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Database: UniProt
Entry: B2HHS2_MYCMM
LinkDB: B2HHS2_MYCMM
Original site: B2HHS2_MYCMM 
ID   B2HHS2_MYCMM            Unreviewed;       526 AA.
AC   B2HHS2;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Flavoprotein {ECO:0000313|EMBL:ACC41770.1};
GN   OrderedLocusNames=MMAR_3344 {ECO:0000313|EMBL:ACC41770.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41770.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC41770.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3};
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DR   EMBL; CP000854; ACC41770.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2HHS2; -.
DR   STRING; 216594.MMAR_3344; -.
DR   KEGG; mmi:MMAR_3344; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_2_0_11; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000001190; 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:UP000001190}.
FT   DOMAIN          93..274
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          347..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        447
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         207..210
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         258..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         386
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            309
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   526 AA;  55387 MW;  0A0F8923600F32F0 CRC64;
     MKWNAWGDPA AAKPLSDGIR ALLKQVVGLE DSGEAELGAD QVKLRPCALS QSDQDALAKI
     VGPEYMRTAD RDRLLRAGGK STPDMLRRKD TGIQDAPDAV LLPGDDQAVA EILRYCSDQG
     IAIVPFGGGT NVTGGLDPNR GQFSAVISLD LRRFNELHSL DEVSGIAELG AGVTGPDAER
     LLGERGFSLG HFPQSFEYAT IGGFAATRSS GQDSAGYGRF NDMIIGLRMI TPAGVLDLGR
     VAASAAGPDL RQLAIGSEGV FGVITKVRLR VHPVPETTRY EAWSFPDFST GVAALRAITQ
     TGTGPTVVRL SDEAETGINL ATHESIGENQ VTGGCLGLTL FEGTKEHTES RHAETRASLE
     AHGGKSLGEG PAQSWEHGRF SAPYLRDSLL AAGALCETLE TATDWSNIAA VKAAVTEALT
     TSLAESGTPA LVMCHVSHVY PTGASLYFTV VAGQRGNPIE QWMAAKKAAS DAMMATGATI
     THHHAVGADH RPWMRDEVGD LGVQLLRAVK ATLDPAGILN PGKLIP
//
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