ID A0A1H4T6R2_9ACTN Unreviewed; 570 AA.
AC A0A1H4T6R2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN04489844_2447 {ECO:0000313|EMBL:SEC51978.1};
OS Nocardioides exalbidus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=402596 {ECO:0000313|EMBL:SEC51978.1, ECO:0000313|Proteomes:UP000198742};
RN [1] {ECO:0000313|Proteomes:UP000198742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22017 {ECO:0000313|Proteomes:UP000198742};
RA Varghese N., Submissions S.;
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; FNRT01000002; SEC51978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4T6R2; -.
DR STRING; 402596.SAMN04489844_2447; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000198742; 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}.
FT DOMAIN 25..387
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 408..532
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 548..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 62598 MW; 34B7295E9CAF9E03 CRC64;
MSLAKALDAD QRADALEHLA AGELDVLVVG GGIVGVGAAL DAVTRGLKVG LVEQRDLASG
TSSRSSKLVH GGLRYLEMFD FALVKEALEE RGLLYTRLAP HLVRPVPFLY PLEHAWERPY
VGAGVALYDG MAMTGKYDMG VPKHKHVFRK QLARMAPDIR TEKLHGAIRY YDCQVDDARL
VMTIARTAAN NGAHVATRTK VTGFLREGDR VVGVSARDLE GQRDLEIRAK VVINAAGVWT
DEVQDLIGGE AQLDVDASKG IHIVVPKDRI RSECGFITKT EKSVLFVIPW DQFWIIGTTD
TAWDYDLAHP AASKTDIDYL LGHVNRLLKD PLDHRDVIGV WAGLRPLLKP MRKEGEMGET
TKLSREHTVA NPVPGLVLVA GGKLTTYRVM ARDAVDHAIR DFDATPASIT DRVPLMGAWG
FEARTNQRVA LSRSSGLDIG VVDHLLGRYG GLVDEVLALI DARPDLGEPL EGAEHYLRAE
VLYAVTHEGA RHLDDVLARR TRVSIETFDR GITAARPAAE LMAGALGWSD AQLEDEVDHY
LRRVEAERQS QLMPTDQEAD EARVKAPDIV
//
