PGK_CORGL
ID PGK_CORGL Reviewed; 405 AA.
AC Q01655;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=Cgl1587, cg1790;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX PubMed=1400158; DOI=10.1128/jb.174.19.6076-6086.1992;
RA Eikmanns B.J.;
RT "Identification, sequence analysis, and expression of a Corynebacterium
RT glutamicum gene cluster encoding the three glycolytic enzymes
RT glyceraldehyde-3-phosphate dehydrogenase, 3-phosphoglycerate kinase, and
RT triosephosphate isomerase.";
RL J. Bacteriol. 174:6076-6086(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X59403; CAA42046.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98980.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21595.1; -; Genomic_DNA.
DR PIR; B43260; B43260.
DR RefSeq; NP_600801.1; NC_003450.3.
DR RefSeq; WP_003862252.1; NC_006958.1.
DR AlphaFoldDB; Q01655; -.
DR SMR; Q01655; -.
DR STRING; 196627.cg1790; -.
DR World-2DPAGE; 0001:Q01655; -.
DR KEGG; cgb:cg1790; -.
DR KEGG; cgl:Cgl1587; -.
DR PATRIC; fig|196627.13.peg.1549; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_11; -.
DR OMA; DMIFDIG; -.
DR BRENDA; 2.7.2.3; 960.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000582; Chromosome.
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-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 2.
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..405
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145937"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
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 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 361..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 67..68
FT /note="PK -> Q (in Ref. 1; CAA42046)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..137
FT /note="TA -> NR (in Ref. 1; CAA42046)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..265
FT /note="RFG -> SV (in Ref. 1; CAA42046)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..350
FT /note="GIAQAIIDAT -> ASPRPSSMQH (in Ref. 1; CAA42046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 42697 MW; FDA8894290A9B7DE CRC64;
MAVKTLKDLL DEGVDGRHVI VRSDFNVPLN DDREITDKGR IIASLPTLKA LSEGGAKVIV
MAHLGRPKGE VNEKYSLAPV AEALSDELGQ YVALAADVVG EDAHERANGL TEGDILLLEN
VRFDPRETSK DEAERTAFAQ ELAALAADNG AFVSDGFGVV HRAQTSVYDI AKLLPHYAGG
LVETEISVLE KIAESPEAPY VVVLGGSKVS DKIGVIEALA AKADKIIVGG GMCYTFLAAQ
GHNVQQSLLQ EEMKATCTDL LARFGDKIVL PVDLVAASEF NKDAEKQIVD LDSIPEGWMS
LDIGPESVKN FGEVLSTAKT IFWNGPMGVF EFAAFSEGTR GIAQAIIDAT AGNDAFSVVG
GGDSAASVRV LGLNEDGFSH ISTGGGASLE YLEGKELPGV AILAQ
