ID A0A101T7J1_9ACTN Unreviewed; 403 AA.
AC A0A101T7J1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
DE EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
GN Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145,
GN ECO:0000313|EMBL:KUN87322.1};
GN ORFNames=AQJ66_10245 {ECO:0000313|EMBL:KUN87322.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN87322.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN87322.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN87322.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-2015) 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 Evidence={ECO:0000256|ARBA:ARBA00000642, ECO:0000256|HAMAP-
CC Rule:MF_00145, ECO:0000256|RuleBase:RU000532};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC Rule:MF_00145}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUN87322.1}.
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; LMWX01000014; KUN87322.1; -; Genomic_DNA.
DR RefSeq; WP_061919438.1; NZ_KQ948854.1.
DR AlphaFoldDB; A0A101T7J1; -.
DR STRING; 285568.AQJ66_10245; -.
DR OrthoDB; 9808460at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000053024; Unassembled WGS sequence.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00145}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00145};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00145}; Reference proteome {ECO:0000313|Proteomes:UP000053024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00145}.
FT BINDING 22..24
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 60..63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-2"
FT BINDING 359..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-2"
SQ SEQUENCE 403 AA; 42097 MW; F895ADA49B93CA6B CRC64;
MKTIDELLAA GVSGKRVFVR ADLNVPLASG TITDDGRIRA VLPTVKALAD AGAKVVVASH
LGRPKGAPDP AFSLAPAASR LGELLGSAVA FATDTVGQSA RETVAGLTDG HVAVLENLRF
NPGETSKDDA ERGAFADLLA ELADVYVGDG FGAVHRKHAS VFDLPARLPH YAGYLIATEV
GVLKKLTDDV ERPYVVALGG AKVSDKLAVI DELIGKADRL LIGGGMAYTF LKAQGHEVGI
SLLQEDQVPV VTEYLERAEK QGVELVLPVD VVVAREFPDL KAQAPTEHAV VDADMIPADQ
EGLDIGPRTR ELYASKLADA RTVFWNGPMG VFEHPDYAEG TKAVAQALVD SNGFTVVGGG
DSAAAVRTLG FDENAFGHIS TGGGASLEYL EGKTLPGLAA LED
//
