PGK_HAEIN
ID PGK_HAEIN Reviewed; 386 AA.
AC P43726;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=HI_0525;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP PROTEIN SEQUENCE OF 2-6.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
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; L42023; AAC22183.1; -; Genomic_DNA.
DR PIR; D64074; D64074.
DR RefSeq; NP_438683.1; NC_000907.1.
DR RefSeq; WP_005694128.1; NC_000907.1.
DR AlphaFoldDB; P43726; -.
DR SMR; P43726; -.
DR STRING; 71421.HI_0525; -.
DR EnsemblBacteria; AAC22183; AAC22183; HI_0525.
DR KEGG; hin:HI_0525; -.
DR PATRIC; fig|71421.8.peg.544; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_6; -.
DR OMA; DMIFDIG; -.
DR PhylomeDB; P43726; -.
DR BioCyc; HINF71421:G1GJ1-538-MON; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000579; 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 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; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10675023"
FT CHAIN 2..386
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000145948"
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 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 339..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 386 AA; 40983 MW; 9029D21368DEB66D CRC64;
MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAT IPTLKLALEK GAKVMVTSHL
GRPTEGEFKP EDSLQPVVDY LKNAGFNVRL EQDYLNGVDV KDGEIVVLEN VRVNKGEKKN
DPELGKKYAA LCDVFVMDAF GTAHRAQAST YGVAEFAPIA CAGPLLAAEL DALGKALKEP
ARPMVAIVGG SKVSTKLEVL NSLSKIADQI IVGGGIANTF IAAAGHNVGK SLYEADLIPV
AKELAANTDI PVPVDVRVGL EFSETAAATE KVVNEVKDDE SIFDIGDKSA EQLAEIIKNA
KTVLWNGPVG VFEFPHFRKG TEIISHAIAN SDAFSIAGGG DTLAAIDLFG IADKISYIST
GGGAFLEFVE GKVLPAVEIL EKRAKN
