PGK_METMP
ID PGK_METMP Reviewed; 414 AA.
AC P62423;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=MMP1532;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00145};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC Rule:MF_00145}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00145}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF31088.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX950229; CAF31088.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_013999848.1; NC_005791.1.
DR AlphaFoldDB; P62423; -.
DR SMR; P62423; -.
DR STRING; 267377.MMP1532; -.
DR EnsemblBacteria; CAF31088; CAF31088; MMP1532.
DR GeneID; 37876132; -.
DR KEGG; mmp:MMP1532; -.
DR PATRIC; fig|267377.15.peg.1569; -.
DR eggNOG; arCOG00496; Archaea.
DR HOGENOM; CLU_025427_0_2_2; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 46017at2157; -.
DR BioCyc; MMAR267377:MMP_RS07870-MON; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000000590; 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; 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..414
FT /note="Phosphoglycerate kinase"
FT /id="PRO_0000146061"
FT BINDING 20..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 60..63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT BINDING 364..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ SEQUENCE 414 AA; 45329 MW; C53F5B915B72E0D6 CRC64;
MFLTLDDFEL EGKTVALRVD INSPIDVNTG DILDDTRIKA CSDTIKSLSE KGAKVVILAH
QSRPGKKDFT TLEAHAKKLS EVLNMEVTHV DGLICASARE AILAMDNGEI ILLENVRLLA
EEVLSDWKSW EEITPEKQAK TVMIKKLHPF FDYFVNDAFA AAHRAQPSLV GFSYYVPMLC
GRVMEKELFT LTKVLKNPER PCVFALGGAK ADDSIEVLKN VLEKQTADQV LTSGVVANIF
LVAKGYKIGP NENVIADMGY TNQIEIAKEL ISKYGDKIVV PIDAALNVDG ERVEKELDLN
EEITYPIHDM GEKTMKLYEE ILKDAKTVVA NGPAGVFENK NFLKGTEELL KSTANSKGFS
VIGGGHLSAA AEVVGLAGKM DHISTGGGAC IEFLAGKKLP VIEMLSKSYE KHKL