ID   A0A0N1LCE9_9PROT        Unreviewed;       334 AA.
AC   A0A0N1LCE9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 14.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394};
DE            EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394};
DE   AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394};
GN   Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394};
GN   ORFNames=IP84_08310 {ECO:0000313|EMBL:KPF68784.1};
OS   beta proteobacterium AAP99.
OC   Bacteria; Proteobacteria; Betaproteobacteria.
OX   NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF68784.1, ECO:0000313|Proteomes:UP000037960};
RN   [1] {ECO:0000313|EMBL:KPF68784.1, ECO:0000313|Proteomes:UP000037960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP99 {ECO:0000313|EMBL:KPF68784.1,
RC   ECO:0000313|Proteomes:UP000037960};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome
RT   Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) =
CC       glycerone phosphate + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU000439, ECO:0000256|SAAS:SAAS00764424}.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism. {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764395}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764434}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_00394,
CC       ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00649394}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPF68784.1}.
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DR   EMBL; LJIA01000007; KPF68784.1; -; Genomic_DNA.
DR   RefSeq; WP_054125636.1; NZ_LJIA01000007.1.
DR   EnsemblBacteria; KPF68784; KPF68784; IP84_08310.
DR   PATRIC; fig|1523428.3.peg.3234; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000037960; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0036439; F:glycerol-3-phosphate dehydrogenase [NADP+] 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:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
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   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; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000037960};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764341};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764443};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764450};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3,
KW   ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00764378};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00809767};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS00764418};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394,
KW   ECO:0000256|SAAS:SAAS00764387};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037960};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    334       Glycerol-3-phosphate dehydrogenase
FT                                [NAD(P)+]. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005876668.
FT   DOMAIN        5    167       NAD_Gly3P_dh_N. {ECO:0000259|Pfam:
FT                                PF01210}.
FT   DOMAIN      188    322       NAD_Gly3P_dh_C. {ECO:0000259|Pfam:
FT                                PF07479}.
FT   NP_BIND       8     13       NAD. {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   REGION      263    264       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00394, ECO:0000256|PIRSR:
FT                                PIRSR000114-2}.
FT   ACT_SITE    199    199       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00394, ECO:0000256|PIRSR:PIRSR000114-
FT                                1}.
FT   BINDING     116    116       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00394}.
FT   BINDING     116    116       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00394, ECO:0000256|PIRSR:PIRSR000114-
FT                                2}.
FT   BINDING     148    148       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     263    263       NAD. {ECO:0000256|HAMAP-Rule:MF_00394,
FT                                ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     284    284       NAD. {ECO:0000256|HAMAP-Rule:MF_00394}.
SQ   SEQUENCE   334 AA;  34244 MW;  A540671DCE614215 CRC64;
     MNHLVVVGAG SWGTALAMAA LRSAAFFSAA GDQPPAARVT LLARDAAQAA AMQAQRENAR
     YLSGIALPAA LHISADAAVL HDASLVLLVT PFAGLREWFE RLGTLGHAAP VLWAAKGMDA
     QSGEMAHELA ARLLPGRACG VVSGPSFASE VARGLPCALT VASSSEALQQ LGSQWLHGST
     LRVYRSADVT GVEVGGAVKN VIAIATGMCD GLNLGLNARA ALITRGLAEM SRFAVALGAK
     PETLAGLTGL GDLILTATGE LSRNRRYGLE FARDGHAHGG FLAEGARCAR AVQHRAAALG
     IEMPITACVA DIVEGRLSPP AAAQQLLARA ARAE
//