ID PGK_METMA Reviewed; 416 AA.
AC Q8PZK7;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 1.
DT 01-MAY-2013, entry version 68.
DE RecName: Full=Phosphoglycerate kinase;
DE EC=2.7.2.3;
GN Name=pgk; OrderedLocusNames=MM_0485;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS JCM 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene
RT transfer between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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 (Potential).
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
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DR EMBL; AE008384; AAM30181.1; -; Genomic_DNA.
DR RefSeq; NP_632509.1; NC_003901.1.
DR ProteinModelPortal; Q8PZK7; -.
DR STRING; 192952.MM_0485; -.
DR EnsemblBacteria; AAM30181; AAM30181; MM_0485.
DR GeneID; 1478827; -.
DR KEGG; mma:MM_0485; -.
DR eggNOG; COG0126; -.
DR HOGENOM; HOG000227108; -.
DR KO; K00927; -.
DR OMA; EKKNDEA; -.
DR ProtClustDB; PRK00073; -.
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.
DR PROSITE; PS00111; PGLYCERATE_KINASE; FALSE_NEG.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1 416 Phosphoglycerate kinase.
FT /FTId=PRO_0000146060.
FT NP_BIND 362 365 ATP (By similarity).
FT REGION 28 30 Substrate binding (By similarity).
FT REGION 65 68 Substrate binding (By similarity).
FT BINDING 44 44 Substrate (By similarity).
FT BINDING 122 122 Substrate (By similarity).
FT BINDING 162 162 Substrate (By similarity).
FT BINDING 337 337 ATP (By similarity).
SQ SEQUENCE 416 AA; 45391 MW; 01535184440FD3F7 CRC64;
MLRVMTSRNF LTIDDFDIRG KTILLRVDMN SPMDTQGHIL DDMRIRSHIA TLKDLESAKV
VVLAHQSRPG KKDFTTMKPH AHLLSRYLGR QVTYVDDIFG TFAKTQIASM EDGDVIMLEN
VRFYSEESLE RTTAEQANTF MVKKLAPFVD IFLNDAFAVS HRSHLSVVGF TEVLPSGAGR
VMEKELISLE KGVKSGERPS VFVLGGAKVD DSLRVTENVL TNGGADRVLL TGVVANVALA
ASGVNIGKAN LDFIKSQGYE DQIERARGLL AKFEDKIGLP KDVALNDNKK RVEAPISELN
SDSLPINDIG LETIVDYTNE IQNAKTVVLN GPAGVSEIED FALGTHEIIK AAIKSDFSII
GGGHISVEVA HLGLEHRFSH ISTGGGACID FLAGEKLPGV EALKAAYNKY QEAKKL
//
