ID A0A1V4HFR7_9BACL Unreviewed; 542 AA.
AC A0A1V4HFR7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=BC351_05630 {ECO:0000313|EMBL:OPH53595.1};
OS Paenibacillus ferrarius.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1469647 {ECO:0000313|EMBL:OPH53595.1, ECO:0000313|Proteomes:UP000190626};
RN [1] {ECO:0000313|Proteomes:UP000190626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CY1 {ECO:0000313|Proteomes:UP000190626};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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|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:OPH53595.1}.
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DR EMBL; MBTG01000023; OPH53595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4HFR7; -.
DR STRING; 1469647.BC351_05630; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000190626; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000190626}.
FT DOMAIN 7..338
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 393..521
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 542 AA; 59669 MW; 9B9B0C9F6E2A6C1C CRC64;
MTKQPLDLIV IGGGITGAGI ALDAQSRGLR TALIDMQDFA AGTSSRSTKL VHGGLRYLKQ
LDVKVVAEVG KERAIVYENG PHVTTPEWML LPFYKGGTFG KFSTSLGLRV YDFLAGVKRS
ERRKMFRPDQ TLSHEPLLKE KDLKGGGYYV EYRTDDARLT IEVMKKAVEL GVMAVNYAKV
EELLVENGKL VGVRVVDQMS GGKDSYSLYA SKIVNAAGPW VDTLREMDKS KQGKTLHLTK
GVHLVFDQSK FPLRQAIYFD TPDGRMVFAI PRDGKTYIGT TDTNYKGDIV NPRITVADRA
YVLRAANEMF PSLELTEADV ESSWSGLRPL IHQEGKDPSE ISRRDEIFVS DSGLISMAGG
KLTGYRKMAE SVVDKIAAML LAEGKVSAAL PPSRTRMLPI SGGDVGGSAK LASFLQGKIS
QGQRLGLTKP EATLLAHRYG SNVDAVYELL EQHRDEAARR GMPAVVLAAL VYAVEREMVV
KPADFFIRRT GALFFDIAWA KKWKAPAVAF LAERFGWDEA QTKAYAAELE RLLHEAVNPL
EA
//
