ID A0A2T0UXY3_9MICO Unreviewed; 572 AA.
AC A0A2T0UXY3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=BCF74_104143 {ECO:0000313|EMBL:PRY62707.1};
OS Knoellia remsis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=407159 {ECO:0000313|EMBL:PRY62707.1, ECO:0000313|Proteomes:UP000237822};
RN [1] {ECO:0000313|EMBL:PRY62707.1, ECO:0000313|Proteomes:UP000237822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1496 {ECO:0000313|EMBL:PRY62707.1,
RC ECO:0000313|Proteomes:UP000237822};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
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|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
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:PRY62707.1}.
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DR EMBL; PVTI01000004; PRY62707.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0UXY3; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000237822; 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: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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000237822}.
FT DOMAIN 25..373
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 401..525
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 572 AA; 62175 MW; AABAE9A4D631CDF2 CRC64;
MANPPKLDGA YRSKAWERLR DNQFDVLVIG GGVTGAGVAL DAATRGLSVA LVEQRDFASG
TSSRSSKLFH GGLRYLEQMN FALVREALKE RELMLTSIAP HLVKPVSFLY PLTHRVWERP
YVTAGLTLYD SMGGARSVPR HKQLTRSGAL RMAPGIKRSA LTGALLYYDA QADDARHTLT
VVRTAAAYGA TVLSSARVTG LKRAGERIVG ATIEDVETGD TVDVSASVVI NCTGVWTDEI
QTLAGGRGRF HVRASKGVHI VVPRDRINSE TGIILRTEKS VLFVIPWGTH WIVGTTDTDW
ELDKAHPAAS EADIDYILEH VNTVLTVPLT HDDIQGVYAG LRPLLSGESD STSQLSREHA
VARPQPGLYS IAGGKYTTYR VMAEDAVDAA GEDLGGDLAS SVTEHIPLVG AQGYHALVNQ
VERLARKRSL PVWRITHLLD RYGSMLDEVL ALADDDPSLL EPLPGAEEYL KVEVVYGVTH
EGALHLDDLL TRRTRISIET PDRGVASAEA AARLVAPHLG WDDERIATEV AAYTARVEAE
RESQKEQNDQ EANAERIAAK DVRNLAVGRA LT
//
