ID A0A1H9UIL3_9PSEU Unreviewed; 513 AA.
AC A0A1H9UIL3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN04487818_107266 {ECO:0000313|EMBL:SES09276.1};
OS Actinokineospora terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155974 {ECO:0000313|EMBL:SES09276.1, ECO:0000313|Proteomes:UP000199051};
RN [1] {ECO:0000313|EMBL:SES09276.1, ECO:0000313|Proteomes:UP000199051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44260 {ECO:0000313|EMBL:SES09276.1,
RC ECO:0000313|Proteomes:UP000199051};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOGI01000007; SES09276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9UIL3; -.
DR STRING; 155974.SAMN04487818_107266; -.
DR Proteomes; UP000199051; 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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 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:UP000199051}.
FT DOMAIN 25..355
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 404..507
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 513 AA; 53176 MW; 0B50DD7CBBEE6EB1 CRC64;
MSTTALNAER RAADLAAITA GEVVDVLVIG GGVTGAGVAL DAAARGLSVA LVEAEDLAFG
TSRWSSKLVH GGLRYLAKGD VGLAHESAVE RGVLMTTTAP HLTRTLPQLI PLHPPVSGRD
AALAYTGLVA GDGLRRATRT RTDLLPSPRR VSAAEARALA PGLRAAGLRG GLLSFDGQLT
DDARLVVALA RTAAGLGARI ITRARVTGVA PDSVEVVDGL TGKQVLVRSR VVVNATGVWA
GTLVPSVRLR PSRGSHLVVD AAAVGCGATS LTVPIPGAFG RFALVLPQDD GRVYIGLTDE
PVDEIPDVPA VPESDVDFLL DVASSVLESR LTRDDVLGSF AGLRPLVDLP SAAGRSADLS
RHHAVLTEDK VVTVVGGKLT TYRRMAADAV DRAIDLAGLS AGPSRTRTLP LVGAAPRTRL
ATLDAPRRLI ARYGTESPTV AAMGLLDPDL GRPVAAGVTA AEVIWAVRHE GALDADDVLH
RRTRIGLVRQ DTDAARPVVT DLVDRALRGL LTP
//
