ID A0A0P1IDB0_9RHOB Unreviewed; 573 AA.
AC A0A0P1IDB0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Aerobic glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:CUK06503.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:CUK06503.1};
GN Name=glpD_2 {ECO:0000313|EMBL:CUK06503.1};
GN ORFNames=RUE5091_02848 {ECO:0000313|EMBL:CUK06503.1};
OS Ruegeria denitrificans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUK06503.1, ECO:0000313|Proteomes:UP000051260};
RN [1] {ECO:0000313|EMBL:CUK06503.1, ECO:0000313|Proteomes:UP000051260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5091 {ECO:0000313|EMBL:CUK06503.1,
RC ECO:0000313|Proteomes:UP000051260};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYUD01000008; CUK06503.1; -; Genomic_DNA.
DR RefSeq; WP_058282523.1; NZ_CYUD01000008.1.
DR AlphaFoldDB; A0A0P1IDB0; -.
DR STRING; 1715692.RUE5091_02848; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000051260; 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:UniProtKB-EC.
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 ECO:0000313|EMBL:CUK06503.1}.
FT DOMAIN 20..403
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 417..535
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 573 AA; 63233 MW; FF2B0096B4ED9748 CRC64;
MSEQRQQNLA ILRKNAAFEV VVVGGGVNGI GVYRELALQG LRVLLVERND FASGCSAAPS
RMIHGGLRYL ENGEFDLVRE SLQERDALLL NAPHMVRPLP TVIPITSVFS GMFNAAASFV
GWQGKPSSRG AVPIKLGLSL YDWVTRKRRI LPRHHFNSAG QTRKDWPALT PKATRSAVYY
DAQITHPERL CVEMIRDVAA EASDCVALNY AEMTRDGDSY SVTDRRSGAT VPVMPKVIVN
ATGAWLDDTV NGLGGRVNER MVSGTKGSHL IIDNPALHQA LGGHMVYFEN TDGRVCIVFP
YQGKVLAGST DIRVDKAARV RCEPEEFDYI LGSLRLVFPG VEISPDQVVF SYSGIRPLPR
SDQDFTGRIS RGHDTRRLDG DVPQFCMVGG KWTTFRAFGE QTADEVMAEL EHARRASTLG
LPIGGGAQFP NARESLKSRL VADFRIAPER AHHLMEHYGT QADDVAQFCQ SVQDAPLTQG
CLYTRAEIIW LTRTEYVETL SDIVLRRTAL AITGQISNAL LAQLADVFAH ERGLGPQETN
DQKQALIHEL SEFYGVTAEA LAARNKKRRT ECV
//
