HEPG_ASPOR
ID HEPG_ASPOR Reviewed; 334 AA.
AC Q2U0J7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase B {ECO:0000303|PubMed:30466366};
DE Short=GAPDH {ECO:0000303|PubMed:30466366};
DE EC=1.2.1.12 {ECO:0000269|PubMed:30466366};
DE AltName: Full=Heptelidic acid biosynthesis cluster protein G {ECO:0000303|PubMed:30466366};
GN Name=hepG {ECO:0000303|PubMed:30466366};
GN Synonyms=gpdB {ECO:0000303|PubMed:30466366}; ORFNames=AO090011000414;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=30466366; DOI=10.1080/09168451.2018.1549934;
RA Shinohara Y., Nishimura I., Koyama Y.;
RT "Identification of a gene cluster for biosynthesis of the sesquiterpene
RT antibiotic, heptelidic acid, in Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 83:1506-1513(2019).
CC -!- FUNCTION: Glyceraldehyde-3-phosphate dehydrogenase; part of the gene
CC cluster that mediates the biosynthesis of heptelidic acid (HA), a
CC sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-
CC phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-
CC tolerant lactic acid bacteria in soy sauce brewing (PubMed:30466366).
CC The GAPDPH hepG/gdpB shows much higher resistance to HA than the GAPDH
CC gpdA located outside of the cluster, but it does not seem to act in
CC self-resistance (PubMed:30466366). {ECO:0000269|PubMed:30466366}.
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:0000269|PubMed:30466366};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10301;
CC Evidence={ECO:0000269|PubMed:30466366};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for glyceraldehyde-3-phosphate (GAP)
CC {ECO:0000269|PubMed:30466366};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000255|RuleBase:RU361160}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|RuleBase:RU361160}.
CC -!- DISRUPTION PHENOTYPE: Does not affect the biosynthesis of heptelidic
CC acid. {ECO:0000269|PubMed:30466366}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AP007171; BAE64918.1; -; Genomic_DNA.
DR RefSeq; XP_001826051.1; XM_001825999.2.
DR AlphaFoldDB; Q2U0J7; -.
DR SMR; Q2U0J7; -.
DR STRING; 510516.Q2U0J7; -.
DR EnsemblFungi; BAE64918; BAE64918; AO090011000414.
DR GeneID; 5998154; -.
DR KEGG; aor:AO090011000414; -.
DR VEuPathDB; FungiDB:AO090011000414; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR OMA; NAKVLAW; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000006564; Chromosome 7.
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 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 Glycolysis; NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Glyceraldehyde-3-phosphate dehydrogenase B"
FT /id="PRO_0000450834"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-3"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-3"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-2"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-2"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-2"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-2"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-3"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000255|PIRSR:PIRSR000149-4"
SQ SEQUENCE 334 AA; 36080 MW; D0618E15F55AA6CF CRC64;
MTAKVGINGF GRIGRIVFRN SFSHENTEVV MVNDPFIEVQ YAAYMLKYDS THGNFEYDVH
IDGDSIVVNG KKVKFYAEKD PAKIPWKDAG AEYIIESTGV FTTVEKASAH LQGGAKKVII
SAPSADAPMY VMGVNEKTYA GADVVSNASC TTNCLAPLTK VLHERFGVVE GLMTAVHAYT
ATQKLVDAPS KKDWRGGRAA AQNLIPSSTG AAKAVGKVIP ELQGKVTGMS IRVPTSNVSV
VDLTCRLEKG ASYEEIITAI KEAAQGELKG ILDYTEDDVV SSDMKGNPHS SIVDIKAGIS
LNPNFLKIVS WYDNEWGYSR RVLDLTAYIA SVGK
