PGK_BORBU
ID PGK_BORBU Reviewed; 393 AA.
AC Q59181; Q59186;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=BB_0056;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=8557349; DOI=10.1128/iai.64.1.262-268.1996;
RA Anda P., Gebbia J.A., Backenson P.B., Coleman J.L., Benach J.L.;
RT "A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi
RT and Borrelia hermsii.";
RL Infect. Immun. 64:262-268(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 346-393.
RC STRAIN=212;
RX PubMed=7812434; DOI=10.1099/13500872-140-11-2931;
RA Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G.;
RT "Conservation of gene arrangement and an unusual organization of rRNA genes
RT in the linear chromosomes of the Lyme disease spirochaetes Borrelia
RT burgdorferi, B. garinii and B. afzelii.";
RL Microbiology 140:2931-2940(1994).
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; U28760; AAB53931.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66451.1; -; Genomic_DNA.
DR EMBL; L32595; AAC41405.1; -; Genomic_DNA.
DR PIR; H70106; H70106.
DR RefSeq; NP_212190.1; NC_001318.1.
DR RefSeq; WP_010255334.1; NC_001318.1.
DR AlphaFoldDB; Q59181; -.
DR SMR; Q59181; -.
DR STRING; 224326.BB_0056; -.
DR PRIDE; Q59181; -.
DR EnsemblBacteria; AAC66451; AAC66451; BB_0056.
DR KEGG; bbu:BB_0056; -.
DR PATRIC; fig|224326.49.peg.454; -.
DR HOGENOM; CLU_025427_0_2_12; -.
DR OMA; DMIFDIG; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
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 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; 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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145911"
FT BINDING 22..24
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60..63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 324
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 CONFLICT 164
FT /note="L -> S (in Ref. 1; AAB53931)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..178
FT /note="KF -> NS (in Ref. 1; AAB53931)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="F -> S (in Ref. 1; AAB53931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 42346 MW; EB437EFD5F7AFFDE CRC64;
MSIKTVKDFS SFAGKRALVR CDFNVPLKEG SISDDTRIRA ALSTIEYLKE RGARIVLVSH
LGRPDGKKNP KYSLKPVANR LSELLGQDVK MLSDCIGSEV VNSTLQMKDG DVVLLENVRF
YAEEEKNDKN FAKKLSENGD VFVNDAFGAA HRAHASTVGV ADYLPSVGGF LMEKEDKFLG
GILKNPERPF VSIIGGSKVS SKIAVLESLL SKSNVVVIGG GMAYTFLHSE GYSIGKSLLE
DEYIGIASSF LKKAKELGVK VILPLDHIVA DDFNKNSIPE YIDSFNIPEN KIGMDIGANT
LKEIENVVKT AKTIIWNGPL GVFEFDSFSK GTAKVAEMVA SCSGLTVVGG GDSVAAVNKF
NLSDKITHVS TGGGASLEYL EGRILPGIKV LEN
