ID   A0A0L0T0E9_ALLMA        Unreviewed;       342 AA.
AC   A0A0L0T0E9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
GN   ORFNames=AMAG_12934 {ECO:0000313|EMBL:KNE68263.1};
OS   Allomyces macrogynus ATCC 38327.
OC   Eukaryota; Fungi; Blastocladiomycota; Blastocladiomycetes;
OC   Blastocladiales; Blastocladiaceae; Allomyces.
OX   NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE68263.1, ECO:0000313|Proteomes:UP000054350};
RN   [1] {ECO:0000313|EMBL:KNE68263.1, ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE68263.1,
RC   ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Heiman D., Howarth C., Larimer J.,
RA   Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of Allomyces macrogynus ATCC 38327.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL   Submitted (NOV-2009) 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; GG745356; KNE68263.1; -; Genomic_DNA.
DR   EnsemblFungi; KNE68263; KNE68263; AMAG_12934.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000054350; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054350};
KW   Glycolysis {ECO:0000256|RuleBase:RU361160};
KW   NAD {ECO:0000256|RuleBase:RU361160};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054350}.
FT   DOMAIN        3    152       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
FT   REGION      151    153       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   REGION      211    212       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   ACT_SITE    152    152       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR000149-1}.
FT   BINDING     182    182       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   BINDING     234    234       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   SITE        179    179       Activates thiol group during catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000149-4}.
SQ   SEQUENCE   342 AA;  36439 MW;  E2D6386A37F76BB5 CRC64;
     MTVKVGINGF GRIGRLVFRA SLENPDVQVV AINDPFIDLE YMTYLLRYDS THGRYKGTIA
     VENGKLVVNG HAITVFNSMK PTEIAWGSAG AVYVVESTGV FLSIEKASQH FQGGAKKVVV
     TAPSPDAPMF VMGVNQDKYD PSTMNVVSNA SCTTNCLAPL AKVINDEFGI VEGLMTTVHA
     TTATQKTVDG PSGKDWRSGR GAAQNIIPAS TGAAKAVGKV IPALNGKLTG MAFRVPTPDV
     SVVDLTVRLA KPATYDQIKA VIKQASQSSL KGILGYTEDA VVSNDFVGDS HSSIFDADAG
     IALNDTFVKL ISWYDNEFGY SCRVIDLVKH IAKKDAEAGL KL
//