ID A0A239GHN6_9ACTN Unreviewed; 567 AA.
AC A0A239GHN6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN05421812_101409 {ECO:0000313|EMBL:SNS68660.1};
OS Asanoa hainanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Asanoa.
OX NCBI_TaxID=560556 {ECO:0000313|EMBL:SNS68660.1, ECO:0000313|Proteomes:UP000198362};
RN [1] {ECO:0000313|EMBL:SNS68660.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNS68660.1};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZPH01000001; SNS68660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239GHN6; -.
DR Proteomes; UP000198362; 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; 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:UP000198362}.
FT DOMAIN 24..376
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 406..527
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 567 AA; 61982 MW; D0E1AC4E260F0726 CRC64;
MEAVALSAAQ RSRALAGMAE RELDVLVVGG GVVGAGCALD AVTRGLSTGL VEARDWASGT
SSRSSKLMHG GLRYLEQFEF GLVAESLRER GLLLQRIAPH LVHPVQFLYP LKHRIWERPY
VGSGLILYDT MGLTSGTARG VPHHKHLTRR GALKVAPGLK RSSLIGAVQY YDGQVDDARH
TMSVVRTAAS YGALVANRAR VVDYLREGEQ VVGALVEDLM TGATREVRAK VVINSTGVWT
DDTQQLADTR GEFHVRTSKG VHFTVPRDRI PIDTGLILRT EKSVLFVIPW GRHWLIGTTD
TDWELDKARP AATATDIEYL LEHVNRVLVS PLTEADIEGV YVGLRPLVAG AAESTSKLSR
DHSVASPVPG MVVVAGGKYT TYRKMAEDTV DLAVRQLEQE NVPESPTKDI PLVGADGYKA
LWNQRHELAE AWGLHVHRIE HLLNRYGSLI FELLRLVAQD RGLAEPLPGA DDYLRVEAMY
AASHEGALHL DDVLARRTRA YFETFSRGVQ AAPDAARLMG EVLGWTDVDV DREVAAYEQA
IEADRKAQEA PDDAAADAAR LVAVDLG
//
