ID A0A2S0VNZ4_9ALTE Unreviewed; 497 AA.
AC A0A2S0VNZ4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:AWB65936.1};
GN ORFNames=C2869_05535 {ECO:0000313|EMBL:AWB65936.1};
OS Saccharobesus litoralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Saccharobesus.
OX NCBI_TaxID=2172099 {ECO:0000313|EMBL:AWB65936.1, ECO:0000313|Proteomes:UP000244441};
RN [1] {ECO:0000313|EMBL:AWB65936.1, ECO:0000313|Proteomes:UP000244441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-QB4 {ECO:0000313|EMBL:AWB65936.1,
RC ECO:0000313|Proteomes:UP000244441};
RA Tan W.R., Lau N.-S., Go F., Amirul A.-A.A.;
RT "Genome sequence of a Cantenovulum-like bacteria.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR EMBL; CP026604; AWB65936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0VNZ4; -.
DR KEGG; cate:C2869_05535; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000244441; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000244441}.
FT DOMAIN 12..365
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 386..486
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 497 AA; 55549 MW; FEE0A81CBCC9455D CRC64;
MEKNSLRSTD YDICIIGGGI NGVGIAREAA LQGLKVCLLE QNDLASGTSS ASSKLIHGGL
RYLEHFEFGL VKKALAEREV LLNMAPHIIW PLSFVLPHQS HLRPAWLIRI GLFLYDNLAK
RSILPSSRVL QFDESSPLQS HIQHGFEYAD AWVDDARLVV LNALAASELG ADIYNYTRCV
NAKAVAGVWR VTLQATATEL PQTITARMVI NAAGPWVNNV FEQVLQQPIE HQIRLVKGSH
IIVPKLHEQN KAYILQNADK RIVFVLPYEQ DFSLIGTTDI EFKGELQQVS SSEAENRYLI
ESVNSYFKTQ LQIQDIVSSY AGVRPLLSDA AEQAQKVTRD YKLALDNQGS APLLSVYGGK
ITTYRKLAHE AMQLIADVFT IQLPRITSEL SLPGGDFTCI NALQGEIEGR YQWLPSQLLQ
RLLRSYGTRC FDILGDSQTL EALGMDFGHG LYQAEVDYLL DTEFAKTLDD ILWRRSKLGL
RLEVAQRNAL ADYINSC
//
