ID   R4J9F1_9HEMI            Unreviewed;       332 AA.
AC   R4J9F1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   02-JUN-2021, entry version 36.
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; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Membracoidea;
OC   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 challenged
RT   by phytoplasma infection.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000256|RuleBase:RU361160};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869,
CC       ECO:0000256|RuleBase:RU361160}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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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-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
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   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; IPR036291; NAD(P)-bd_dom_sf.
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|PIRSR:PIRSR000149-3, ECO:0000256|RuleBase:RU361160};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160}.
FT   DOMAIN          2..149
FT                   /note="Gp_dh_N"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NP_BIND         11..12
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   REGION          148..150
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   REGION          208..209
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   ACT_SITE        149
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         32
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         77
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         119
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         179
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         231
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         313
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            176
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="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
//