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Database: UniProt/SWISS-PROT
Entry: GPMA_ECOSM
LinkDB: GPMA_ECOSM
Original site: GPMA_ECOSM 
ID   GPMA_ECOSM              Reviewed;         250 AA.
AC   B1LM46;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   10-OCT-2018, entry version 64.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000255|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000255|HAMAP-Rule:MF_01039};
GN   Name=gpmA {ECO:0000255|HAMAP-Rule:MF_01039};
GN   OrderedLocusNames=EcSMS35_0778;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia
RT   coli SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC       {ECO:0000255|HAMAP-Rule:MF_01039}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC       Rule:MF_01039}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
DR   EMBL; CP000970; ACB17040.1; -; Genomic_DNA.
DR   RefSeq; WP_001295305.1; NC_010498.1.
DR   ProteinModelPortal; B1LM46; -.
DR   SMR; B1LM46; -.
DR   PRIDE; B1LM46; -.
DR   EnsemblBacteria; ACB17040; ACB17040; EcSMS35_0778.
DR   KEGG; ecm:EcSMS35_0778; -.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; RMLPYWY; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000007011; Chromosome.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN         1    250       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_1000135950.
FT   REGION       10     17       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       23     24       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       89     92       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      116    117       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      185    186       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01039}.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01039}.
FT   ACT_SITE     89     89       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_01039}.
FT   BINDING      62     62       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01039}.
FT   BINDING     100    100       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01039}.
FT   SITE        184    184       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01039}.
SQ   SEQUENCE   250 AA;  28556 MW;  A6E0A49406F8482A CRC64;
     MAVTKLVLVR HGESQWNKEN RFTGWYDVDL SEKGVSEAKA AGKLLKEEGY SFDFAYTSVL
     KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA
     VTPPELTKDD ERYPGHDPRY AKLSEKELPL TESLALTIDR VIPYWNETIL PRMKSGERVI
     IAAHGNSLRA LVKYLDNMSE EEILELNIPT GVPLVYEFDE NFKPLKRYYL GNADEIAAKA
     AAVANQGKAK
//
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