ID A0A1H4SWN4_9FLAO Unreviewed; 548 AA.
AC A0A1H4SWN4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN04489761_3117 {ECO:0000313|EMBL:SEC48281.1};
OS Tenacibaculum sp. MAR_2009_124.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1250059 {ECO:0000313|EMBL:SEC48281.1, ECO:0000313|Proteomes:UP000199366};
RN [1] {ECO:0000313|EMBL:SEC48281.1, ECO:0000313|Proteomes:UP000199366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2009_124 {ECO:0000313|EMBL:SEC48281.1,
RC ECO:0000313|Proteomes:UP000199366};
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; FNSF01000005; SEC48281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4SWN4; -.
DR STRING; 1250059.SAMN04489761_3117; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000199366; 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: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:UP000199366}.
FT DOMAIN 22..345
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..528
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 548 AA; 62418 MW; 5092D6BE1543A29D CRC64;
MNNFSFFNRE NSKQELQSTE FDILIIGGGI TGAGIALDAA SRGMKVALIE KNDFASGTSS
KSTKLIHGGL RYLKQFDFWL VKEVGTERAI VHKLAPHLVI PEKMILPLIE GGTYGSWLTS
IGLKVYDVLA SVEGDDKRKM LDKEEALEKE PLLPEGVLNG AGYYAEYRTD DARLTIEVLK
TASQYDAQII NYVEANEFIY KNKRVVGAKV TDVFSKETFN VNAKYVVNAA GPWVDELRQI
NNSKIGKRLH LTKGVHLVVA HEKLPVKQSV YFDIPDGRMM FAIPRGKVTY FGTTDTNYQE
DKNNVETSIV DALYLIEAVN NMFPEITLTL EDIESSWAGL RPLIHEEGKS ASELSRKDEI
FVSDTKLISI AGGKLTGYRK MAERIVDLVA KKMTRRFEIE FDPIQTEEIV LSGGPFQNFK
SVKIYNKQVN KRMKSEGFTK QDAAYLVYNY GKQTSTILDK FDELSEENSE KRLLKAEIWF
SIHHEMTCTP TDFFMRRTGR LFFDKPSVDR NKQFVIAEFA TYFNWEKELV EIHNQELEEK
IQLAVQFK
//
