ID A0A418T296_9RHOB Unreviewed; 505 AA.
AC A0A418T296;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=D3P04_06305 {ECO:0000313|EMBL:RJE87342.1};
OS Paracoccus onubensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1675788 {ECO:0000313|EMBL:RJE87342.1, ECO:0000313|Proteomes:UP000284202};
RN [1] {ECO:0000313|Proteomes:UP000284202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1011MAR3C25 {ECO:0000313|Proteomes:UP000284202};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA Laiz L., Saiz-Jimenez C.;
RT "Acidovorax cavernicola nov. sp. isolated from Gruta de las Maravillas
RT (Aracena, Spain).";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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:RJE87342.1}.
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DR EMBL; QZCG01000003; RJE87342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418T296; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000284202; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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; PS00977; FAD_G3PDH_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000284202}.
FT DOMAIN 9..356
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 387..490
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 505 AA; 56715 MW; 8A506EB16F061123 CRC64;
MTSDPEMIDL FVIGGGINGA GIARDAAGRG LKVVLCEKDD LAQGTSSRSG KLVHGGLRYL
EYYEFRLVRE ALIEREVLMR SAPHIIWPMR FVLPHSPQDR PAWLVRLGLF LYDNLGGRQK
LPGTRTLNLR RDPEGAPLMN QYAKGFEYSD CWVDDARLVV LNAVDAAERG AEVLTRSPCI
SARREDGAWT VQTRSDLTGE TRTFRARCVV NCAGPWVSDV IGRVAGANSK RNVRLVKGSH
IIVPKFWHGN NAYLVQNHDR RVIFINPYEG DKALIGTTDI AYEGRAEDVK ADESEIEYLI
AAVNRYFKEK LRRSDVLETF SGVRPLFDDG QGNPSAVTRD YVFDLDMNGG APLLNVFGGK
ITTFRELAER GMHRLQEVFP DMGPDWTETA TLPGGEIANA DYESYANLLR ELHPWMPRKL
VHHYGRLYGA RTKDVVAGAM KLDDLGRHFG GQLYEAEARY LTRKEWAMTA EDILLRRTKH
YLHLTAAERA AFAKWFETAA LADAA
//
