ID I0UU09_9MICC Unreviewed; 588 AA.
AC I0UU09;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=HMPREF1324_2143 {ECO:0000313|EMBL:EID51362.1};
OS Rothia aeria F0474.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=1125724 {ECO:0000313|EMBL:EID51362.1, ECO:0000313|Proteomes:UP000004863};
RN [1] {ECO:0000313|EMBL:EID51362.1, ECO:0000313|Proteomes:UP000004863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0474 {ECO:0000313|EMBL:EID51362.1,
RC ECO:0000313|Proteomes:UP000004863};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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:EID51362.1}.
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DR EMBL; AJJQ01000023; EID51362.1; -; Genomic_DNA.
DR RefSeq; WP_006887852.1; NZ_AJJQ01000023.1.
DR AlphaFoldDB; I0UU09; -.
DR PATRIC; fig|1125724.3.peg.899; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000004863; 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 31..365
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 416..540
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 588 AA; 63899 MW; 78E04B1269C9B50F CRC64;
MGSQQFNKLS HLTASSRARA LADMAEGPEL DVLVIGGGIT GAGIALDAAT RGLRTGIVEA
GDWAAGTSAW SSKLIHGGLR YLYNLDFKLV AEALKERGLL LEKIAPHLVH AQPFLWPLKT
PVIERSYSAI GIGMYDTLAY IGSRGKKGVP SQRHFTKKGT KTVFPDIKDS AFTGAIQFYD
ARVDDARLVV DVVRTASGYG ALAASRTQVV GIDKDTSGKV VGARLADLES GQELTVKAKH
IINATGVWTE ESESLANPDA GLEVLASKGI HIVVPRDRIQ ATSGIFTKTE KSVLFIIPWQ
RYWIIGTTDT PYTEDRERPV ATRQDIDYVL EQANKLIADP LTHDDIIGTY SGLRPLLQPK
VKGDGAQSTK VSREHTVTEV APGMSAIAGG KLTTYRVMAA DAVDFALGDR AQERPSVTET
IALVGADGYR AIEAGRGRYA QRYGWDEDRI THLLERYGAQ IEDLGALIDA DPDLGAPLKH
APQFLRADVV FAVRYEGALH LEDVLVRRVR LDLEQRDRGL AAAPEILEIM RSELGWSPEQ
AQKEFDLYAA RVAAIRQAET ASTDAEASAK IEAVEPVAPR RTLNVHHS
//
