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Database: UniProt
Entry: A0A2C1Z2V0_9BACI
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Original site: A0A2C1Z2V0_9BACI 
ID   A0A2C1Z2V0_9BACI        Unreviewed;       413 AA.
AC   A0A2C1Z2V0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=sn-glycerol-1-phosphate dehydrogenase {ECO:0000313|EMBL:PGV51730.1};
GN   ORFNames=COD92_12830 {ECO:0000313|EMBL:PGV51730.1};
OS   Bacillus sp. AFS037270.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV51730.1, ECO:0000313|Proteomes:UP000225442};
RN   [1] {ECO:0000313|EMBL:PGV51730.1, ECO:0000313|Proteomes:UP000225442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS037270 {ECO:0000313|EMBL:PGV51730.1,
RC   ECO:0000313|Proteomes:UP000225442};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PGV51730.1}.
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DR   EMBL; NUNF01000024; PGV51730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1Z2V0; -.
DR   Proteomes; UP000225442; 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; cd08175; G1PDH; 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   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   NAD {ECO:0000256|ARBA:ARBA00023027}; 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}.
SQ   SEQUENCE   413 AA;  45529 MW;  F023CB0552472C32 CRC64;
     MEKIITEIMS LANSCDCGNH HNQIPIETIL VGNNVLGEAA AYLEKKAFKK AVIIADEQTF
     RAAGEELSKH LSTTKVVYST CLLQPDENNN VVADEKSLVQ AKLETSQDTE VILAVGSGTI
     HDIARFTSTK MKIPFISIPT APSVDGFTSM GAPIIVRGMK KTFQMMAPIA VFADLGILRD
     APKKMIAAGF GDMLAKYTSL ADWKFGHLTY GEPYCPLVAN ITREALQLCV EKADKIAAAD
     EEGIRILIEA LIQSGLAMLL FGQSHPASGG EHHLSHYWEM EFLRQNRPQV LHGAKVGVAV
     ALLADVYERE FIPAISVLRK LDDTIKTVED YCIVRNIKEN IEEIKAVYAA IPKASQLREL
     IEKVGGEILP SQLGIDGDLI MRSLTEAHHL RNRFTALKFL NEVIKVNHQE VVR
//
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