G3P_EMENI
ID G3P_EMENI Reviewed; 336 AA.
AC P20445; C8V605; P41763; Q5AUI9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
GN Name=gpdA; ORFNames=AN8041;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3066699; DOI=10.1016/0378-1119(88)90377-0;
RA Punt P.J., Dingemanse M.A., Jacobs-Meijsing B.J.M., Pouwels P.H.,
RA van den Hondel C.A.M.J.J.;
RT "Isolation and characterization of the glyceraldehyde-3-phosphate
RT dehydrogenase gene of Aspergillus nidulans.";
RL Gene 69:49-57(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2121607; DOI=10.1016/0378-1119(90)90142-e;
RA Punt P.J., Dingemanse M.A., Kuyvenhoven A., Soede R.D., Pouwels P.H.,
RA van den Hondel C.A.M.J.J.;
RT "Functional elements in the promoter region of the Aspergillus nidulans
RT gpdA gene encoding glyceraldehyde-3-phosphate dehydrogenase.";
RL Gene 93:101-109(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA Kim Y., Nandakumar M.P., Marten M.R.;
RT "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL Fungal Genet. Biol. 44:886-895(2007).
CC -!- FUNCTION: Involved in osmoadaptation.
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:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Up-regulated when grown with elevated levels of potassium
CC chloride. {ECO:0000269|PubMed:17258477}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA59663.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M19694; AAA33307.1; -; Genomic_DNA.
DR EMBL; M33539; AAA33308.1; -; Genomic_DNA.
DR EMBL; AACD01000139; EAA59663.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF73760.1; -; Genomic_DNA.
DR PIR; JT0344; DEASG3.
DR RefSeq; XP_681310.1; XM_676218.1.
DR AlphaFoldDB; P20445; -.
DR SMR; P20445; -.
DR STRING; 162425.CADANIAP00004062; -.
DR PRIDE; P20445; -.
DR EnsemblFungi; CBF73760; CBF73760; ANIA_08041.
DR EnsemblFungi; EAA59663; EAA59663; AN8041.2.
DR GeneID; 2868966; -.
DR KEGG; ani:AN8041.2; -.
DR VEuPathDB; FungiDB:AN8041; -.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_1_1; -.
DR InParanoid; P20445; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 945145at2759; -.
DR SABIO-RK; P20445; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IMP:AspGD.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEP:AspGD.
DR GO; GO:0006094; P:gluconeogenesis; ISA:AspGD.
DR GO; GO:0006096; P:glycolytic process; ISA:AspGD.
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 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase; Reference proteome;
KW Stress response.
FT CHAIN 1..336
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145554"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 210..211
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 178
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 36311 MW; C274CA4DE954B8D8 CRC64;
MAPKVGINGF GRIGRIVFRN AIEAGTVDVV AVNDPFIETH YAAYMLKYDS QHGQFKGTIE
TYDEGLIVNG KKIRFHTERD PANIPWGQDG AEYIVESTGV FTTQEKASAH LKGGAKKVVI
SAPSADAPMF VMGVNNETYK KDIQVLSNAS CTTNCLAPLA KVINDNFGII EGLMTTVHSY
TATQKVVDGP SAKDWRGGRT AATNIIPSST GAAKAVGKVI PSLNGKLTGM AMRVPTSNVS
VVDLTVRTEK AVTYDQIKDA VKKASENELK GILGYTEDDI VSTDLNGDTR SSIFDAKAGI
ALNSNFIKLV SWYDNEWGYS RRVVDLITYI SKVDAQ
