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Database: UniProt/SWISS-PROT
Entry: PGK_METMA
LinkDB: PGK_METMA
Original site: PGK_METMA 
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   29-OCT-2014, entry version 75.
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=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. {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}.
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DR   EMBL; AE008384; AAM30181.1; -; Genomic_DNA.
DR   RefSeq; NP_632509.1; NC_003901.1.
DR   RefSeq; WP_011032438.1; 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; AGHPVGK; -.
DR   BioCyc; MMAZ192952:GCK2-502-MONOMER; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-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; SSF53748; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    416       Phosphoglycerate kinase.
FT                                /FTId=PRO_0000146060.
FT   NP_BIND     362    365       ATP. {ECO:0000255|HAMAP-Rule:MF_00145}.
FT   REGION       28     30       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   REGION       65     68       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING      44     44       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING     122    122       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING     162    162       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00145}.
FT   BINDING     337    337       ATP. {ECO:0000255|HAMAP-Rule:MF_00145}.
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
//
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