GPMA_MANSM
ID GPMA_MANSM Reviewed; 227 AA.
AC Q65Q32;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=MS2321;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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 -!- 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}.
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DR EMBL; AE016827; AAU38928.1; -; Genomic_DNA.
DR RefSeq; WP_011201466.1; NC_006300.1.
DR AlphaFoldDB; Q65Q32; -.
DR SMR; Q65Q32; -.
DR STRING; 221988.MS2321; -.
DR EnsemblBacteria; AAU38928; AAU38928; MS2321.
DR KEGG; msu:MS2321; -.
DR eggNOG; COG0588; Bacteria.
DR HOGENOM; CLU_033323_1_5_6; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 1122642at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000607; 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; 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.
PE 3: Inferred from homology;
KW Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..227
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000229127"
FT ACT_SITE 8
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 86
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 7..14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 20..21
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 227 AA; 25639 MW; 8B1469A9928696F6 CRC64;
MELVFIRHGL SEWNALNLFT GWRDVNLSEK GVEEAKEAGR KLKAAGFEFD IAFTSVLTRA
IKTCNLVLEE SNQLWVPQIK TWRLNERHYG GLQGLNKAEA AAEHGDEQVR IWRRSYDVLP
PVLDPKDPNS AHNDRRYAHL PADVVPDCEN LKVTLERVLP FWEDQIAPAI KAGKRVLVAA
HGNSLRALAK HIEGISDADI MDLEIPTGQP LVYTLDDNLK VVSKRYL
