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Database: UniProt
Entry: A6EEZ0_9SPHI
LinkDB: A6EEZ0_9SPHI
Original site: A6EEZ0_9SPHI 
ID   A6EEZ0_9SPHI            Unreviewed;       512 AA.
AC   A6EEZ0;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:EDM36061.1};
GN   ORFNames=PBAL39_23677 {ECO:0000313|EMBL:EDM36061.1};
OS   Pedobacter sp. BAL39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM36061.1, ECO:0000313|Proteomes:UP000003664};
RN   [1] {ECO:0000313|EMBL:EDM36061.1, ECO:0000313|Proteomes:UP000003664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL39 {ECO:0000313|EMBL:EDM36061.1,
RC   ECO:0000313|Proteomes:UP000003664};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:EDM36061.1}.
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DR   EMBL; ABCM01000010; EDM36061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6EEZ0; -.
DR   STRING; 391596.PBAL39_23677; -.
DR   eggNOG; COG0578; Bacteria.
DR   Proteomes; UP000003664; 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: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:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 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.
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:UP000003664}.
FT   DOMAIN          3..360
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          396..487
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   512 AA;  56442 MW;  F2B52F56DA08C84F CRC64;
     MWDLIVVGGG ATGLGTALDA ASRGYKTLLL EQADFAKGTS SRSTKLVHGG VRYLAQGDIG
     LVREALYERG LLLKNAPHLV KNESFIIPNY EWWGGAFYTI GLTMYDLLAG SLGFGRAKHI
     SKKEVIRRLP TIQQKGLYGG VVYHDGQFDD SRLAINLAQT SLEQGATVLN YFKVGGLLKN
     EQGKISGVIA ADIETGITYE LKSKSVVNAT GVFVDDLLQM DKPGNKPLVR PSQGVHLVLD
     MSFMPADDAL MIPKTDDGRV LFAVPWHDKL VVGTTDTPLN EHSLEPVALE EEIKFILRTA
     GRYLAKAPTR KDVLSVFAGL RPLAAPQNGS SKTKEISRSH KLFVSDSGLI TITGGKWTTY
     RRMGQDTVDK AIVVGQLPVK DVRTKDLPIH GSIQNVDRTD HLYVYGSDRK ALLALRNENS
     SWAEQLDVRA DFIKAEVIWA VRYEMARTVE DVLARRVRVL FLDARMAIDM APKVAALMAA
     ELKKDQAWEQ AQVAEFTKLA GSYLLEEYIP SR
//
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