ID A0A142XLD0_9BACT Unreviewed; 349 AA.
AC A0A142XLD0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000313|EMBL:AMV27797.1};
DE EC=1.1.1.261 {ECO:0000313|EMBL:AMV27797.1};
GN Name=egsA {ECO:0000313|EMBL:AMV27797.1};
GN ORFNames=VT84_25570 {ECO:0000313|EMBL:AMV27797.1};
OS Gemmata sp. SH-PL17.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Gemmata.
OX NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV27797.1, ECO:0000313|Proteomes:UP000076098};
RN [1] {ECO:0000313|EMBL:AMV27797.1, ECO:0000313|Proteomes:UP000076098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV27797.1,
RC ECO:0000313|Proteomes:UP000076098};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-1};
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DR EMBL; CP011271; AMV27797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142XLD0; -.
DR STRING; 1630693.VT84_25570; -.
DR KEGG; ges:VT84_25570; -.
DR PATRIC; fig|1630693.3.peg.5442; -.
DR OrthoDB; 9763580at2; -.
DR Proteomes; UP000076098; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0050492; F:glycerol-1-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08174; G1PDH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR032837; G1PDH.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR PANTHER; PTHR43616:SF5; GLYCEROL DEHYDROGENASE 1; 1.
DR Pfam; PF13685; Fe-ADH_2; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000112-1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000112-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AMV27797.1};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000076098};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT BINDING 96..100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 118..121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 123
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-2"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 170
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 246
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 262
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 349 AA; 37295 MW; 51AC5085105E6684 CRC64;
MLRPTQIAIP TLVRAKAGAL DRLGRYLDRS GHRRVAVAMS QGLAPPLPDR VTSSLKEQSV
EAAAWIEVAD NGLESTVRAF ADLPKGVTAI VGVGGGKALD VAKYIAFLGR LPYFAVPTSL
SNDGFCSPQS SLTVRGARRS LPAALPFGVI VDTAVCLGAP RVLTLSGVGD LVAKFTAIRD
WKLAFHAKGE PIDDFATLMS DGTIYSFMSH PAIDLEGIRL LATALLLNGI AMEICGSSRP
ASGSEHLISH ALDATSARPR LHGLQVGVAT YLVSVLQGDN TERIAALFDS TGFWDVIAAD
PFSREEWMTA VRKAPSIKEG YYTVLSSRDA VPEVEHLLNS DPRLVRCFQ
//
