PGK_BACSU
ID PGK_BACSU Reviewed; 394 AA.
AC P40924; O32252;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=BSU33930;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-23.
RC STRAIN=168 / IS58;
RX PubMed=9084183; DOI=10.1099/00221287-143-3-991;
RA Schmid R., Bernhardt J., Antelmann H., Voelker U., Mach H., Voelker A.,
RA Hecker M.;
RT "Identification of vegetative proteins for a two-dimensional protein index
RT of Bacillus subtilis.";
RL Microbiology 143:991-998(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-394.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8021172; DOI=10.1128/jb.176.13.3903-3910.1994;
RA Leyva-Vazquez M.A., Setlow P.;
RT "Cloning and nucleotide sequences of the genes encoding triose phosphate
RT isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.";
RL J. Bacteriol. 176:3903-3910(1994).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND THR-299, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
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.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB15398.1; -; Genomic_DNA.
DR EMBL; L29475; AAA21678.1; -; Genomic_DNA.
DR PIR; C69675; C69675.
DR RefSeq; NP_391273.1; NC_000964.3.
DR RefSeq; WP_003243051.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P40924; -.
DR SMR; P40924; -.
DR STRING; 224308.BSU33930; -.
DR iPTMnet; P40924; -.
DR jPOST; P40924; -.
DR PaxDb; P40924; -.
DR PRIDE; P40924; -.
DR EnsemblBacteria; CAB15398; CAB15398; BSU_33930.
DR GeneID; 938572; -.
DR KEGG; bsu:BSU33930; -.
DR PATRIC; fig|224308.179.peg.3678; -.
DR eggNOG; COG0126; Bacteria.
DR InParanoid; P40924; -.
DR OMA; DMIFDIG; -.
DR PhylomeDB; P40924; -.
DR BioCyc; BSUB:BSU33930-MON; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145905"
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 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 350..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 388
FT /note="V -> A (in Ref. 3; AAA21678)"
FT /evidence="ECO:0000305"
FT CONFLICT 393..394
FT /note="DK -> R (in Ref. 3; AAA21678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 42190 MW; C909AF1D76AF0F83 CRC64;
MNKKTLKDID VKGKVVFCRV DFNVPMKDGE VTDDTRIRAA LPTIKHLADQ GAKVLLASHL
GRPKGEVVEE LRLTPVAARL GELLGKEVKK ADEAYGDAVK AQISEMKDGD VLVLENVRFY
PGEEKNDPEL AKAFAELADV YVNDAFGAAH RAHASTAGIA EHLPAVAGFL MEKELDVLGK
AVSNPDRPFT AIIGGAKVKD KIGVIESLLD KVDNLIIGGG LAYTFVKALG YEVGKSLLEE
DKIELAKSFM DRAKEKGVNF YMPEDVLVAD DFSNDANVKI VPISEIPSDL EAIDIGTKTR
ETYADVIKNS KLVVWNGPMG VFEIDLFAQG TKAVAEALAE AKDTYSVIGG GDSAAAVEKF
GLADKMSHIS TGGGASLEFM EGKELPGVAA LNDK
