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Database: UniProt
Entry: A0A0S8A5G4_9BACT
LinkDB: A0A0S8A5G4_9BACT
Original site: A0A0S8A5G4_9BACT 
ID   A0A0S8A5G4_9BACT        Unreviewed;       520 AA.
AC   A0A0S8A5G4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KPJ94355.1};
GN   ORFNames=AMS18_03825 {ECO:0000313|EMBL:KPJ94355.1};
OS   Gemmatimonas sp. SG8_17.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatimonas.
OX   NCBI_TaxID=1703355 {ECO:0000313|EMBL:KPJ94355.1, ECO:0000313|Proteomes:UP000051607};
RN   [1] {ECO:0000313|EMBL:KPJ94355.1, ECO:0000313|Proteomes:UP000051607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_17 {ECO:0000313|EMBL:KPJ94355.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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}.
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:KPJ94355.1}.
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DR   EMBL; LJNM01000052; KPJ94355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8A5G4; -.
DR   PATRIC; fig|1703355.3.peg.3530; -.
DR   Proteomes; UP000051607; Unassembled WGS sequence.
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: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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
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   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          19..376
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          418..501
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   520 AA;  57593 MW;  3F53E33393315340 CRC64;
     MNRDSMTDRL RDRTTEAWDI IVIGGGATGM GIAVDAASRG FEVLLLEQAD FGKGTSSRST
     KLVHGGVRYL QQGNISLVME ALRERGRLLQ NAPHLVSDLA FVVPNYEWWE APFYGVGMKV
     YDVMAGRYRF GRSKNLSVEE TIARLPNIER EGLRGGVLYH DGQFDDARLL VNLAQTAFEQ
     GATVINYAKV NDLMKDSAGF LTGVRVVDQE NGEEFQAGAR VVINATGPFC DEIRRLDSPT
     AAAVIQPSQG VHITLDRSFL AGDTAIMVPR TTDGRVMFAL PWHDHVIVGT TDTPLDRVSL
     EPRPTAEEVD FILETTVQYL VRDPTREDVL SAFAGIRPLV RAGQADNTAT LSREHSIEIS
     ASGLLTIAGG KWTTYRNMAE DCVDHAITVG DLEDRPCVTK SLRIHGHLRD AERFGELAWY
     GSDATAVRTL IESEDRFGER LHPALPYRAG EVVWSTRSEM TRTVDDYLSR RSRATFLNAR
     AAMEMAPTVA QLLAEALGRD DSWVQSQVRE YRQIASGYLP
//
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