ID A0A0A8UVV9_LEGHA Unreviewed; 493 AA.
AC A0A0A8UVV9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:CEK10919.1};
GN ORFNames=LHA_1887 {ECO:0000313|EMBL:CEK10919.1};
OS Legionella hackeliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=449 {ECO:0000313|EMBL:CEK10919.1, ECO:0000313|Proteomes:UP000032803};
RN [1] {ECO:0000313|Proteomes:UP000032803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC35250 {ECO:0000313|Proteomes:UP000032803};
RA Gomez-Valero L.;
RL Submitted (SEP-2014) 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; LN681225; CEK10919.1; -; Genomic_DNA.
DR RefSeq; WP_045106208.1; NZ_UGOC01000002.1.
DR AlphaFoldDB; A0A0A8UVV9; -.
DR STRING; 449.LHA_1887; -.
DR KEGG; lha:LHA_1887; -.
DR PATRIC; fig|449.7.peg.2244; -.
DR HOGENOM; CLU_015740_5_0_6; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000032803; Chromosome I.
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; 6.10.250.1890; -; 1.
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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 6..356
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 377..474
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 493 AA; 56058 MW; BD1E985816F7A998 CRC64;
MEQIFDVAVV GGGINGCGAA ADAALRGLSV ILLEQGDLAS KTSSSSSKLI HGGLRYLEYY
DFGLVKKALD ERQRLLTLAP HLVRPQLFVL PYQESMRPAW LLRTGLFLYD NLSRNNQLPK
SKFIRRKQGP YFSPLKKEYD KGFLLYDCTT DDSRLTITNA LLAKKHGAAI HNYTKLTHAT
VEQGLWYLTV KTMFGEEHLI KARAIINATG PWVESCNELL GIPNQFKLSL VKGSHLVVHK
LYEGQHAYLL QHEDKRIVFI VPYQGHTMIG TTDVALKGSL DEINISNEEV DYLCALVNNY
LRTSIQREDI INTWSGVRPL LAASGELKAL SRDYTYFYTD SPAPAVTIYG GKITTYRQLA
METINKLQTV FPYLGTSKTE HTPLPGATWN NMSYKDYLFY ARDKYFWLTD EIKERYLASY
GTCTEELLAG CNKMTDLGYD FGSGLFQAEV NYLCREEWAH TSEDILWRRT KLGLNFSPEN
MQELSEYLLH TYQ
//
