PGK_MYCPU
ID PGK_MYCPU Reviewed; 771 AA.
AC Q98QW4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=MYPU_2460;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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: In the N-terminal section; belongs to the phosphoglycerate
CC kinase family. {ECO:0000305}.
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DR EMBL; AL445563; CAC13419.1; -; Genomic_DNA.
DR PIR; F90542; F90542.
DR AlphaFoldDB; Q98QW4; -.
DR SMR; Q98QW4; -.
DR STRING; 272635.MYPU_2460; -.
DR EnsemblBacteria; CAC13419; CAC13419; CAC13419.
DR KEGG; mpu:MYPU_2460; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_362403_0_0_14; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000528; 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 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..771
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145972"
FT REGION 1..406
FT /note="Phosphoglycerate kinase"
FT REGION 407..771
FT /note="Unknown"
FT BINDING 20..22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 58..61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 334
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"
SQ SEQUENCE 771 AA; 86689 MW; CFC542BC9071AB98 CRC64;
MKKLITDLNL NDKKVLIRLD LNVPLKGKKI TSLKRIEESI PTIKYVQERG GKIILLSHLG
RVKTKEDKEK KSLSIVVEAL ASLLNSPVKF VDQTRGKKLE SAIEKLKPGD VLLIENTRFE
DLNNNAESNN DPELGKYWAS LGDVFINDAF GTAHRAHASN VGIASNIKES ALGILVQKEV
NALWKLMEQQ EKPFVAILGG SKVSDKINVL EKIIDKVDRL IIGGAMAYTF LKAQGIGIGD
SIYEQDKIEF ATEFLKKYNH KIILPIDHAL AKKFKNAKPI FNNENPLEIP QTFIGMDVGP
KTIELIHKYI KGDTKLGISP AKTIFWNGPM GVTEFEEFQS GSLAVVEAIS QLVGAYSVVG
GGDSIAIIEK LNAQMLFSHI STGGGASLEF IESKVLPGID AIQNYEQTYE QYDSQVQSQD
FSQNFDSPLV EETFSQSTSE NFSDFASSTQ EHFATSENQN TLINNYENPG FDSQDMFKTE
EQNDSTSSFL TSTNPFSSEF SNEFKTSDFQ DLKQTQETET QETLIPHTFE YTTDDLRHTL
EQYVRETSFQ TRESTFPTEE ASFETLEETS FQTLEESFPT QSFEQVEQTS EKNMEVSTEN
FENASSQTNS FTVSDIPKTT STFEDLETPE TQNTTLEEVA LETSNFEAQN LETPNLQTSN
FETSNLETSN FETSNFETST FESFNTGNFS TPSSTFEDLD LQSATFQTND ESERSTQENF
EPTEVIESDL LAMKTTELEQ EITNNTSRDI LSEDEVAAPH KKRFWFFGRK R