ID A0A239U625_9STAP Unreviewed; 556 AA.
AC A0A239U625;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:GEP84314.1};
GN ORFNames=SPI02_08990 {ECO:0000313|EMBL:GEP84314.1};
OS Staphylococcus piscifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=70258 {ECO:0000313|EMBL:GEP84314.1, ECO:0000313|Proteomes:UP000321736};
RN [1] {ECO:0000313|EMBL:GEP84314.1, ECO:0000313|Proteomes:UP000321736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109625 {ECO:0000313|EMBL:GEP84314.1,
RC ECO:0000313|Proteomes:UP000321736};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Staphylococcus piscifermentans NBRC
RT 109625.";
RL Submitted (JUL-2019) 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:GEP84314.1}.
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DR EMBL; BKAR01000008; GEP84314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239U625; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000321736; 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 21..352
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..532
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 556 AA; 62599 MW; 673B177C883C48E9 CRC64;
MSLSTLKRNE IKDNFKNQEY DIVIIGGGIT GAGVALDASQ RGMKVALVEM QDFAQGTSSR
STKLVHGGLR YLKQLQVGVV AETGRERAIV YENGPHVTTP EWMLLPMHKG GTFGKFSTSI
GLAMYDRLAG VKKSERKKML SKKETLAKEP LVKKDGLKGG GYYVEYRTDD ARLTIEVLKR
AAEKGADILN YTKSMNFTYD DKEKVNGIQV TDMLTDEPYT IHAKKVINAS GPWVDEVRSS
DYSKNNKQLR LTKGVHIVID QSKFPLQQAV YFDTEKDGRM IFAIPREGKA YIGTTDTFYD
NDKTSPLPNQ KDRDYLIDAV NYMFPGLDIE DKDIESSWAG VRPLILEEGK DPSEISRKDE
IWEGKSGLLT IAGGKLTGYR HMAKGIVDLV SKRLQQEYKL KFKPCETKEL KISGGDVGGS
ANFEQFVKEK TKEGEASNLD AKTAEDIARR YGSNADQLYQ IAYTAQYQNS GLPIELYTEL
VYGIQHEMVY KPTDFLIRRT GMLYFDIEDV KKYKEAVMDV MSQLLNYDAE QRALYAEELN
EAIEEATHGN HQPAEK
//
