PGK2_RHINI
ID PGK2_RHINI Reviewed; 417 AA.
AC P29406;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Phosphoglycerate kinase 2;
DE EC=2.7.2.3;
GN Name=PGK2;
OS Rhizopus niveus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4844;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 4810 / AS 3.4817;
RX PubMed=8082204; DOI=10.1007/bf00351673;
RA Yanai K., Tanaka N., Horiuchi H., Ohta A., Takagi M.;
RT "Cloning and characterization of two 3-phosphoglycerate kinase genes of
RT Rhizopus niveus and heterologous gene expression using their promoters.";
RL Curr. Genet. 25:524-530(1994).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {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; D10156; BAA01020.1; -; Genomic_DNA.
DR PIR; S44063; S44063.
DR AlphaFoldDB; P29406; -.
DR SMR; P29406; -.
DR PRIDE; P29406; -.
DR UniPathway; UPA00109; UER00185.
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 Transferase.
FT CHAIN 1..417
FT /note="Phosphoglycerate kinase 2"
FT /id="PRO_0000145888"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 44656 MW; 45AC26C03CF01776 CRC64;
MSLSNKLSIR DLDLKNKRVL IRVDFNVPMK DGAITNNNRI VQALPTVKYA LDNGASAVIL
MSHLGRPNGE AVAKYSLKPV AAEVEKLLGK PVEFLNDCVG PDVEKACQSA TGGKVILLEN
LRFHIEEEGS AKVRWSKVKA DAEAVKKFRA SLTALADIYV NDAFGTAHRA HSSMVGVDLS
QRAAGFLMQK ELEYFAKALE NPARPFLAIL GGAKVSDKIQ LIENMLDKVN ALIVCGGMAF
TFKKTLDNVK QIGKSLFDEA GSKLVRNLVK KAAEKNVKLV FPVDFVTADK FAPDANTGYA
TDADGIPDEW EGLDCGKKSS ELFREEILKS KTIVWNGPSG VFEFDAFANG TKSVLNAVIE
ATKEGATTII GGGDTATAAL KWGAEGKVSH ISTGGGASLE LLEGKELPGV TALSSKN