ID   A4X820_SALTO            Unreviewed;       508 AA.
AC   A4X820;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ABP55020.1};
GN   OrderedLocusNames=Strop_2576 {ECO:0000313|EMBL:ABP55020.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS   105044 / CNB-440).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP55020.1, ECO:0000313|Proteomes:UP000000235};
RN   [1] {ECO:0000313|Proteomes:UP000000235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC   {ECO:0000313|Proteomes:UP000000235};
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; CP000667; ABP55020.1; -; Genomic_DNA.
DR   RefSeq; WP_012013801.1; NC_009380.1.
DR   AlphaFoldDB; A4X820; -.
DR   STRING; 369723.Strop_2576; -.
DR   KEGG; stp:Strop_2576; -.
DR   PATRIC; fig|369723.5.peg.2653; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   Proteomes; UP000000235; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000235}.
FT   DOMAIN          24..351
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          403..506
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   508 AA;  53839 MW;  2CF66230A212C0E9 CRC64;
     MDATLTGPRR DRELAELAGG VAVDLLVVGL GVTGAGVALD AASRGLSVAA VEAHDLAHGT
     SRWSSKLVHG GLRYLAHGQV GIAYESAVER HVLMTRTAPH LIRALPMLLP MTEDTAGWQD
     RAAAVGLRAG DLLRVCAGTT RRTLPGTRRL GPAEAGAMAP ALRRVGLHGA HLSWDGQLCD
     DARLVVGLSR AAAARSARIL PRARVVELHG DGATVEDTRT GETLHIAARA VINATGVWAS
     SLTRHVRLRP SRGTHLVLPA ALLGGLWAGL TIPVPGEFAR YVLALPQTDG LAYVGLTDEP
     LVGPIPDVPE PTEADIAFLL DVLNSVLDRP LRRSDVLSAY AGLRPLLADA TDRTADLSRQ
     HAVIDDPDGI ISVVGGKLTT YRRMAEDAVD TAVRRRDLTA GACRTRRLPL PGAASPARLA
     RVPAPRRLIA RYGVEAVNVL AEAPAHLHRP ISAEIPVTGA ELLWAARHEL ARTVDDLLDR
     RTRLGLVPAH RDAALPVAGE VLELAARR
//