ID GLPD_STAES Reviewed; 557 AA. AC Q8CPE6; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase; DE EC=1.1.5.3; GN Name=glpD; OrderedLocusNames=SE_0979; OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=176280; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12228 / FDA PCI 1200; RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x; RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.; RT "Genome-based analysis of virulence genes in a non-biofilm-forming RT Staphylococcus epidermidis strain (ATCC 12228)."; RL Mol. Microbiol. 49:1577-1593(2003). 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 -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic CC route): step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000305}. 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; AE015929; AAO04576.1; -; Genomic_DNA. DR RefSeq; NP_764534.1; NC_004461.1. DR RefSeq; WP_002439581.1; NZ_WBME01000001.1. DR AlphaFoldDB; Q8CPE6; -. DR SMR; Q8CPE6; -. DR KEGG; sep:SE_0979; -. DR PATRIC; fig|176280.10.peg.953; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_015740_5_2_9; -. DR OrthoDB; 9766796at2; -. DR UniPathway; UPA00618; UER00674. DR Proteomes; UP000001411; 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:UniProtKB-EC. DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro. 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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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 Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase. FT CHAIN 1..557 FT /note="Aerobic glycerol-3-phosphate dehydrogenase" FT /id="PRO_0000270066" FT BINDING 21..49 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255" SQ SEQUENCE 557 AA; 62276 MW; 6F6044C656324F7C CRC64; MSLSTLKRDH IKKNLRDTEY DVVIVGGGIT GAGIALDASN RGMKVALVEM QDFAQGTSSR STKLVHGGLR YLKQLQVGVV AETGKERAIV YENGPHVTTP EWMLLPMHKG GTFGKFSTSI GLAMYDRLAG VKKSERKKML SKQETLNKEP LVKRDGLKGG GYYVEYRTDD ARLTIEVMKK AAENGAEILN YTKSEHFTYD SNKKVNGIEV LDMIDGETYA IKAKKVINAS GPWVDEVRSG DYARNNKQLR LTKGVHVVID QSKFPLGQAV YFDTEKDGRM IFAIPREGKA YVGTTDTFYD NEKATPLTTQ EDRDYLINAI NYMFPTVNVK DEDIESTWAG IRPLILEKGK DPSEISRKDE VWEGESGLLT IAGGKLTGYR HMALEIVDLL AKRLKQEYGL KFESCATKNL KISGGDVGGS KNFEHFVEQK VDAAKGFGID EDVARRLASK YGSNVDQLFN IAQTAPYHDS KLPLEIYVEL VYSIQQEMVY KPTDFLVRRS GKLYFNIQDV LDYKNAVIDV MADMLNYSET QKEAYTEEVE VAIDEARTGN DQPATKA //