ID M2B9G3_TREDN Unreviewed; 584 AA.
AC M2B9G3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=HMPREF9733_00580 {ECO:0000313|EMBL:EMB25980.1};
OS Treponema denticola SP33.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=999437 {ECO:0000313|EMBL:EMB25980.1, ECO:0000313|Proteomes:UP000016183};
RN [1] {ECO:0000313|EMBL:EMB25980.1, ECO:0000313|Proteomes:UP000016183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP33 {ECO:0000313|EMBL:EMB25980.1,
RC ECO:0000313|Proteomes:UP000016183};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Fenno C.J.,
RA Baranova O.V., Mathney J., Dewhirst F.E., Izard J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Treponema denticola SP33.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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:EMB25980.1}.
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DR EMBL; AGDZ01000017; EMB25980.1; -; Genomic_DNA.
DR RefSeq; WP_010693801.1; NZ_KB442453.1.
DR AlphaFoldDB; M2B9G3; -.
DR PATRIC; fig|999437.3.peg.583; -.
DR HOGENOM; CLU_017779_2_0_12; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000016183; 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;
FT DOMAIN 121..307
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 560..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 487
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 431
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 344
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 584 AA; 66392 MW; EBAAF6073EB752A1 CRC64;
MGKRYEYKDF KPVWEQVPPP KDSFREAAKW GDPNEFKEPN ERLYKYMKTV FGIGDEIFKQ
KRFEGLEALP KNLPVNLDQK HIEALKEIFG EADVSTAVKD RVSVAYGKTM YDAYRLREGI
LENIADVVVY PSSHDQIVKL VAYANEHKIP LYVYGGGSSV TRGVEAVRGG ISLDMRKNFN
KVLAFNETDQ TITVQAGMSG PQLEAHLNNA QKEFNAKMAY TCGHFPQSFE YSSVGGWVVT
RGAGQNSTYY GNIKDIVFQQ TYVTPAGIVK SYGLPAHAVG PDIDELMMGS EGSFGILTNV
TLRFFKYRPE TRKKFSFIFK TWEDGMKACR EIMQNESGFP SVFRLSDAEE TDMALKLYGV
EGTIAETAMN LMGYKPMKRC LFLGWSEGAK EFSKQLYKKV KRICKQNGGL FLTGKPVDGW
EHGRFTDPYL RESLQDYGVI IDTMECSVTW DMMPKVHEEV RRFAKSRPHT VCMTHLSHAY
PQGANLYFIF IGLFKNKEEY LEYQYGIFDN IMKAGAAMSH HHGVGKMTAA WVEESIGQTN
FKIFKALKKH FDPNNIMNPG GTLGLDMPED QKRKPKYAGK TWEE
//
