PGK_ASPOR
ID PGK_ASPOR Reviewed; 417 AA.
AC P41756; Q2U2M7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgkA; ORFNames=AO090038000395;
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 [GENOMIC DNA].
RA Ogawa M., Kitamoto K., Gomi K., Kumagai C., Tamura G.;
RT "Cloning and nucleotide sequence of the phosphoglycerate kinase gene (pgkA)
RT from Aspergillus oryzae.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; D28484; BAA05843.1; -; Genomic_DNA.
DR EMBL; AP007169; BAE64188.1; -; Genomic_DNA.
DR RefSeq; XP_001825321.1; XM_001825269.2.
DR RefSeq; XP_003190640.1; XM_003190592.1.
DR AlphaFoldDB; P41756; -.
DR SMR; P41756; -.
DR STRING; 510516.P41756; -.
DR PRIDE; P41756; -.
DR EnsemblFungi; BAE64188; BAE64188; AO090038000395.
DR GeneID; 5997416; -.
DR KEGG; aor:AO090038000395; -.
DR HOGENOM; CLU_025427_0_0_1; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000006564; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..417
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145875"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64..67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 44383 MW; 6A25309DF5922A5A CRC64;
MSLSNKLAIT DVDLKDKRVL IRVDFNVPLD ADKKITNNQR IVGALPTIKY AIENGAKAVV
LMSHLGRPDG KANPKYSLKP VATELEKLLS KSVIFAENCV GKETEEIVNK ATGGQIILLE
NLRFHAEEEG SSKDAEGKKV KADKEKVEEF RKGLTALGDV YINDAFGTAH RAHSSMVGVD
LPQKASGFLV KKELEYFAKA LESPQRPFLA ILGGAKVSDK IQLIDNLLPK VNSLIITGAM
AFTFKKTLEN VKIGNSLFDE AGSKIVGDIV EKAKKNNVKI VLPVDYVTAD KFAADAKTGY
ATDADGIPDG YMGLDVGEKS VELYKKTIAE AKTILWNGPP GVFELEPFAN ATKKTLDAAV
AAAQSGSIVI IGGGDTATVA AKYGAEAKLS HVSTGGGASL ELLEGKVLPG VDALSSK
