ID A0A3N5ZWG8_9BACL Unreviewed; 548 AA.
AC A0A3N5ZWG8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=CW357_02810 {ECO:0000313|EMBL:RPJ97060.1};
OS Rummeliibacillus sp. TYF005.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Rummeliibacillus.
OX NCBI_TaxID=2058214 {ECO:0000313|EMBL:RPJ97060.1, ECO:0000313|Proteomes:UP000271255};
RN [1] {ECO:0000313|EMBL:RPJ97060.1, ECO:0000313|Proteomes:UP000271255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TYF005 {ECO:0000313|EMBL:RPJ97060.1,
RC ECO:0000313|Proteomes:UP000271255};
RA Fan X., Li M., Cui L., Li Y.;
RT "Rummeliibacillus sp. strain TYF005.";
RL Submitted (MAY-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:RPJ97060.1}.
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DR EMBL; QGPZ01000004; RPJ97060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5ZWG8; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000271255; 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:UP000271255}.
FT DOMAIN 20..344
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 399..523
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 548 AA; 62132 MW; 84704E53554A3F6F CRC64;
MFSAAKRDQV IQTLNDYSFD VLVVGGGITG AGIALDAVSR GLSVALVDMQ DFAAGTSSRS
TKLVHGGLRY LKQLQVDVVK ETGREREIVY ENGVHITTPQ WMLLPFYKGG TFGPLSTSIG
LKMYDNLAGV KKTERRKMLN SKETLLKEPL LKQQDLKGGG YYVEYRTDDA RLTIEVLKKA
VELGAICLNY AKVEEFEYED QKVVGAVVRD QISQKTWTIQ ANAVVNATGP WVDTIRQKDT
INNNKKLRLT KGVHIVIDQS IFPLQQSVYF DTPDKRMVFA IPRDGKAYVG TTDTFYEDNP
LKPIATDEDI EYLVDTIHYM FPDVQVSKQD IESCWAGVRP LIYEEGKDPS EISRKDEVWE
SPSGLLTIAG GKLTGYRKMA EKIVNQIVKR KLFKKAGPCI TAELALSGAK GINSQNFDAY
VQYKAQEGTR YGLSLEEGYQ LVRKYGTNID HLYRIIHTLN VHEKTTQLPL DLHAQLIYAM
QYEMAYTPAD FFVRRSSRMF FDIDSVKKYK DAVIQLMSKY LHYVPGEEQQ YRKELEELLF
DATHFANE
//
