ID A0A1H8VM33_9GAMM Unreviewed; 520 AA.
AC A0A1H8VM33;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN04488052_11388 {ECO:0000313|EMBL:SEP16461.1};
OS Aquisalimonas asiatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=406100 {ECO:0000313|EMBL:SEP16461.1, ECO:0000313|Proteomes:UP000199657};
RN [1] {ECO:0000313|EMBL:SEP16461.1, ECO:0000313|Proteomes:UP000199657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEP16461.1,
RC ECO:0000313|Proteomes:UP000199657};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOEG01000013; SEP16461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8VM33; -.
DR STRING; 406100.SAMN04488052_11388; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000199657; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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:UP000199657}.
FT DOMAIN 9..368
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 391..497
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 520 AA; 57599 MW; B22EE3F960302FF1 CRC64;
MTNENSNYDL VVVGGGINGA GIARDAAGRG LRVLLCERDD IAAHTSSAST KLIHGGLRYL
EYYEFSLVRK ALKEREVLLK AAPHIIWPMR FVMPHTRSLR PRWMIRAGLF LYDHLGGRSS
LPGSRGLRLA TDPAGQPLRP EFTDGFAYSD CWVQDSRLVV LNALDAAERG AEVCIHTACV
GARREGDHWA VDLQDQHSGA NRTIQARALV NAAGPWVSRF LQSVTGRAEQ AAGKHVRLVK
GSHLVVPRLF DHDQAYLLQN DDRRVIFVIP YEHDYSLIGT TDEAFEGDPR SLSISDAETE
YLCNTINHYF QRAITPADVV WSYAGVRPLY DDAAADASAV TRDYVLDLDT DGGRAPLLSV
FGGKITTYRT LAEDALAQLA GPLQLAARPW TATETLPGGD IPAADFDAWL AALGEDYPFL
PPGLLWRYAR NYGTRMHTLV GHARSLDDLG EHLGDGMYTA ELDYLIRYEW ARTADDVLWR
RSRMGLHVSE TTRQAIDAWF SRHGAPEQPG LTGEAHRAAR
//
