ID G1PDH_THESM Reviewed; 350 AA. AC C6A2E4; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 16-MAY-2012, entry version 23. DE RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+]; DE Short=G1P dehydrogenase; DE Short=G1PDH; DE EC=1.1.1.261; DE AltName: Full=Enantiomeric glycerophosphate synthase; DE AltName: Full=sn-glycerol-1-phosphate dehydrogenase; GN Name=egsA; OrderedLocusNames=TSIB_0726; OS Thermococcus sibiricus (strain MM 739 / DSM 12597). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=604354; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MM 739 / DSM 12597; RX PubMed=19447963; DOI=10.1128/AEM.00718-09; RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.; RT "Metabolic versatility and indigenous origin of the archaeon RT Thermococcus sibiricus, isolated from a siberian oil reservoir, as RT revealed by genome analysis."; RL Appl. Environ. Microbiol. 75:4580-4588(2009). CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of CC dihydroxyacetonephosphate (DHAP or glycerone phosphate) to CC glycerol-1-phosphate (G1P). The G1P thus generated is used as the CC glycerophosphate backbone of phospholipids in the cellular CC membranes of Archaea (By similarity). CC -!- CATALYTIC ACTIVITY: sn-glycerol-1-phosphate + NAD(P)(+) = CC glycerone phosphate + NAD(P)H. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase CC family. 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; CP001463; ACS89789.1; -; Genomic_DNA. DR RefSeq; YP_002994138.1; NC_012883.1. DR ProteinModelPortal; C6A2E4; -. DR STRING; C6A2E4; -. DR GeneID; 8095715; -. DR GenomeReviews; CP001463_GR; TSIB_0726. DR KEGG; tsi:TSIB_0726; -. DR eggNOG; COG0371; -. DR HOGENOM; HOG000228570; -. DR KO; K00096; -. DR OMA; CGVGTIM; -. DR ProtClustDB; PRK00843; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050492; F:glycerol-1-phosphate dehydrogenase [NAD(P)+] activity; IEA:EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1; -. DR InterPro; IPR023002; G1P_dehydrogenase_arc. DR InterPro; IPR016205; Glycerol_DH. DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Metal-binding; NAD; NADP; KW Oxidoreductase; Phospholipid biosynthesis; Zinc. FT CHAIN 1 350 Glycerol-1-phosphate dehydrogenase FT [NAD(P)+]. FT /FTId=PRO_1000206482. FT NP_BIND 97 101 NAD (By similarity). FT NP_BIND 119 122 NAD (By similarity). FT METAL 171 171 Zinc; catalytic (By similarity). FT METAL 251 251 Zinc; catalytic (By similarity). FT METAL 267 267 Zinc; catalytic (By similarity). FT BINDING 124 124 Substrate (By similarity). FT BINDING 128 128 NAD (By similarity). FT BINDING 171 171 Substrate (By similarity). FT BINDING 255 255 Substrate (By similarity). SQ SEQUENCE 350 AA; 38069 MW; 74DD6AA862A25B71 CRC64; MVMFMHLMEL PREVLLGEDL KDKVSQVAKR LKLGENVLIL YGPKTKEIAG KDIEKHLKEF FHVKNLLIKE ASMKNVQKAL EIIRNENIDW LLGVGGGSII DVAKLASFKA DVPFISFPTT ASHDGIASAN ASIRDLGAKT SIKARPPVAV IADVNIIKTA PYRYLAAGVG DMVSNLTAVK DWELAHRIRG EYFSEYAASL SLMSAKMVIK NADIIRLSNE ESVRKVIKAL ISSGVAMSIA GSSRPASGAE HLFSHALDAI APKPALHGEQ CGVGTIIMAY LHGLNWKKIR ETLKRVGAPT NAYELEIDPG FIIEALTIAH TIRPERYTIL GKDGLTKEAA EKAAKITGVI //