ID A0A1Z8VLI6_9PROT Unreviewed; 518 AA.
AC A0A1Z8VLI6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=CBC21_01650 {ECO:0000313|EMBL:OUU60055.1};
OS Proteobacteria bacterium TMED61.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1986601 {ECO:0000313|EMBL:OUU60055.1, ECO:0000313|Proteomes:UP000196561};
RN [1] {ECO:0000313|EMBL:OUU60055.1, ECO:0000313|Proteomes:UP000196561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED61 {ECO:0000313|EMBL:OUU60055.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-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}.
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:OUU60055.1}.
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DR EMBL; NHDO01000011; OUU60055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z8VLI6; -.
DR Proteomes; UP000196561; 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 4..359
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 382..481
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 499..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 58111 MW; AB76D64F690E6853 CRC64;
MMFDVFVVGG GINGCGIARD AAGRGLSVCL AEKDDLGAKT SSGSTKLVHG GLRYLEHYAF
NLVRNSLIER EVLWSIAPHI IYPLRFVLPH HRGLRPSALL RLGLFIYDHL GGRKKLSKSR
KISFASDEVG QPLRSEFKIG FEYSDCWVDD ARLVLMNARD AADRGAKVMV HHEVVSARRE
SGLWVINTRD RHSATHEFRA RILVNAAGPW VSQLTDSAIE GAVHRDMRLI RGSHIVVPKL
YAHDRCYLLQ NSDGRIVFVI PYEGDFSLIG TTDEEHQESL EKIAIEKNEA EYLCVSVNQY
FKTSISLEDI VWSYSAVRPL FDDGTSDAKS ITRDYRVVSE FNETGAPLIS VLGGKITTYR
KLAEEVMAEI SHCLGALGPS WTGSAPLPGG SFACLEFKNE VTRLQEEYPF LSDSYAHRLM
RLYGSLAHQI LRGAKSYKDL GRFFGGHLYE NEVRYLMKYE WAMSVEDVLW RRTKEGLRLS
DNEVGQLSKF LKEVAHENKS VGPNSEVSST TTVERSVA
//
