GPMA_BURP1
ID GPMA_BURP1 Reviewed; 249 AA.
AC Q3JWH7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BURPS1710b_0662;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEXES WITH
RP 2,3-DIPHOSPHOGLYCERATE; 3-PHOSPHO-D-GLYCERATE AND VANADATE, ACTIVE SITE,
RP AND SUBUNIT.
RC STRAIN=1710b;
RX PubMed=21904048; DOI=10.1107/s1744309111030405;
RA Davies D.R., Staker B.L., Abendroth J.A., Edwards T.E., Hartley R.,
RA Leonard J., Kim H., Rychel A.L., Hewitt S.N., Myler P.J., Stewart L.J.;
RT "An ensemble of structures of Burkholderia pseudomallei 2,3-
RT bisphosphoglycerate-dependent phosphoglycerate mutase.";
RL Acta Crystallogr. F 67:1044-1050(2011).
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 ECO:0000269|PubMed:21904048}.
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; CP000124; ABA50316.1; -; Genomic_DNA.
DR RefSeq; WP_004198007.1; NC_007434.1.
DR PDB; 3EZN; X-ray; 2.10 A; A/B=1-249.
DR PDB; 3FDZ; X-ray; 2.25 A; A/B=1-249.
DR PDB; 3GP3; X-ray; 1.50 A; A/B/C/D=1-249.
DR PDB; 3GP5; X-ray; 2.25 A; A/B=1-249.
DR PDB; 3GW8; X-ray; 1.93 A; A/B=1-249.
DR PDB; 3LNT; X-ray; 2.10 A; A/B=1-249.
DR PDBsum; 3EZN; -.
DR PDBsum; 3FDZ; -.
DR PDBsum; 3GP3; -.
DR PDBsum; 3GP5; -.
DR PDBsum; 3GW8; -.
DR PDBsum; 3LNT; -.
DR AlphaFoldDB; Q3JWH7; -.
DR SMR; Q3JWH7; -.
DR DrugBank; DB02580; Pentaglyme.
DR EnsemblBacteria; ABA50316; ABA50316; BURPS1710b_0662.
DR GeneID; 56594472; -.
DR KEGG; bpm:BURPS1710b_0662; -.
DR HOGENOM; CLU_033323_1_1_4; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 1122642at2; -.
DR BRENDA; 5.4.2.11; 1031.
DR UniPathway; UPA00109; UER00186.
DR EvolutionaryTrace; Q3JWH7; -.
DR Proteomes; UP000002700; Chromosome I.
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 1: Evidence at protein level;
KW 3D-structure; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..249
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000229113"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:21904048"
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 ECO:0000269|PubMed:21904048"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:21904048"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:21904048"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:21904048"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:21904048"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:21904048"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:21904048"
FT SITE 182
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:3GP3"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:3GP3"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3GP3"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3GP3"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3GP3"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3GP3"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:3EZN"
SQ SEQUENCE 249 AA; 27893 MW; E51933D372E4896E CRC64;
MYKLVLIRHG ESTWNKENRF TGWVDVDLTE QGNREARQAG QLLKEAGYTF DIAYTSVLKR
AIRTLWHVQD QMDLMYVPVV HSWRLNERHY GALSGLNKAE TAAKYGDEQV LVWRRSYDTP
PPALEPGDER APYADPRYAK VPREQLPLTE CLKDTVARVL PLWNESIAPA VKAGKQVLIA
AHGNSLRALI KYLDGISDAD IVGLNIPNGV PLVYELDESL TPIRHYYLGD QEAIAKAQAA
VAQQGKSAA
