ID A0A2P8H767_9BACL Unreviewed; 553 AA.
AC A0A2P8H767;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=B0H99_101310 {ECO:0000313|EMBL:PSL42062.1};
OS Planomicrobium soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planomicrobium.
OX NCBI_TaxID=1176648 {ECO:0000313|EMBL:PSL42062.1, ECO:0000313|Proteomes:UP000242682};
RN [1] {ECO:0000313|EMBL:PSL42062.1, ECO:0000313|Proteomes:UP000242682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12259 {ECO:0000313|EMBL:PSL42062.1,
RC ECO:0000313|Proteomes:UP000242682};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PSL42062.1}.
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DR EMBL; PYAT01000001; PSL42062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8H767; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000242682; 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 20..374
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 402..530
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 553 AA; 61749 MW; 79D7F8796DC581D6 CRC64;
MFSAKQRTQQ IGHMSNHEFD VVIIGGGITG AGIALDAVSR GLSVALLEMQ DFAAGTSSRS
TKLVHGGLRY LKNFQLKIVA EVGREREIVY ENAVHVTEPK RMLLPFYKGG TFGPVFMSIG
LRTYDLLANV KKAERRTMLD PAETLSKEPL LKRDGLVGGG YYVEYRTDDA RLTLETMKKA
AELGTVCLNY VKAEGFIYTD GKISGVQAVD LVNGESIDVF AKKVVNATGA WIDEVQDFDA
ETPEKKLRLT KGVHIVVDQK KFPLKQAVYF DTPDKRMVFA IPRDTKVYVG TTDDFYDEDP
ISPAAEKKDV DYLIMAVKRT FPLVQLAPED VESTWAGVRP LIYEEGKDPS DISRKDEIWV
SENGLISIAG GKLTGYRKMA EVVMDKVVKL LKKETGVKFG KSETKHLPLS GGDFGGSKNF
ASFVHNTAVL SQQYGLSPEQ GRLYAQFFGT NAEKVFSYYR DLSENIPGGI PKTLAAVVEY
AIEEEMARTP SDFFIRRTGD LYFHIQDVVR YQEGVLEYMS HALEYTPEQK EAYQQELLEE
IKVATRYGRD VLG
//
