ID E3E4T2_PAEPS Unreviewed; 194 AA.
AC E3E4T2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Phosphoglycerate kinase {ECO:0000313|EMBL:ADO57060.1};
GN Name=gpmB {ECO:0000313|EMBL:ADO57060.1};
GN ORFNames=PPSC2_14520 {ECO:0000313|EMBL:ADO57060.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO57060.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO57060.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO57060.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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; CP002213; ADO57060.1; -; Genomic_DNA.
DR RefSeq; WP_013371658.1; NC_014622.2.
DR AlphaFoldDB; E3E4T2; -.
DR STRING; 1406.LK13_02175; -.
DR KEGG; ppm:PPSC2_14520; -.
DR PATRIC; fig|886882.15.peg.3098; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_8_4_9; -.
DR OrthoDB; 9782128at2; -.
DR Proteomes; UP000006868; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADO57060.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW Transferase {ECO:0000313|EMBL:ADO57060.1}.
FT ACT_SITE 8
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 7..14
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 194 AA; 22311 MW; 84C549E7853C1163 CRC64;
MLIGLIRHGL TDWNAVGKIQ GHSDIPLNEE GRRQARLLAE RLKEEPYHWD GLITSSLSRA
KETGDIIASA LHLPLLEPDD RLRERAYGQV EGMTQAEREE KWGVDWHLLD LGQESDADLQ
LRALAFMEAL WTENRDKNLL VVSHGGFLAN LYKALYQEKF TERIGNLSLS VLQREDADWE
PLLYNCTKHL QEKK
//
