ID N1WNJ4_9LEPT Unreviewed; 533 AA.
AC N1WNJ4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=LEP1GSC060_1104 {ECO:0000313|EMBL:EMY78817.1};
OS Leptospira weilii serovar Ranarum str. ICFT.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218598 {ECO:0000313|EMBL:EMY78817.1, ECO:0000313|Proteomes:UP000012313};
RN [1] {ECO:0000313|EMBL:EMY78817.1, ECO:0000313|Proteomes:UP000012313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICFT {ECO:0000313|EMBL:EMY78817.1,
RC ECO:0000313|Proteomes:UP000012313};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAR-2013) 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:EMY78817.1}.
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DR EMBL; AOHC02000016; EMY78817.1; -; Genomic_DNA.
DR AlphaFoldDB; N1WNJ4; -.
DR STRING; 1218598.LEP1GSC060_1104; -.
DR Proteomes; UP000012313; 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: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}.
FT DOMAIN 19..374
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 397..514
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 533 AA; 59650 MW; 0D09CBAD422139D6 CRC64;
MEKPNRTEQI SKLQKESFDI LVIGGGSTGA GTAFDSAKRG YKTALIEKKD FASGTSSRST
KLIHGGVRYL AQFHFKLIHE ALTERQRLLE NAPHLVKPLK FLLPAYRFYE RPYYGIGLTL
YDILASKGKL PSHKSVSKSE AISEFAAIQK DGLFGGITYY DAQFNDSRLN VLLARSAEKE
GAIVANRVEL VSFIKKNGKI VGADLKDLET EKTFPVYAKV IANTTGIWVD HVRKLDDQRA
LNVLSPSQGI HLVFSIEKIP CESAMIIPKT KDGRVVFIIP WEDHVILGTT DTPIENPGDE
PLPIGNEVQF LLDTGNEYLE NPVTEKDILS VFVGIRPLIS PEGNQDTKNI SREEVVLVSN
SGLVTMGGGK WSTYRKMAED LVDKLIQVGN LENKAKCSTK FYSYPGAEGY SESLYQEIEK
TYKVDTQFAK RLQNYYGTEV FEILGKKPKL LSKGIPYFEE EVLFAAKEEF ALGVTDIIAR
RFRVLFVDLD LAQKMVVPVA ALLSKQLKWK DKKKKSEESA AIDLIANLKK SYR
//
