ID Q5NJY9_LACPN Unreviewed; 400 AA.
AC Q5NJY9;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 138.
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:CAD99189.1};
GN ORFNames=AVR83_01750 {ECO:0000313|EMBL:AOB21735.1}, C7M36_00571
GN {ECO:0000313|EMBL:QHM36312.1}, C7M40_01443
GN {ECO:0000313|EMBL:QHM49489.1}, Lp19_2196
GN {ECO:0000313|EMBL:KZU94222.1}, LpLQ80_03510
GN {ECO:0000313|EMBL:AWI39626.1}, SN35N_0905
GN {ECO:0000313|EMBL:BBA81284.1};
OS Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1590 {ECO:0000313|EMBL:CAD99189.1};
RN [1] {ECO:0000313|EMBL:CAD99189.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NC8 {ECO:0000313|EMBL:CAD99189.1};
RX PubMed=17294332; DOI=10.1007/s00284-006-0013-x;
RA Naterstad K., Rud I., Kvam I., Axelsson L.;
RT "Characterisation of the gap operon from Lactobacillus plantarum and
RT Lactobacillus sakei.";
RL Curr. Microbiol. 54:180-185(2007).
RN [2] {ECO:0000313|EMBL:AEG64642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=299v {ECO:0000313|EMBL:AEG64642.1};
RX PubMed=23395591; DOI=10.1016/j.micres.2013.01.003;
RA Glenting J., Beck H.C., Vrang A., Riemann H., Ravn P., Hansen A.M.,
RA Antonsson M., Ahrne S., Israelsen H., Madsen S.;
RT "Anchorless surface associated glycolytic enzymes from Lactobacillus
RT plantarum 299v bind to epithelial cells and extracellular matrix
RT proteins.";
RL Microbiol. Res. 168:245-253(2013).
RN [3] {ECO:0000313|EMBL:AOB21735.1, ECO:0000313|Proteomes:UP000093296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF {ECO:0000313|EMBL:AOB21735.1,
RC ECO:0000313|Proteomes:UP000093296};
RA Petkau K., Fast D., Duggal A., Foley E.;
RT "Comparative evaluation of the genomes of common bacterial members of the
RT Drosophila intestinal community.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KZU94222.1, ECO:0000313|Proteomes:UP000076882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19.1 {ECO:0000313|EMBL:KZU94222.1,
RC ECO:0000313|Proteomes:UP000076882};
RA Martino M.E.;
RT "Comparative genomics of 54 Lactobacillus plantarum strains reveals genomic
RT uncoupling from niche constraints.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:BBA81284.1, ECO:0000313|Proteomes:UP000269784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN35N {ECO:0000313|EMBL:BBA81284.1,
RC ECO:0000313|Proteomes:UP000269784};
RX PubMed=29607926; DOI=.1248/bpb.b17-00840;
RA Noda M., Shiraga M., Kumagai T., Danshiitsoodol N., Sugiyama M.;
RT "Characterization of the SN35N Strain-Specific Exopolysaccharide Encoded in
RT the Whole Circular Genome of a Plant-Derived Lactobacillus plantarum.";
RL Biol. Pharm. Bull. 41:536-545(2018).
RN [6] {ECO:0000313|EMBL:QHM36312.1, ECO:0000313|Proteomes:UP000464882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM101167 {ECO:0000313|EMBL:QHM36312.1,
RC ECO:0000313|Proteomes:UP000464882};
RA Jeong D.-Y.;
RT "Lactobacillus plantatrum SRCM101167 having anti-virus activity species
RT isolated from Korea kimchi.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:QHM49489.1, ECO:0000313|Proteomes:UP000465032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM49489.1,
RC ECO:0000313|Proteomes:UP000465032};
RA Jeong D.-Y.;
RT "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT isolated from Korea kimchi.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000313|EMBL:AWI39626.1, ECO:0000313|Proteomes:UP000244922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LQ80 {ECO:0000313|EMBL:AWI39626.1,
RC ECO:0000313|Proteomes:UP000244922};
RA Moriya N., Nakano K., Shiroma A., Shinzato M., Ashimine N., Minami M.,
RA Tamotsu H., Shimoji M., Nakanishi T., Ohki S., Teruya K., Satou K.,
RA Hirano T., Hagi T., Kobayashi M., Nomura M., Kimoto H.N., Tajima K.,
RA Cai Y., Suzuki C.;
RT "Complete Genome Sequence of Lactobacillus plantarum Strain LQ80 Selected
RT for Preparation of Fermented Liquid Feed for Pig.";
RL Submitted (APR-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00145}.
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; HQ622815; AEG64642.1; -; Genomic_DNA.
DR EMBL; CP013753; AOB21735.1; -; Genomic_DNA.
DR EMBL; CP028977; AWI39626.1; -; Genomic_DNA.
DR EMBL; AP018405; BBA81284.1; -; Genomic_DNA.
DR EMBL; AJ567908; CAD99189.1; -; Genomic_DNA.
DR EMBL; LUXM01000033; KZU94222.1; -; Genomic_DNA.
DR EMBL; CP028334; QHM36312.1; -; Genomic_DNA.
DR EMBL; CP028241; QHM49489.1; -; Genomic_DNA.
DR RefSeq; WP_003641045.1; NZ_WYDR01000028.1.
DR GeneID; 79830089; -.
DR PATRIC; fig|1590.142.peg.650; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000076882; Unassembled WGS sequence.
DR Proteomes; UP000093296; Chromosome.
DR Proteomes; UP000244922; Chromosome.
DR Proteomes; UP000269784; Chromosome.
DR Proteomes; UP000464882; Chromosome.
DR Proteomes; UP000465032; 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 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|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00145}.
FT BINDING 21..23
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 59..62
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 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT ECO:0000256|PIRSR:PIRSR000724-1"
FT BINDING 211
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 329
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 356..359
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 400 AA; 42797 MW; 1BD70A88477EF7A8 CRC64;
MAKLIVSDLD VKDKKVLIRV DFNVPIKDGK IGDDNRIVAA LPTIKYVIEH DGKAILFSHL
GRIKSEDDKK GLSLRPVAER LSNLLNKPVT FVPVTEGEQL ETAINNMNDG DVLVVENTRF
EDVVNGEQVK RESGNDPELG KYWASLGDVY VNDAFGTAHR SHASNVGIAS NMDQVAAGFL
MEKEIKFLGD AVDNPKHPFV AILGGAKVSD KIGVIDHLIS KADKIIIGGG MTYTFYAAKG
MGIGNSLVEK DKIELAKSII EKAGDKLVLP SDSIVAEKFD NDVPSKVVEG SIPDGYMALD
IGPKSIEEFE DVLRDAKTVV WNGPMGVFEM SNYAKGTLEI GKFLGTLSDA TTIVGGGDST
AAVKQLGVGD KLTHISTGGG ASLEYLEGKE LPGIAAISEK
//
