PGK_MYCPN
ID PGK_MYCPN Reviewed; 409 AA.
AC P78018;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=MPN_429; ORFNames=MP412;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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:0000305}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; U00089; AAB96060.1; -; Genomic_DNA.
DR PIR; S73738; S73738.
DR RefSeq; NP_110117.1; NC_000912.1.
DR RefSeq; WP_010874785.1; NC_000912.1.
DR AlphaFoldDB; P78018; -.
DR SMR; P78018; -.
DR IntAct; P78018; 2.
DR STRING; 272634.MPN_429; -.
DR EnsemblBacteria; AAB96060; AAB96060; MPN_429.
DR KEGG; mpn:MPN_429; -.
DR PATRIC; fig|272634.6.peg.464; -.
DR HOGENOM; CLU_025427_0_2_14; -.
DR OMA; DMIFDIG; -.
DR BioCyc; MetaCyc:MON-549; -.
DR BioCyc; MPNE272634:G1GJ3-693-MON; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000808; 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 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..409
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145971"
FT BINDING 22..24
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60..63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 365..368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 44212 MW; 6AF230188D398731 CRC64;
MVDFKTVQAF DFQGKTVVLR ADLNVPMKDG VITDNERILA SLDTIKYLLG HNCKIVLLSH
LSRVKSLDDK KGKKSLQPVA SALQNLLKNT KVHFCPENTG DKVKVAVNQL PLGEILVLEN
TRYCDVNEAG EVVKHESKNN AELAQFWASL GDIFVNDAFG TAHRRHASNA GIAKYIKNSC
IGLLMERELI NLYRLINNPP KPFVVVLGGA KVSDKLQVVN NLFKIADHIL IGGGMVNTFL
KALGNEVGTS LVEEDLVQTA KQILDSDKDK KIVLGVDQML HASFKDEPGV ECVVAPQWPA
ELQGFMSLDV GSKTVALFSS YLAKAKTIFW NGPMGVFEFS NYAQGTLAIG KAIAQNQQAF
SVIGGGDSAA AAKQLQIADQ FSFISTGGGA SLALIGGEEL VGISDIQKK