ID E9SVF3_RHOHA Unreviewed; 542 AA.
AC E9SVF3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=FAD linked oxidase, C-terminal domain protein {ECO:0000313|EMBL:EGD26287.1};
GN ORFNames=HMPREF0724_10221 {ECO:0000313|EMBL:EGD26287.1};
OS Prescottella equi ATCC 33707.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Prescottella.
OX NCBI_TaxID=525370 {ECO:0000313|EMBL:EGD26287.1, ECO:0000313|Proteomes:UP000004245};
RN [1] {ECO:0000313|EMBL:EGD26287.1, ECO:0000313|Proteomes:UP000004245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33707 {ECO:0000313|EMBL:EGD26287.1,
RC ECO:0000313|Proteomes:UP000004245};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD26287.1}.
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DR EMBL; ADNW02000001; EGD26287.1; -; Genomic_DNA.
DR RefSeq; WP_005513729.1; NZ_CM001149.1.
DR AlphaFoldDB; E9SVF3; -.
DR STRING; 43767.A6I91_19920; -.
DR GeneID; 57577662; -.
DR HOGENOM; CLU_017779_2_0_11; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000004245; 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|PIRSR:PIRSR625650-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR625650-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000004245}.
FT DOMAIN 109..290
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 84..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 463
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 141..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 223..226
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 274..280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 325
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 542 AA; 55975 MW; 1F8C77B5C45826AF CRC64;
MSDAFVPESP TTPAPAMEWD AWGVAEFRRH LSPQVTALLQ QALGVSAEQS PPPEESDAIV
RESALGAPLV HALEDLLGVD NVRTDGPTRL RHAGGKSTPD LLRRKSTGEQ DAPDAVLLPG
THDEVLALLR FCAAEGIAVV PFGGGTSVVG GVDPVRGRFG SVVALDLRRL DALVDLDAVS
GVATLQAGVT GPQAEQLLGE HGFSLGHFPQ SFQFATIGGF AATRSSGQAS AGYGRFDDMV
EWLRVATPSG TLDLGRGPAS AAGPDLRELF VGSEGTLGII TEVGLRVHPV PERTAYQAWS
FPDFETGAAA LRAVAQSGSA PTVMRLSDEA ETGINLALSG DVGGDSPTSG CLAITTFEGT
DAHVDARYTE ATALLAAAGG TALGEAPAQA WEHGRFNAPY LRDALLNAGA IAETLETATR
WSNLTNLRSA VTTALTESLA AQGTPGIVMC HISHTYPTGA SLYFTVVCAQ AADPLAQWAA
AKRAAGDAIV AAGGTITHHH AVGVDHRPWM GSEVGDLGGR VLRAVKDAID PAGILNPGKL
IP
//
