ID A0A1I4CF90_9ACTN Unreviewed; 575 AA.
AC A0A1I4CF90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN04488085_103447 {ECO:0000313|EMBL:SFK78967.1};
OS Geodermatophilus ruber.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=504800 {ECO:0000313|EMBL:SFK78967.1, ECO:0000313|Proteomes:UP000199152};
RN [1] {ECO:0000313|EMBL:SFK78967.1, ECO:0000313|Proteomes:UP000199152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45317 {ECO:0000313|EMBL:SFK78967.1,
RC ECO:0000313|Proteomes:UP000199152};
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; FOSW01000003; SFK78967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4CF90; -.
DR STRING; 504800.SAMN04488085_103447; -.
DR InParanoid; A0A1I4CF90; -.
DR Proteomes; UP000199152; 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:UP000199152}.
FT DOMAIN 29..385
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 409..533
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 547..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63028 MW; 0F5A0DBD792758BB CRC64;
MTDGLERSSA LSSAGRAHAM AEMESGELDV LVVGGGVVGT GCALDAVTRG LRVGLVEARD
WASGTSSRSS KLLHGGLRYL EMLDFALVRE ALHERGLHLQ RLAPHLARPV PFLYPLEHRL
WERAYVGAGI ALYDAMALTS GHGRGLPHHR HMTRRRALRE APCLKPDSLV GAIQYWDGQV
DDARHVMMIA RTAAAYGALC ANRVEVVTFL RQGERVTGAR ARDLETGREF DIEADQVINA
TGVWTDDTQS MVGTRGQIHV QASKGIHLVV PRDRINSSTG IILRTEKSVL FVIPWGRHWI
VGTTDTPWTY DKAHPAATAA DIEYVLDHVN AVLRTPLTHA DVEGVYAGLR PLLTGESDAT
SKLSREHVVA HPAPGLVVVA GGKYTTYRVM AKDAVDEASR ALDERVPESI TDEVPLVGAE
GYHALWNQRH ELAAESGLHV ARIEHLLRRQ GTLVLDLLPL VADDPSLGQP LAGTEDYLRA
EVVYAASHEG ARHLDDVLAR RTRISIETWH RGLESAEEAA RLMGEVLGWD EEQIKREVNF
YERRVAAERK SQEQPDDAFA DAARLEAGDV VPTAS
//
