ID A0A1Y5SAY9_9RHOB Unreviewed; 531 AA.
AC A0A1Y5SAY9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:SLN36558.1};
GN ORFNames=PAM7971_01569 {ECO:0000313|EMBL:SLN36558.1};
OS Pacificibacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pacificibacter.
OX NCBI_TaxID=658057 {ECO:0000313|EMBL:SLN36558.1, ECO:0000313|Proteomes:UP000193307};
RN [1] {ECO:0000313|EMBL:SLN36558.1, ECO:0000313|Proteomes:UP000193307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7971 {ECO:0000313|EMBL:SLN36558.1,
RC ECO:0000313|Proteomes:UP000193307};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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}.
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DR EMBL; FWFW01000004; SLN36558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5SAY9; -.
DR STRING; 658057.SAMN04488032_10317; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000193307; 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; 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; PS00977; FAD_G3PDH_1; 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 ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000193307}.
FT DOMAIN 6..355
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..506
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 531 AA; 59023 MW; E600457DAFDBA5D8 CRC64;
MEPDFDLLVI GGGINGCGIA RDASGRGLSV CLAEMNDIAS ATSASSTKLF HGGLRYLEYF
EFRLVREALI EREVLLKAMP HIAWPMRFVL PYHKSMRFDL STPTSKILSA VMPWMKGRRP
AWLIRLGLFM YDNLGGREIL PGTTRLDLRS APEGKPLKKR FEKAYEYSDC WVEDSRLVVL
NARDAEQRGA SIRTREKVVS ANVVDGVWHV EMQNTLTGAG TKVTAGMVVN AAGPWVGDVL
RGTLKSNQQG NVRLVRGSHI VTKRLFEHDK CYFFQGTDGR IIFAIPYETD FTLIGTTDAD
HPDPSQKPEC TPEECDYLIN FINEYLENPI EAVDVVWSYS GVRPLYDDGA SSASAATRDY
VLKLDKSRGA PSLNVFGGKI TTYRRLAESA LDLVSEVYPK TPKSWTAGVA LPGGDFPVDG
VDNLIKAATS RYPFLTNRWA KRLVRAYGCE VHDILGDANS VADLGVDFGA DLTEREVIWL
IDKEYARSAE DVVWRRSKLG LRMTKAQITN LDIWIQSHLQ ADQSAVAQGG Q
//
