ID C0ZQF5_RHOE4 Unreviewed; 539 AA.
AC C0ZQF5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Putative FAD-linked oxidase {ECO:0000313|EMBL:BAH35723.1};
GN OrderedLocusNames=RER_50150 {ECO:0000313|EMBL:BAH35723.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH35723.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH35723.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR EMBL; AP008957; BAH35723.1; -; Genomic_DNA.
DR AlphaFoldDB; C0ZQF5; -.
DR KEGG; rer:RER_50150; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_2_0_11; -.
DR Proteomes; UP000002204; 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 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; 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 106..287
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 460
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 138..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 220..223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 271..277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 322
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 539 AA; 56645 MW; 97AA0F6565069FE5 CRC64;
MSMSTEKSAL QPPMQWDAWG DPAKKRELSD AVTSLLTGFL GVSAPTRSRL AIEDVQVAPS
AMTQSHVEAL AGLVGAEYVS TKDSDRILRA GGKSTPDLLR RRSVEPQDAP DAVVTPGTDA
EVEQVLRYCS ANRIAVVPFG GGTSVVGGLD PIRDGFDAVL SLDLRRFDQL VGLDEESGIA
TFGGGTTGPR AEELLREHGF SVGHFPQSFL FATLGGFAAT RSSGQASAGY GRFEDMVQGL
TVVTPSGVVE TGRAPASAAG PDLGELFVGS EGTFGVITHV RVRVHRLPET TVREGWSFPD
FATGAAALRE LVQEGSAPTV LRLSDEAESG VNLATTDKIG ENAFTGGCLG ITTYEGTASH
TAERMAEARA ILTAHGGTSL GEEPGNSWEH GRFDAPYLRD ALLDVGALCE TLETATTWGN
LANLRSSVTE ALTKALVEQG TQPLVMCHIS HTYKTGASLY FTVVSAQTED PIAQWHKAKT
AAGDAIIAAG GTITHHHAVG ADHRPWMKDE IGELGANILR AVKNAVDPAG ILNPGKLIP
//
