ID A0A0Q4RJ77_9BACL Unreviewed; 565 AA.
AC A0A0Q4RJ77;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=ASF12_27860 {ECO:0000313|EMBL:KQO15831.1};
OS Paenibacillus sp. Leaf72.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO15831.1, ECO:0000313|Proteomes:UP000051722};
RN [1] {ECO:0000313|EMBL:KQO15831.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO15831.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO15831.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO15831.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQO15831.1}.
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DR EMBL; LMLV01000003; KQO15831.1; -; Genomic_DNA.
DR RefSeq; WP_056033894.1; NZ_LMLV01000003.1.
DR AlphaFoldDB; A0A0Q4RJ77; -.
DR STRING; 1736234.ASF12_27860; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000051722; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051722}.
FT DOMAIN 31..387
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 414..543
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 565 AA; 62090 MW; B27E1199798F1BAD CRC64;
MSRQTGSAKQ GAFSALNREQ LYRSLGEETF DLLVIGGGIT GAGIALDAQT RGIKTALVDM
QDFAAGTSSR STKLVHGGLR YLKQLEIGVV AEVGKERAIV YENGPHVTTP EWMLLPFYTG
GTFGKFSTSL GLRVYDFLAG VKRGERRKMF SVDETMSREP LLKREGMKGG GYYVEYRTDD
ARLTIEVMKK AVDMGALAIP YVKVESFIYE DGRVVGANVR DLLSGAESKV RAVKVVNATG
PWVDTLREQD GSKQGKTVHL TKGVHLVFDQ SRFPLHQAVY FDTPDGRMVF AIPRDGKTYI
GTTDTNYKAD KAHPRMTKQD LDYILQAANF MFPSIKLKAS DVESSWAGLR PLIHQEGKDP
SEISRKDEVF VAGSGLISIA GGKLTGYRKM AESVVNTVST QLTAEGRSGI RPSGTKNLPL
SGGDFGGSSH FPAFVAKKTE EGVRAGLSRA EAERLARHFG TNVDRVIGLI PQYKGQATAS
GQELPLSLRI ELMYALEYEL TTKPADFWIR RTGNLLFDRA RVLQWKEAVH AEMAALFGWS
EETSAAYAAE LEQELHYAVT PVEQE
//
