ID   PGK_METFV               Reviewed;         410 AA.
AC   P20971; E3GXC7;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=Mfer_0156;
OS   Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=523846;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX   PubMed=2401408; DOI=10.1016/0378-1119(90)90157-m;
RA   Fabry S., Heppner P., Dietmaier W., Hensel R.;
RT   "Cloning and sequencing the gene encoding 3-phosphoglycerate kinase from
RT   mesophilic Methanobacterium bryantii and thermophilic Methanothermus
RT   fervidus.";
RL   Gene 91:19-25(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S;
RX   PubMed=21304736; DOI=10.4056/sigs.1283367;
RA   Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA   Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA   Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; M55529; AAA72936.1; -; Genomic_DNA.
DR   EMBL; CP002278; ADP76959.1; -; Genomic_DNA.
DR   PIR; PN0008; PN0008.
DR   AlphaFoldDB; P20971; -.
DR   SMR; P20971; -.
DR   STRING; 523846.Mfer_0156; -.
DR   KEGG; mfv:Mfer_0156; -.
DR   HOGENOM; CLU_025427_0_2_2; -.
DR   BRENDA; 2.7.2.3; 3286.
DR   SABIO-RK; P20971; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000002315; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..410
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146057"
FT   BINDING         22..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
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"
SQ   SEQUENCE   410 AA;  45871 MW;  6AA54EB65C292EFA CRC64;
     MFKFYTMDDF DYSGSRVLVR VDINSPVDPH TGRILDDTRM RLHSKTLKEL VDENAKVAIL
     AHQSRPGKRD FTTMEEHSKV LSNILDMPVT YVEDIFGCAA RESIRNMENG DIILLENVRF
     YSEEVLKRDP KVQAETHLVR KLSSVVDYYI NDAFAAAHRS QPSLVGFPLK LPSAAGRLME
     REVKTLYKII KNVEKPCVYI LGGVKIDDSI MIMKNILKNG SADYILTSGL VANVFLEASG
     IDIKEKNRKI LYRKNYKKFI KMAKKLKDKY GEKILTPVDV AINKNGKRID VPIDDIPNFP
     IYDIGMETIK IYAEKIREAK TIFANGPAGV FEEQQFSIGT EDLLNAIASS NAFSVIAGGH
     LAAAAEKMGI SNKINHISSG GGACIAFLSG EELPAIKVLE EARKRSDKYI
//