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Database: UniProt
Entry: A0A0M2JY89_9MYCO
LinkDB: A0A0M2JY89_9MYCO
Original site: A0A0M2JY89_9MYCO 
ID   A0A0M2JY89_9MYCO        Unreviewed;       538 AA.
AC   A0A0M2JY89;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Flavoprotein {ECO:0000313|EMBL:KKF01603.1};
GN   ORFNames=WN67_12845 {ECO:0000313|EMBL:KKF01603.1};
OS   Mycolicibacterium obuense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF01603.1, ECO:0000313|Proteomes:UP000034150};
RN   [1] {ECO:0000313|EMBL:KKF01603.1, ECO:0000313|Proteomes:UP000034150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|EMBL:KKF01603.1,
RC   ECO:0000313|Proteomes:UP000034150};
RA   Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium obuense UC1.";
RL   Submitted (APR-2015) 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:KKF01603.1}.
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DR   EMBL; LAUZ02000046; KKF01603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2JY89; -.
DR   STRING; 1807.MOBUDSM44075_03476; -.
DR   PATRIC; fig|1807.13.peg.3797; -.
DR   Proteomes; UP000034150; Unassembled WGS sequence.
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}.
FT   DOMAIN          105..286
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        459
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         137..143
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         219..222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         270..276
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            321
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   538 AA;  56335 MW;  AF20D0471B348F77 CRC64;
     MSSLAGQPTR PPMAWNAWGD PAAAKPLSPG IRSLLSQALG IDAEPTAEPT LEEVRVRPSA
     LSPSDREGLA AIVGAENVLV EDRDRLLRAG GKSTLDLLRR RDFGVQDGPD AVLVPGDDDE
     VAAVLRFCAD HSIAVVPFGG GTSVVGGLDP LRGDFKAVVS VDLRRFDELH TLDDVSWEAE
     LGAGLTGPEA EQLLNERGFS LGHFPQSFCF ATIGGFAATR SSGQDSSGYG RFDDMVHGLR
     AVTPAGVFDA GRAPASAAGP DLRQLLLGSE GTFGVITKVR VRVHPVPETT RYEAWSFPDF
     ATGAAALRAV AQTGAGPTVI RLSDEAETGV NLATADSIGE TQITGGCLAI TAFEGTEAHV
     VSRHAETRDL LSGNGGTSLG EGPARAWEHG RFNAPYLRDG LLSAGALCET LETATSWSNV
     PTLKAAVTDA LTRSLADSGT PALVMCHISH VYPTGASLYF TVVAAQRGNP IEQWRAAKTA
     ASEAMVRVGA TITHHHAVGA DHRPWMRDEV GDLGVAVLRA VKSTLDPTGI MNPGKLIP
//
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