ID E1RFA7_METP4 Unreviewed; 404 AA.
AC E1RFA7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 01-MAY-2013, entry version 17.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=Mpet_0278;
OS Methanoplanus petrolearius (strain DSM 11571 / OCM 486 / SEBR 4847).
OC Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC Methanomicrobiaceae; Methanoplanus.
OX NCBI_TaxID=679926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11571 / OCM 486 / SEBR 4847;
RX DOI=10.4056/sigs.1183143;
RA Brambilla E., Djao O., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA Nolan M., Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C.,
RA Rohde M., Spring S., Sikorski J., Goker M., Woyke T., Bristow J.,
RA Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H.;
RT "Complete genome sequence of Methanoplanus petrolearius type strain
RT (SEBR 4847).";
RL Stand. Genomic Sci. 3:203-211(2010).
CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC D-glyceroyl phosphate.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
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DR EMBL; CP002117; ADN35055.1; -; Genomic_DNA.
DR RefSeq; YP_003893493.1; NC_014507.1.
DR EnsemblBacteria; ADN35055; ADN35055; Mpet_0278.
DR GeneID; 9742721; -.
DR KEGG; mpi:Mpet_0278; -.
DR HOGENOM; HOG000227108; -.
DR KO; K00927; -.
DR OMA; EKKNDEA; -.
DR BioCyc; MPET679926:GHOF-283-MONOMER; -.
DR UniPathway; UPA00109; UER00185.
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:HAMAP.
DR GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR Gene3D; 3.40.50.1260; -; 1.
DR Gene3D; 3.40.50.1270; -; 1.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1; -.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; PGK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Transferase.
FT NP_BIND 355 358 ATP (By similarity).
FT REGION 21 23 Substrate binding (By similarity).
FT REGION 59 62 Substrate binding (By similarity).
FT BINDING 38 38 Substrate (By similarity).
FT BINDING 116 116 Substrate (By similarity).
FT BINDING 156 156 Substrate (By similarity).
FT BINDING 330 330 ATP (By similarity).
SQ SEQUENCE 404 AA; 43888 MW; D08FB5D825C11F9D CRC64;
MKIGRLEDLG SLRGTALLRV DFNSPIDPSS NMILDDKRFR EHAPTVKALE DSKCVIVTHQ
SRPMKKDFTN LRAHAERLER LIGRPVDYID DIFGACARDA VKTMDYGEVL MLENVRFNSE
EVLTMDGEDA MKTHLVKGLS AMADYYVFDA FGTAHRSQPT IVGLPRVMRS VAGLLMDKEV
STLSKVLTDA PGPVTFVLGG TKVDDSLAVA KNALEAGITD NVVFTGVVAN VVYLAEGKKI
GKPSTDLVHS LGYDKEIEVA AELLKKYSDR IVTPDHVAVK EDGVRAEYPL ENMPQDKGIM
DLGIESLAEL TGIISNSGTI VLNGPAGVFE DEQFSAGTYE LIRASEKAEF SVVGGGHTAA
VIEKMGVADR FSHISTGGGA CIEFLTGKKL PAVEALEYSK EKFW
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