GPMA_POLAQ
ID GPMA_POLAQ Reviewed; 229 AA.
AC A4T096;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Pnuc_1948;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP35160.1; -; Genomic_DNA.
DR RefSeq; WP_011903783.1; NC_009379.1.
DR AlphaFoldDB; A4T096; -.
DR SMR; A4T096; -.
DR STRING; 312153.Pnuc_1948; -.
DR PRIDE; A4T096; -.
DR EnsemblBacteria; ABP35160; ABP35160; Pnuc_1948.
DR GeneID; 31482339; -.
DR KEGG; pnu:Pnuc_1948; -.
DR eggNOG; COG0588; Bacteria.
DR HOGENOM; CLU_033323_1_1_4; -.
DR OMA; RMLPYWY; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000231; 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; 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 Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..229
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_1000084327"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 229 AA; 26322 MW; E946BD6C41659698 CRC64;
MKQLVLIRHG ESAWNLENRF TGWADVDLTP KGAEQALAAG EHLRKAGYEF DVAYTSVLRR
AIRTLWHVQD AMDLMWLPVV HSWRLNERHY GALTGLNKAE TAAQYGDEQV HIWRRSYDIR
PPLLEADDER NPKNDSRYAK LNESDIPLGE CLKDNVERVL PLWNESIAPA LKANKRVLLV
AHGNSIRSLI KYLDQMSDEA IMEVNVPNGI PLVYELDDNL KPIQHFYLD
