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Database: UniProt
Entry: A0A077LY87_9MICO
LinkDB: A0A077LY87_9MICO
Original site: A0A077LY87_9MICO 
ID   A0A077LY87_9MICO        Unreviewed;       533 AA.
AC   A0A077LY87;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Putative alkyldihydroxyacetonephosphate synthase agpS {ECO:0000313|EMBL:CCH76939.1};
DE            EC=2.5.1.26 {ECO:0000313|EMBL:CCH76939.1};
GN   Name=agpS {ECO:0000313|EMBL:CCH76939.1};
GN   ORFNames=BN12_1550008 {ECO:0000313|EMBL:CCH76939.1};
OS   Tetrasphaera japonica T1-X7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH76939.1, ECO:0000313|Proteomes:UP000035721};
RN   [1] {ECO:0000313|EMBL:CCH76939.1, ECO:0000313|Proteomes:UP000035721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T1-X7 {ECO:0000313|EMBL:CCH76939.1,
RC   ECO:0000313|Proteomes:UP000035721};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:CCH76939.1}.
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DR   EMBL; CAJB01000063; CCH76939.1; -; Genomic_DNA.
DR   RefSeq; WP_048553805.1; NZ_HF570958.1.
DR   AlphaFoldDB; A0A077LY87; -.
DR   STRING; 1194083.BN12_1550008; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000035721; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:UniProtKB-EC.
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   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:UP000035721};
KW   Transferase {ECO:0000313|EMBL:CCH76939.1}.
FT   DOMAIN          99..278
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        452
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         131..137
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         262..268
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            313
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   533 AA;  57457 MW;  167F295FFF88EC50 CRC64;
     MAEGRRTGGT RSWWGWGTQE AALSPDEVST LVERTRLMLP GHDFTDHPPP APEDLPVPAP
     RIRVPDSLAA LFSSDVTDRL SHSRGKAFRD VVRNLHGDVT HVADLVARPA TEQDVVDILD
     FCGSANIAVV PYGGGSSVVG GVEPRVDGPA AILDLERLDE VLEVDRVSRA ARIQAGALGP
     HLERRLRPAG LTLRHFPQSF EFSTLGGWLA TRAGGHFATL YTHIDDLTES IRVVTPAGTS
     TSRRLPGSGA GPSPDRLFLG SEGTLGVITE AWMRLQDRPR FGVTASIGFD DFGAAVAATR
     TIAQSGLHPA NCRLLDPAES RINAGASLAD SLLIVAFESA DHPVDAWLER AVEIAADHGG
     SVLSERRRGA DDDRDSSATW RSSFIRMPYR RDALARRGVI VETFETACTW DRFETFHAAV
     TAAAQEAVDR VCGTGVVTCR FTHVYPDGPA PYYGVFAPGR WGSTVAQWDE IKQAVSEAIA
     TNGGTITHHH AVGRDHRPWY DRQRPDPFAA ALRAAKDVLD PAGVLNPGVL IDP
//
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