PGK_PYRHO
ID PGK_PYRHO Reviewed; 410 AA.
AC O58965;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=PH1218; ORFNames=PHBK036;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of phosphoglycerate kinase from Pyrococcus horikoshii
RT OT3.";
RL Submitted (JUN-2005) to the PDB data bank.
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: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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; BA000001; BAA30318.1; -; Genomic_DNA.
DR PIR; D71065; D71065.
DR RefSeq; WP_010885305.1; NC_000961.1.
DR PDB; 2CUN; X-ray; 2.10 A; A/B=1-410.
DR PDBsum; 2CUN; -.
DR AlphaFoldDB; O58965; -.
DR SMR; O58965; -.
DR IntAct; O58965; 1.
DR MINT; O58965; -.
DR STRING; 70601.3257635; -.
DR EnsemblBacteria; BAA30318; BAA30318; BAA30318.
DR GeneID; 1443540; -.
DR KEGG; pho:PH1218; -.
DR eggNOG; arCOG00496; Archaea.
DR OMA; DMIFDIG; -.
DR OrthoDB; 46017at2157; -.
DR UniPathway; UPA00109; UER00185.
DR EvolutionaryTrace; O58965; -.
DR Proteomes; UP000000752; 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 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; Glycolysis; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..410
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000146067"
FT BINDING 19..21
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 57..60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 358..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2CUN"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2CUN"
FT TURN 161..165
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:2CUN"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:2CUN"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 381..387
FT /evidence="ECO:0007829|PDB:2CUN"
FT HELIX 393..404
FT /evidence="ECO:0007829|PDB:2CUN"
SQ SEQUENCE 410 AA; 46403 MW; 6912EDE7BD26486E CRC64;
MFRLEDFNFH NKTVFLRVDL NSPMKDGKII SDARFKAVLP TIRYLIESGA KVVIGTHQGK
PYSEDYTTTE EHARVLSELL DQHVEYIEDI FGRYAREKIK ELKSGEVAIL ENLRFSAEEV
KNKPIEECEK TFLVKKLSKV IDYVVNDAFA TAHRSQPSLV GFARIKPMIM GFLMEKEIEA
LMRAYYSKDS PKIYVLGGAK VEDSLKVVEN VLRRERADLV LTGGLVANVF TLAKGFDLGR
KNVEFMKKKG LLDYVKHAEE ILDEFYPYIR TPVDFAVDYK GERVEIDLLS ENRGLLHQYQ
IMDIGKRTAE KYREILMKAR IIVANGPMGV FEREEFAIGT VEVFKAIADS PAFSVLGGGH
SIASIQKYGI TGITHISTGG GAMLSFFAGE ELPVLRALQI SYEKFKEVVK
