ID A0A1I6SF38_9BACL Unreviewed; 364 AA.
AC A0A1I6SF38;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000313|EMBL:SFS75543.1};
GN ORFNames=SAMN05444972_10736 {ECO:0000313|EMBL:SFS75543.1};
OS Marininema halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1155944 {ECO:0000313|EMBL:SFS75543.1, ECO:0000313|Proteomes:UP000198660};
RN [1] {ECO:0000313|EMBL:SFS75543.1, ECO:0000313|Proteomes:UP000198660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45789 {ECO:0000313|EMBL:SFS75543.1,
RC ECO:0000313|Proteomes:UP000198660};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPAA01000007; SFS75543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6SF38; -.
DR OrthoDB; 9763580at2; -.
DR Proteomes; UP000198660; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
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 Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
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 250
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 266
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 364 AA; 39876 MW; 679161770D8E8D63 CRC64;
MAKKVHIPLQ LIIEHEAIPK LYKSPIGSWI QGARILLISG SGSTRKVTEK ISNAIEGYAS
EVSVLTCQDN KLDTINDIER QVLEDTPDLI FGVGGGKALD MSKVVGTRSN VPVVLFPTAI
SSDAICSPVA VIKMMSQSTS IGVKMPQAVV IDLDVLTSCP PRLMSAGIGD LLSNKTALYD
WKLAHQAGKE EMNTFANLMA NNAVDSFMNL LNRPELNQSQ LMKVAAEALI MSGIAMSIAG
SSRPCSGSEH LISHALDYHC GAKALHGEQV AIGVLFSQYL QGQQEKIEKL TPYYEKLGLP
THYADLGYTR EEMHRAIVKA PSMRDRYTIF DEFNLTEDRI DRIMDEVYPD QAKNRYCLTG
LSVG
//
