ID F3M382_9BACL Unreviewed; 576 AA.
AC F3M382;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=HMPREF9412_4896 {ECO:0000313|EMBL:EGG38090.1};
OS Paenibacillus sp. HGF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG38090.1, ECO:0000313|Proteomes:UP000004272};
RN [1] {ECO:0000313|EMBL:EGG38090.1, ECO:0000313|Proteomes:UP000004272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF5 {ECO:0000313|EMBL:EGG38090.1,
RC ECO:0000313|Proteomes:UP000004272};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2011) 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|ARBA:ARBA00000153,
CC 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 -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
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:EGG38090.1}.
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DR EMBL; AEXS01000019; EGG38090.1; -; Genomic_DNA.
DR RefSeq; WP_009589973.1; NZ_AEXS01000019.1.
DR AlphaFoldDB; F3M382; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000004272; 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:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 25..350
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 408..537
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
FT REGION 541..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 63078 MW; D81D9691AAF29E29 CRC64;
MEQSQSFSSL DRGHRFQRIA EGTYDLIVIG GGITGAGIAL DAVTRGMSVL LVEMQDFAAG
TSSRSTKLVH GGLRYLKQFE VGMVAEVGKE RAVVYENGPH VTTPEWMLLP IHQGGTFGKF
STSIGLMVYD FLAGVKRGER RSMLSASETL KREPLLKQEG LKGGGYYVEY RTDDARLTLE
VMKEAAARGA VLFNYAKAES LNYDANGRIT GVTVRDMLGG AVKSVSGTKI VNAAGPWVDQ
VREMDKSRKG KMLQLTKGVH LVIDQSRFPL RQAVYFDTPD GRMVFAIPRD GKTYVGTTDT
VYKADPVRPL ITVEDRDYIL KAIHYMFPGV KLSPADVESG WAGVRPLILE EGKSPSEISR
KDEIWESPSG LITIAGGKLT GYRKMADTVV DLVAKRIQES GGKAYGASVT KNLPISGGQV
GGSSQFPDFV RKQTEIGAAQ GIDRKLAEHW ARMYGSNAAE LFRLAKEGSD QAEASALPVS
VLVPLMYAIE HEMASKPADF FIRRTGSLLF HIDWTRKWKV PVINYMATVL GWNEQQRTEY
TRELDEELAS AEQPAANEPP AQAPIPPNAS KAKLSS
//
