ID A0A1G8M3K9_9RHOB Unreviewed; 532 AA.
AC A0A1G8M3K9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN04488026_100510 {ECO:0000313|EMBL:SDI62377.1};
OS Aliiruegeria lutimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=571298 {ECO:0000313|EMBL:SDI62377.1, ECO:0000313|Proteomes:UP000199382};
RN [1] {ECO:0000313|EMBL:SDI62377.1, ECO:0000313|Proteomes:UP000199382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25294 {ECO:0000313|EMBL:SDI62377.1,
RC ECO:0000313|Proteomes:UP000199382};
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; FNEK01000005; SDI62377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8M3K9; -.
DR STRING; 571298.SAMN04488026_100510; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000199382; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199382}.
FT DOMAIN 12..389
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 412..519
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 532 AA; 59067 MW; 9B2E74A5126103F0 CRC64;
MSEKRSQREI FDVFIIGGGI NGCGIARDAA GRGLKVGLAE MGDLASATSS ASTKLFHGGL
RYLEYFELRL VREALIEREV LLQAMPHISW PMRFVLPYHP DMRFDRQTPA SRLLGWTMPW
TRGQRPSWMI RSGLFMYDHL GGRKILPGTT SVDLRNDPAG VPINDKFTKA YEYSDCWVED
ARLVVLNARD AEARGAHIMV RTKVTRAVRD AGVWKITLQN SETGASRQVQ ASMLVNAAGP
WVKDVLEEIA HADTRESVRL VRGSHIVTRK LFDHDKCYFF QGPDGRIVFA IPYESDFTLI
GTTDLEHDRA DTKPVCTEEE KAYLIQLASD YFKRPITEED VVWTYSGVRP LYDDGASSAT
AATRDYVLKV DSDGDAPLLS IFGGKITTYR KLAEAALEKI SAHVPGATGK WTAGAPLPGG
NFPVDGVPAL IAKAQADYPF LDAAWAKRLV RAYGTELWQV LGDAVELSDL GVLFGYNLTE
REVAWLMDKE FARTTDDVLW RRSKLGLRLD AEQVAALDKF MKGVRGGAPD AA
//
