; UP000008205; 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 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:UP000008205}.
FT DOMAIN 47..226
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 398
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 210..216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 262
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 484 AA; 53700 MW; 4EDDEBF40DED518B CRC64;
MSLSRVAIVD QLKEIVGADR VITDETVLKK NSIDRFRKFP DIHGIYTLPI PAAVVKLGST
EQVSRVLNFM NAHKINGVPR TGASATEGGL ETVVENSVVL DGSAMNQIIN IDIENMQATA
QCGVPLEVLE NALREKGYTT GHSPQSKPLA QMGGLVATRS IGQFSTLYGA IEDMVVGLEA
VLADGTVTRI KNVPRRAAGP DIRHIIIGNE GALCYITEVT VKIFKFTPEN NLFYGYVLED
MKTGFNILRE IMVEGYRPSI ARLYDAEDGT QHFTHFADGK CVLIFMAEGN PRIAKATGEG
IAEIVACYPQ CQRVDSKLIE TWFNNLNWGP DKVAAERVQI LKTGNMGFTT EVSGCWSCIH
EIYESVINRI RTEFPHADDI TMLGGHSSHS YQNGTNMYFV YDYNVVDCKP EEEIDKYHNP
LNKIICEETI RLGGSMVHHH GIGKHRVHWS KLEHGSAWTL LEGLKKQFDP NGIMNTGTIY
PIEK
//
