PGK_THET8
ID PGK_THET8 Reviewed; 390 AA.
AC P09403; Q5SJV2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=TTHA0906;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3052437; DOI=10.1042/bj2540509;
RA Bowen D., Littlechild J.A., Fothergill J.E., Watson H.C., Hall L.;
RT "Nucleotide sequence of the phosphoglycerate kinase gene from the extreme
RT thermophile Thermus thermophilus. Comparison of the deduced amino acid
RT sequence with that of the mesophilic yeast phosphoglycerate kinase.";
RL Biochem. J. 254:509-517(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; X12464; CAA31006.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70729.1; -; Genomic_DNA.
DR RefSeq; WP_011228285.1; NC_006461.1.
DR RefSeq; YP_144172.1; NC_006461.1.
DR PDB; 1V6S; X-ray; 1.50 A; A/B=1-390.
DR PDBsum; 1V6S; -.
DR AlphaFoldDB; P09403; -.
DR SMR; P09403; -.
DR STRING; 300852.55772288; -.
DR EnsemblBacteria; BAD70729; BAD70729; BAD70729.
DR GeneID; 3169950; -.
DR KEGG; ttj:TTHA0906; -.
DR PATRIC; fig|300852.9.peg.898; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_0; -.
DR OMA; DMIFDIG; -.
DR PhylomeDB; P09403; -.
DR BRENDA; 2.7.2.3; 2305.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; P09403; -.
DR Proteomes; UP000000532; 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 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 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glycolysis; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..390
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000146027"
FT BINDING 19..21
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57..60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 347..350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1V6S"
FT TURN 118..123
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1V6S"
FT TURN 151..155
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:1V6S"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:1V6S"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1V6S"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:1V6S"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:1V6S"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 372..379
FT /evidence="ECO:0007829|PDB:1V6S"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1V6S"
SQ SEQUENCE 390 AA; 41777 MW; 3829E89FCEDC90B3 CRC64;
MRTLLDLDPK GKRVLVRVDY NVPVQDGKVQ DETRILESLP TLRHLLAGGA SLVLLSHLGR
PKGPDPKYSL APVGEALRAH LPEARFAPFP PGSEEARREA EALRPGEVLL LENVRFEPGE
EKNDPELSAR YARLGEAFVL DAFGSAHRAH ASVVGVARLL PAYAGFLMEK EVRALSRLLK
DPERPYAVVL GGAKVSDKIG VIESLLPRID RLLIGGAMAF TFLKALGGEV GRSLVEEDRL
DLAKDLLGRA EALGVRVYLP EDVVAAERIE AGVETRVFPA RAIPVPYMGL DIGPKTREAF
ARALEGARTV FWNGPMGVFE VPPFDEGTLA VGQAIAALEG AFTVVGGGDS VAAVNRLGLK
ERFGHVSTGG GASLEFLEKG TLPGLEVLEG
