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Database: UniProt
Entry: A0A0Q4QBL8_9BACL
LinkDB: A0A0Q4QBL8_9BACL
Original site: A0A0Q4QBL8_9BACL 
ID   A0A0Q4QBL8_9BACL        Unreviewed;       386 AA.
AC   A0A0Q4QBL8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Glycerol-1-phosphate dehydrogenase {ECO:0000313|EMBL:KQN97874.1};
GN   ORFNames=ASF12_20925 {ECO:0000313|EMBL:KQN97874.1};
OS   Paenibacillus sp. Leaf72.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQN97874.1, ECO:0000313|Proteomes:UP000051722};
RN   [1] {ECO:0000313|EMBL:KQN97874.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQN97874.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN97874.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQN97874.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQN97874.1}.
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DR   EMBL; LMLV01000033; KQN97874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4QBL8; -.
DR   STRING; 1736234.ASF12_20925; -.
DR   Proteomes; UP000051722; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051722}.
SQ   SEQUENCE   386 AA;  41282 MW;  FA3F4CB125B8FAC0 CRC64;
     MEKFKLAAAG YDASSVQSIV IEPLLIERGA TQQVAPYLVK KGYRKVLIVS DNITYEIAGK
     QLEAAIAAKD IAVKATLIKP NQQGDVIADE VSIVQLLLDI QHYAAEVVIA AGSGTLHDIT
     RYAAFTAGIP FVSVPTAPSV DGFNSKGAPI IIRGEKITIA AIGPDAIFAD LDVLTQAPVA
     MVAAGFGDML GKYTSLFDWS YGSLAGEEAY SDIVATITRD ALMQCVENVE LIASRSEEGI
     RALISALIES GLAMLLFGQS HSASGAEHHL SHYWEMEYIR LGNRQLLHGA KVGVACAEIS
     GLYHRLADEQ APAISGTEHA ERISQLIAEI PNEETIRGWL KQVGGPSTTA ELGVSDELLA
     RSLSEAHLVR PNRYTLLRAY NEGAGK
//
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