ID A0A1N7N8K8_9RHOB Unreviewed; 532 AA.
AC A0A1N7N8K8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN05421759_10764 {ECO:0000313|EMBL:SIS94539.1};
OS Roseivivax lentus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=633194 {ECO:0000313|EMBL:SIS94539.1, ECO:0000313|Proteomes:UP000186684};
RN [1] {ECO:0000313|EMBL:SIS94539.1, ECO:0000313|Proteomes:UP000186684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29430 {ECO:0000313|EMBL:SIS94539.1,
RC ECO:0000313|Proteomes:UP000186684};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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; FTOQ01000007; SIS94539.1; -; Genomic_DNA.
DR RefSeq; WP_076448406.1; NZ_FTOQ01000007.1.
DR AlphaFoldDB; A0A1N7N8K8; -.
DR STRING; 633194.SAMN05421759_10764; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000186684; 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}.
FT DOMAIN 11..388
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 411..519
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 532 AA; 59187 MW; A167CA94EADDFE45 CRC64;
MAQRPDTDIS DLFIIGGGIN GCGIARDAAG RGLSVTLAEM NDLASATSSA STKLFHGGLR
YLEYFEFRLV REGLIERETL LRAMPHISWP MRFVLPYHKD MRFESETPTS KLLSVVMPWM
KGRRPAWLIR LGLFMYDTLG GRKILPGTST LDLTGVPEGA PLEDRFEQAF EYSDCWIEDS
RLVVLNARDA EARGAEILTR TKVLSAERAD DLWQIKTQEN ENGPVRVHHA RMLVNAGGPW
VGDIIQTKVR LNTREGVRLV RGSHIVTRKL YDHDKCYFFQ GTDGRIIFAI PYETDFTLIG
TTDAEHADPA EKPVATEAEQ RYLIDFSNQY FKREITPNDI VWTYSGVRPL YDDGASSATA
ATRDYTLKVD ADGGAPMLNV FGGKITTYRR LAEAALEKIG AHLSVAKGPW TAGVPLPGGD
FPVDGVTARI EALKARYPFL TDRWARRLVR AYGTEAAEVL GDAKDAGALG KSFGADLTEA
EIRWLMAREY AQTAEDVVWR RSKLGLRMTE QDIAALDAFM AQAHHGHARA AE
//
