ID A0A0W1DGP7_9SPHN Unreviewed; 516 AA.
AC A0A0W1DGP7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:KTE17335.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:KTE17335.1};
GN ORFNames=ATE71_02075 {ECO:0000313|EMBL:KTE17335.1};
OS Sphingopyxis sp. H115.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759073 {ECO:0000313|EMBL:KTE17335.1, ECO:0000313|Proteomes:UP000054021};
RN [1] {ECO:0000313|EMBL:KTE17335.1, ECO:0000313|Proteomes:UP000054021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H115 {ECO:0000313|EMBL:KTE17335.1,
RC ECO:0000313|Proteomes:UP000054021};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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}.
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:KTE17335.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNSA01000002; KTE17335.1; -; Genomic_DNA.
DR RefSeq; WP_058801751.1; NZ_LNSA01000002.1.
DR AlphaFoldDB; A0A0W1DGP7; -.
DR STRING; 1759073.ATE71_02075; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000054021; 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; 6.10.250.1890; -; 1.
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.
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 ECO:0000313|EMBL:KTE17335.1}.
FT DOMAIN 9..329
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 386..502
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 516 AA; 57011 MW; 7C655949A6F3A9F5 CRC64;
MSDAPSPYDV IVVGAGVNGA GVARDAAGRG ARVLLIEAND LAGGTSSKST KLIHGGLRYL
EHYEFGLVRE ALKEREVLWG IAPHIIRPLR FVLPYRDGLR PRWLLRLGLF LYDHIGGRKK
LPATRSIDLR RHTAGAPLQP QYVKGFEYSD GWVDDARLVA LNARDAADRG ARVRTRTRAE
MLRCEDGLWI VDARDDQGHQ YRFTGRSVVN AAGPAVLDLL KRADAEPDHQ MRLVRGSHIV
VRKVFEHGYA YFFQLPDGRI FFAIPYERDF TLIGTTDQDH EGPASEARAS DEEIAYLCEG
ASLYFRAPVT PADVVWTYSG VRPLVEDGSG RPEAATRGYR IDLDMAEGAP LLTIYGGKIT
SYRHVAQDAV DQLTGHIDAL ARKHWTGKAS LPGGDFATDG IAALKAEYKL AYPFLPAATV
DRIAQAYGTD ARRWLAGADG WDALGGEIAH GLSLAEVRWM VTHEWARTTD DILWRRSKLG
LHFSADEVAA LAEQTARLVA EARLADPEYF EGRVDS
//
