ID E8QXN8_ISOPI Unreviewed; 398 AA.
AC E8QXN8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=Isop_3518 {ECO:0000313|EMBL:ADV64075.1};
OS Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Isosphaera.
OX NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV64075.1, ECO:0000313|Proteomes:UP000008631};
RN [1] {ECO:0000313|EMBL:ADV64075.1, ECO:0000313|Proteomes:UP000008631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43644 / DSM 9630 / IS1B
RC {ECO:0000313|Proteomes:UP000008631};
RX PubMed=21475588; DOI=10.4056/sigs.1533840;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL Stand. Genomic Sci. 4:63-71(2011).
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 ---------------------------------------------------------------------------
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; CP002353; ADV64075.1; -; Genomic_DNA.
DR RefSeq; WP_013566363.1; NC_014962.1.
DR AlphaFoldDB; E8QXN8; -.
DR STRING; 575540.Isop_3518; -.
DR KEGG; ipa:Isop_3518; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_0; -.
DR InParanoid; E8QXN8; -.
DR OrthoDB; 9808460at2; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000008631; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:UP000008631};
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 38
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 61..64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 208
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 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
FT BINDING 327
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 353..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145"
SQ SEQUENCE 398 AA; 42448 MW; DF17E2519729830A CRC64;
MSKKQTIRDL KLDGATVLVR VDFNVPQKAD GAVADDRRIR SALPTLQYAL DHGAALVLVS
HLGRPTGKPE EDAKFRMDPV ARRLEELIGR PVVKADDVVG PSAQAARANL KPGGIVMLEN
VRFHPGEKKG DPEFARQLAS LADAYVNDAF GTCHRDEASM VAVPSAFPAE RRAIGFLVEK
ELDILQTLLG EPKRPMLAIM GGAKVSDKIQ VIENLLAKVD RLLIGGAMTY TFLQAKGHAI
GTSRSEPDKL DLARMLMEKA GDKLMLPVDV RVTDSVSPPG TVQTIDGHDL PEGWGGIDIG
PKTAAIYADL IKTAGTVVWN GPVGKFEDEP FRDGTLAIAR ALAESPAITV VGGGETAEAI
EQFGLADKVT HVSTGGGAFL ESLEGKTFNS LAIIPDLN
//
