ID C9QL17_VIBOR Unreviewed; 522 AA.
AC C9QL17;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 59.
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:EGU47405.1};
GN ORFNames=VIOR3934_18023 {ECO:0000313|EMBL:EGU47405.1};
OS Vibrio orientalis CIP 102891 = ATCC 33934.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU47405.1, ECO:0000313|Proteomes:UP000002817};
RN [1] {ECO:0000313|EMBL:EGU47405.1, ECO:0000313|Proteomes:UP000002817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102891 / ATCC 33934 {ECO:0000313|Proteomes:UP000002817};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU47405.1}.
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DR EMBL; AFWH01000051; EGU47405.1; -; Genomic_DNA.
DR RefSeq; WP_004413042.1; NZ_AFWH01000051.1.
DR AlphaFoldDB; C9QL17; -.
DR STRING; 675816.VIA_002139; -.
DR PATRIC; fig|675816.5.peg.3411; -.
DR eggNOG; COG0578; Bacteria.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000002817; 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; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 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 17..335
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 393..499
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 522 AA; 58753 MW; 5A274E855C08EC14 CRC64;
MSIQHNATAS NASEILDLIV IGGGINGAGI AADAAGRGLS VGLYEANDFA SATSSASSKL
IHGGLRYLEH YEFRLVSEAL AEREVLLRKA PHVARPMRFR LPHRPFLRPA WMIRCGLFLY
DNLGKRTTLP ASKGVDLSKS GLLKPEMKKG FEYSDCWVDD ARLVLLNVLA AKENNAEIRN
YCRVEKAHRA NGIWHVTVHD VMTDQRFERK AKTLVNAAGP WVKQFFDDGL EQASPRNIRL
IKGSHIVVPR IHDEPQAYIL QNKDNRIVFM IPYLDKFSII GTTDVEYKGD PREVAISDDE
VDYLIDIVNQ HFVKQLDRDD VVWTYSGVRP LCDDESDSPQ AITRDYTLEL DAELDQAPLL
SVFGGKLTTY RKLGEAALKK LEPYLSNMGS PWTANQTLPG GNFSCSREQL AQTIQAKYSW
LPEALILRYV TQFGTYTWKM LDGKTSLADM GTEFSQGAQG VYQLEIDYLF NHELAVTQED
ILWRRTKLGL YLSEEEQSAI ADYIRQSLQD KVVTINEINK AG
//
