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Database: UniProt/SWISS-PROT
Entry: GPMA_PECAS
LinkDB: GPMA_PECAS
Original site: GPMA_PECAS 
ID   GPMA_PECAS              Reviewed;         250 AA.
AC   Q6D7E3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   30-AUG-2017, entry version 84.
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=ECA1382;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia
RT   carotovora subsp. atroseptica and characterization of virulence
RT   factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG74292.1; -; Genomic_DNA.
DR   RefSeq; WP_011092967.1; NC_004547.2.
DR   ProteinModelPortal; Q6D7E3; -.
DR   SMR; Q6D7E3; -.
DR   STRING; 218491.ECA1382; -.
DR   EnsemblBacteria; CAG74292; CAG74292; ECA1382.
DR   KEGG; eca:ECA1382; -.
DR   PATRIC; fig|218491.5.peg.1416; -.
DR   eggNOG; ENOG4105DKJ; Bacteria.
DR   eggNOG; COG0588; LUCA.
DR   HOGENOM; HOG000221682; -.
DR   KO; K01834; -.
DR   OMA; RMLPYWY; -.
DR   OrthoDB; POG091H03E2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; 2.
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;
KW   Reference proteome.
FT   CHAIN         1    250       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_0000229120.
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;  28423 MW;  902B7B2C92EBF502 CRC64;
     MAVTKLVLVR HGESQWNNEN RFTGWYDVDL SEKGRSEAKA AGQLLKDEGF AFDFAYTSVL
     KRAIHTLWSV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA
     ITPPELTRDD ERFPGHDPRY ASLSDKELPQ TESLALTIER VVPYWTETIL PRIKSGERVI
     VAAHGNSLRA LVKYLDNMGE DEILELNIPT GVPLVYEFDE NFKPIKRYYL GNADEIAAKA
     AAVANQGKAK
//
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