GPMA_RHOOB
ID GPMA_RHOOB Reviewed; 251 AA.
AC C1AZ61;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
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}; OrderedLocusNames=ROP_17420;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={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 -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR EMBL; AP011115; BAH49989.1; -; Genomic_DNA.
DR AlphaFoldDB; C1AZ61; -.
DR SMR; C1AZ61; -.
DR STRING; 632772.ROP_17420; -.
DR EnsemblBacteria; BAH49989; BAH49989; ROP_17420.
DR KEGG; rop:ROP_17420; -.
DR PATRIC; fig|632772.20.peg.1826; -.
DR HOGENOM; CLU_033323_1_1_11; -.
DR OMA; RMLPYWY; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000002212; 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 Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..251
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_1000149528"
FT ACT_SITE 14
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 92
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 13..20
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 26..27
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 119..120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 186..187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 185
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 251 AA; 27745 MW; 28A4537E8ADDB4CA CRC64;
MNGMSTGTLV LLRHGESEWN ALNLFTGWVD VHLTDKGIAE GKRAGELLLE HNLLPDVLYT
SLLRRAISTA NIALDTADRH WIPVIRDWRL NERHYGALQG RNKAQVKDKY GDEQFMLWRR
SYDTPPPTIE PGSEYSQDTD PRYANLDEVP LTECLKDVVV RLIPYWEDTI SADLLAGKTV
LITAHGNSLR ALVKHLDGIS DEDIAGLNIP TGIPLRYDLD ENLKPLNPGG TYLDPEAAAA
GAAAVANQGG K
