ID   R4J9F1_9HEMI            Unreviewed;       332 AA.
AC   R4J9F1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   06-JUL-2016, entry version 16.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
OS   Macrosteles quadripunctulatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Paraneoptera; Hemiptera; Euhemiptera;
OC   Membracoidea; Cicadellidae; Deltocephalinae; Macrosteles.
OX   NCBI_TaxID=1128428 {ECO:0000313|EMBL:AGJ71762.1};
RN   [1] {ECO:0000313|EMBL:AGJ71762.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Galetto L., Marzachi C., Bosco D.;
RT   "Determining housekeeping genes in two leafhopper vector species
RT   challenged by phytoplasma infection.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC       {ECO:0000256|RuleBase:RU361160}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC       {ECO:0000256|RuleBase:RU361160}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU361160}.
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DR   EMBL; JX273237; AGJ71762.1; -; mRNA.
DR   UniPathway; UPA00109; UER00184.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR10836; PTHR10836; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis {ECO:0000256|RuleBase:RU361160};
KW   NAD {ECO:0000256|RuleBase:RU361160};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361160}.
FT   DOMAIN        2    149       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
FT   ACT_SITE    149    149       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR000149-1}.
FT   SITE        176    176       Activates thiol group during catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000149-4}.
SQ   SEQUENCE   332 AA;  35511 MW;  4EB990DBEFA68EEE CRC64;
     MWKIGINGFG RIGRLVLRAS LERGGQVVAI NDPFIGLDYM VYMFKHDSTH GRFKGEVKAE
     GDFLVVNGNK IAVFSERDPK AIPWGKAGAE YVVESTGVFT TIDKASAHLE GGAKKVIISA
     PSADAPMFVV GVNLDAYDPS YKVVSNASCT TNCLAPLAKV VHDNFEIVEG LMTTVHATTA
     TQKTVDGPSG KLWRDGRGAQ QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPVPNVSVV
     DLTVXLGKEA SYDDIKAKVK EAAEGPLKGI LGYTEDDVVS SDFVGDNHSS IFDAKAGIPL
     NGKFVKLISW YDNEFGYSSR VIDLIKYIQS KD
//