PGK_CHLPN
ID PGK_CHLPN Reviewed; 402 AA.
AC Q9Z7M5; Q9JQF8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=CPn_0679, CP_0068, CpB0706;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD18818.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF37956.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98886.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98635.1; -; Genomic_DNA.
DR PIR; C72049; C72049.
DR PIR; D86575; D86575.
DR RefSeq; NP_224875.1; NC_000922.1.
DR RefSeq; WP_010883317.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7M5; -.
DR SMR; Q9Z7M5; -.
DR STRING; 115711.CP_0068; -.
DR EnsemblBacteria; AAD18818; AAD18818; CPn_0679.
DR EnsemblBacteria; AAF37956; AAF37956; CP_0068.
DR GeneID; 45050730; -.
DR KEGG; cpa:CP_0068; -.
DR KEGG; cpj:pgk; -.
DR KEGG; cpn:CPn_0679; -.
DR KEGG; cpt:CpB0706; -.
DR PATRIC; fig|115713.3.peg.750; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_0; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 462069at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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 Transferase.
FT CHAIN 1..402
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145927"
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 59..62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 356..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 402 AA; 43046 MW; 14720238499ECF28 CRC64;
MDKLTVQDLS PEEKKVLVRV DFNVPMQDGK ILDDIRIRSA MPTINYLLKK HAAVILMSHL
GRPKGQGFQE EYSLQPVVDV LEGYLGHHVP LAPDCVGEVA RQAVAQLSPG RVLLLENLRF
HIGEEHPEKD PTFAAELSSY GDFYVNDAFG TSHRKHASVY VVPQAFPGRA AAGLLMEKEL
EFLGRHLLTS PKRPFTAILG GAKISSKIGV IEALLNQVDY LLLAGGMGFT FLQALGKSLG
NSLVEKSALD LARNVLKIAK SRNVTIVLPS DVKAAENLQS KEYSVISIDQ GIPPHLQGFD
IGPRTTEEFI RIINQSATVF WNGPVGVYEV PPFDSGSIAI ANALGNHPSA VTVVGGGDAA
AVVALAGCST KVSHVSTGGG ASLEFLEQGF LPGTEVLSPS KS
