ID   A0A2A4JAM7_HELVI        Unreviewed;       364 AA.
AC   A0A2A4JAM7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   20-JUN-2018, entry version 5.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE            EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN   ORFNames=B5V51_4446 {ECO:0000313|EMBL:PCG69167.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
OC   Noctuoidea; Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG69167.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG69167.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG69167.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG69167.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis
RT   virescens, in response to modern agricultural practices.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(+) = glycerone
CC       phosphate + NADH. {ECO:0000256|RuleBase:RU361243}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU361243}.
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:PCG69167.1}.
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DR   EMBL; NWSH01002106; PCG69167.1; -; Genomic_DNA.
DR   Proteomes; UP000218220; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1040.10; -; 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; IPR017751; G3P_DH_NAD-dep_euk.
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   TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000218220};
KW   NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU361243};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361243};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218220}.
FT   DOMAIN       10    177       NAD_Gly3P_dh_N. {ECO:0000259|Pfam:
FT                                PF01210}.
FT   DOMAIN      199    343       NAD_Gly3P_dh_C. {ECO:0000259|Pfam:
FT                                PF07479}.
FT   NP_BIND      14     19       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   REGION      273    274       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000114-2}.
FT   ACT_SITE    209    209       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000114-1}.
FT   BINDING     101    101       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     124    124       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000114-2}.
FT   BINDING     158    158       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     273    273       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     300    300       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000114-3}.
FT   BINDING     302    302       NAD. {ECO:0000256|PIRSR:PIRSR000114-3}.
SQ   SEQUENCE   364 AA;  39998 MW;  DDC294D94B0F9B2F CRC64;
     MAEKTLKNRV CIIGSGNWGS AIAKIVGKNA ARLPNFEDRV TMWVYEEMIE GKKLTEIINE
     THENVKYLPG HKLPPNVVAI PDVVEAAKDA DLLIFVVPHQ FVRTICSTLL GKIKPTAAAL
     SLIKGFDIAE GGGIDLISHI ITRCLKIPCA VLMGANIASE VADEKFCETT IGCRDVMLAP
     MMRDIIQTEY FRVVVVDDED AVEICGALKN IVAVGAGFVD GLGFGDNTKA AVIRLGLMEM
     IKFVDVFYPG SKLSTFFESC GVADLITTCY GGRNRRVAEA FVKTGRSIKE LEDEMLNGQK
     LQGPITAEEV NHMLANKNME NKFPLFTAVF RICRGELKPS DFINCIRSHP EHMTRKQSAP
     KCSL
//