ID R8ASR9_PLESH Unreviewed; 502 AA.
AC R8ASR9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:EON89379.1};
GN ORFNames=PLESHI_05967 {ECO:0000313|EMBL:EON89379.1};
OS Plesiomonas shigelloides 302-73.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Plesiomonas.
OX NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON89379.1, ECO:0000313|Proteomes:UP000014012};
RN [1] {ECO:0000313|EMBL:EON89379.1, ECO:0000313|Proteomes:UP000014012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=302-73 {ECO:0000313|EMBL:EON89379.1,
RC ECO:0000313|Proteomes:UP000014012};
RX PubMed=23814109;
RA Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype O1).";
RL Genome Announc. 1:e00404-13(2013).
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:EON89379.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AQQO01000037; EON89379.1; -; Genomic_DNA.
DR RefSeq; WP_010862818.1; NZ_KB944507.1.
DR AlphaFoldDB; R8ASR9; -.
DR STRING; 703.SAMEA2665130_00180; -.
DR PATRIC; fig|1315976.3.peg.1173; -.
DR HOGENOM; CLU_015740_5_0_6; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000014012; 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.
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:UP000014012}.
FT DOMAIN 5..331
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 384..482
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 502 AA; 56627 MW; AEF34DF1F483E795 CRC64;
MEINDLMVVG GGINGAGIAA DAAGRGLSVV LCEAADLAGA TSSASSKLIH GGLRYLEHYE
FRLVGEALAE REVLLKMAPH LAFPMRFRLP HQPHLRPAWM IRAGLFLYDH LGKRTTLPGS
CGIRFAPQDG LQPDLRRGFE YSDCWVDDAR LVVANARQVV EKGGQVLTRT AVVSAKRENG
LWRVETEQRG PHASGERRVW WARALVNATG PWVKQFFDDS LQAASPRNIR LIKGSHIVVP
RVNSGPQAYI LQNEDHRIVF VIPWLDKFSI IGTTDVEYHG DPRAVQIDET EIDYLLGVYN
RHFSAPLRRE DVRWHYAGVR PLCDDESDSP QAVTRDYTLE LADWSGKAPL LSVFGGKLTT
YRKLAQAAMH RLQPYFPEMG PDWTAQSVLP GGEMDMDRRQ YSEALCRDYP WLPADMAYRY
ACTYGARSRQ ILRGAESLEE LGQHFGHDLY QAEIRYLQTQ EWAQTAEDML WRRTKLGMFL
TGEEQAHLAE WLDKQGKLSA VA
//
