PGK_NEUCR
ID PGK_NEUCR Reviewed; 418 AA.
AC P38667; Q7RVG7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk-1; Synonyms=pgk, pgka; ORFNames=NCU07914;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=74A;
RX PubMed=1385737; DOI=10.3109/10425179209020812;
RA Azevedo J.E., Tropschug M., Werner S.;
RT "Primary structure and in vitro expression of the N. crassa
RT phosphoglycerate kinase.";
RL DNA Seq. 2:265-267(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; X56512; CAA39865.1; -; mRNA.
DR EMBL; CM002239; EAA33194.1; -; Genomic_DNA.
DR PIR; A56616; A56616.
DR PIR; T43864; T43864.
DR RefSeq; XP_962430.1; XM_957337.3.
DR AlphaFoldDB; P38667; -.
DR SMR; P38667; -.
DR STRING; 5141.EFNCRP00000008201; -.
DR PRIDE; P38667; -.
DR EnsemblFungi; EAA33194; EAA33194; NCU07914.
DR GeneID; 3878602; -.
DR KEGG; ncr:NCU07914; -.
DR VEuPathDB; FungiDB:NCU07914; -.
DR HOGENOM; CLU_025427_0_0_1; -.
DR InParanoid; P38667; -.
DR OMA; DMIFDIG; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..418
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145883"
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"
FT CONFLICT 70
FT /note="G -> R (in Ref. 1; CAA39865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 45057 MW; 3BDD4B14655D90F2 CRC64;
MSLSNKLSIE DVDLKGKRVL IRVDFNVPLD AEKKVTNPQR IAGAIPTIKY ALDHGAKAVV
LMSHLGRPDG KPNPKYSLKP VVPELEKLLG KKVTFAPDCV GPEVEEIVNK ADNGEVILLE
NLRFHIEEEG KGTDAEGNKV KADKAKVEEF RKNLTKLGDV YINDAFGTAH RAHSSMVGID
LPVKAAGFLM KKELQYFAKV LESPQRPFLS ILGGAKVSDK IQLIDNLLDK VNTLIVCGGM
AFTFKKTLQN MPIGNSLFDE AGAKIVPDLV KKAEKNNVKL VLPVDFTIAD KFDKDANTGY
ATDKDGIPDG WMGLDCGEES VKLFTQAINE SQTILWNGPA GVFEFDKFAK GTKATLDACV
KAAEEGRTVI IGGGDTATVA AKYGVEDKLS HVSTGGGASL ELLEGKALPG VVALSERQ
