ID A0A098G479_9GAMM Unreviewed; 507 AA.
AC A0A098G479;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-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:CEG56781.1};
GN ORFNames=LFA_1358 {ECO:0000313|EMBL:CEG56781.1};
OS Legionella fallonii LLAP-10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG56781.1, ECO:0000313|Proteomes:UP000032430};
RN [1] {ECO:0000313|Proteomes:UP000032430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
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; LN614827; CEG56781.1; -; Genomic_DNA.
DR RefSeq; WP_045095394.1; NZ_LN614827.1.
DR AlphaFoldDB; A0A098G479; -.
DR STRING; 1212491.LFA_1358; -.
DR KEGG; lfa:LFA_1358; -.
DR HOGENOM; CLU_015740_5_0_6; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000032430; Chromosome.
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:UP000032430}.
FT DOMAIN 6..359
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 380..480
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 507 AA; 57606 MW; F73CFA6B96FB563A CRC64;
MEQVFDVAII GGGINGCGCA ADAALRGLSV VLFEQDDLAS KTSSSSTKLI HGGLRYLENY
EFALVKKALE ERQVLLNLAP HLVHPQSFIL PYQKHMRPAW LLRLGLFFYD HLSRKNHLPK
CKSIKRTKKN NYFTPLIDQI KRGFLFYDAS TDDARLTITN ALQAKNHGAS IRPNSKVTQI
EAGNKIWQLT IQPKSGTPYK IKAKSLINAA GPWVAPIAQL TQIAVNREIT LVKGSHIIVP
QLYEGKHAYF LQHDDKRVIF VIPYHGFSMI GTTDTLFNES INSPVRISVE EIDYLLNLVN
TYFKSQLSSK DLIFSWSGVR PLLSSEGKDL KALSRDYSYE FNITPAPIVT IFGGKITTYR
QLAEETINQL VSIFPQMQSC KTKRTPLPGA TFGTVNFEQY LIYARKKYHW LDKELLNRYL
YSYGSCTEHF LSKCTSIESM GKRYGTSLYQ VELDYLISEE WARHIEDILE RRTKLGLVID
SSSKKELENY LTNINHCPAD QSESVCH
//
