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Entry: A0A3S5EV86_9ACTN
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ID   A0A3S5EV86_9ACTN        Unreviewed;       347 AA.
AC   A0A3S5EV86;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU000439};
DE            EC=1.1.1.94 {ECO:0000256|RuleBase:RU000439};
GN   Name=gpsA_1 {ECO:0000313|EMBL:VEI03451.1};
GN   ORFNames=C0Z10_00265 {ECO:0000313|EMBL:AZZ38444.1}, FEZ32_04940
GN   {ECO:0000313|EMBL:QCV87804.1}, NCTC13652_01656
GN   {ECO:0000313|EMBL:VEI03451.1};
OS   Acidipropionibacterium jensenii.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Acidipropionibacterium.
OX   NCBI_TaxID=1749 {ECO:0000313|EMBL:VEI03451.1, ECO:0000313|Proteomes:UP000277858};
RN   [1] {ECO:0000313|Proteomes:UP000285875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS280 {ECO:0000313|Proteomes:UP000285875};
RA   Deptula P., Laine P., Smolander O.-P., Paulin L., Auvinen P., Varmanen P.;
RT   "Whole genome sequencing of Acidipropionibacterium jensenii strains JS279
RT   and JS280.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:VEI03451.1, ECO:0000313|Proteomes:UP000277858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13652 {ECO:0000313|EMBL:VEI03451.1,
RC   ECO:0000313|Proteomes:UP000277858};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AZZ38444.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JS280 {ECO:0000313|EMBL:AZZ38444.1};
RX   PubMed=31671651;
RA   Deptula P., Loivamaa I., Smolander O.P., Laine P., Roberts R.J.,
RA   Piironen V., Paulin L., Savijoki K., Auvinen P., Varmanen P.;
RT   "Red-Brown Pigmentation of Acidipropionibacterium jensenii Is Tied to
RT   Haemolytic Activity and cyl-Like Gene Cluster.";
RL   Microorganisms 7:0-E512(2019).
RN   [4] {ECO:0000313|EMBL:QCV87804.1, ECO:0000313|Proteomes:UP000310120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FAM 19038 {ECO:0000313|EMBL:QCV87804.1,
RC   ECO:0000313|Proteomes:UP000310120};
RA   Roder T., Wuthrich D., Sattari Z., von Ah U., Bar C., Ronchi F.,
RA   Macpherson A.J., Ganal-Vonarburg S.C., Bruggmann R., Vergeres G.;
RT   "The metagenome of a microbial culture collection derived from dairy
RT   environment covers the genomic content of the human microbiome.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.94;
CC         Evidence={ECO:0000256|RuleBase:RU000439};
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC       ECO:0000256|RuleBase:RU000437}.
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DR   EMBL; CP025570; AZZ38444.1; -; Genomic_DNA.
DR   EMBL; CP040635; QCV87804.1; -; Genomic_DNA.
DR   EMBL; LR134473; VEI03451.1; -; Genomic_DNA.
DR   RefSeq; WP_028701948.1; NZ_LR134473.1.
DR   AlphaFoldDB; A0A3S5EV86; -.
DR   STRING; 1122997.GCA_000425285_00024; -.
DR   GeneID; 82884424; -.
DR   KEGG; aji:C0Z10_00265; -.
DR   OrthoDB; 9812273at2; -.
DR   Proteomes; UP000277858; Chromosome 1.
DR   Proteomes; UP000285875; Chromosome.
DR   Proteomes; UP000310120; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000437};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277858}.
FT   DOMAIN          5..167
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          188..332
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         266..267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         266
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ   SEQUENCE   347 AA;  35861 MW;  90642954757D2680 CRC64;
     MPTFTVLGAG AMGTALCKPF IDAGWEVRLW GTWLDDHLID AIEAGQPHPR IKVAAAPGIR
     TFRSGQLAEA LEGADVVDIA VTSEGLPRVT EMALDHIAGL RALCLTAKGF WTDPEGRIRL
     LPDAIRAIAD QKGVSLPPLV AVGGPVKANE CAAGEVTATT YASRDLALAE TLAREAATDT
     YGIRPSDDET GVELCAALKN VYAISLGIAD GLGEATGVPR HNLKAAAFAQ AIREMSLLVA
     AVGGHSETPY GLAGVGDLEV TGLSGRNKLY GVRLGKGETP DGALAEMNRL EQTVEGYPAA
     PLAVAFAHQA GADEGTLPLL HAVARILQGG VDDVYAAVAA AVKPARP
//
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