GPMA_MYCLB
ID GPMA_MYCLB Reviewed; 247 AA.
AC B8ZT86;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=MLBr02441;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA Rougemont J., Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX PubMed=25613812; DOI=10.1016/j.tube.2014.12.003;
RA Baugh L., Phan I., Begley D.W., Clifton M.C., Armour B., Dranow D.M.,
RA Taylor B.M., Muruthi M.M., Abendroth J., Fairman J.W., Fox D. III,
RA Dieterich S.H., Staker B.L., Gardberg A.S., Choi R., Hewitt S.N.,
RA Napuli A.J., Myers J., Barrett L.K., Zhang Y., Ferrell M., Mundt E.,
RA Thompkins K., Tran N., Lyons-Abbott S., Abramov A., Sekar A.,
RA Serbzhinskiy D., Lorimer D., Buchko G.W., Stacy R., Stewart L.J.,
RA Edwards T.E., Van Voorhis W.C., Myler P.J.;
RT "Increasing the structural coverage of tuberculosis drug targets.";
RL Tuberculosis 95:142-148(2015).
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: Homotetramer, dimer of dimers. {ECO:0000250|UniProtKB:P9WIC9}.
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; FM211192; CAR72540.1; -; Genomic_DNA.
DR RefSeq; WP_010908901.1; NC_011896.1.
DR PDB; 4EO9; X-ray; 2.45 A; A=1-247.
DR PDBsum; 4EO9; -.
DR AlphaFoldDB; B8ZT86; -.
DR SMR; B8ZT86; -.
DR PRIDE; B8ZT86; -.
DR EnsemblBacteria; CAR72540; CAR72540; MLBr02441.
DR KEGG; mlb:MLBr02441; -.
DR HOGENOM; CLU_033323_1_1_11; -.
DR OMA; RMLPYWY; -.
DR OrthoDB; 1122642at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000006900; 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 1: Evidence at protein level;
KW 3D-structure; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..247
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_1000149524"
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"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 35..50
FT /evidence="ECO:0007829|PDB:4EO9"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:4EO9"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:4EO9"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:4EO9"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4EO9"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4EO9"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4EO9"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:4EO9"
SQ SEQUENCE 247 AA; 27481 MW; 8962617FE1CF76DC CRC64;
MQQGNTATLI LLRHGESDWN ARNLFTGWVD VGLTDKGRAE AVRSGELLAE HNLLPDVLYT
SLLRRAITTA HLALDTADWL WIPVRRSWRL NERHYGALQG LDKAVTKARY GEERFMAWRR
SYDTPPPPIE KGSEFSQDAD PRYTDIGGGP LTECLADVVT RFLPYFTDVI VPDLRTGRTV
LIVAHGNSLR ALVKHLDEMS DDEVVGLNVP TGIPLRYDLD ADLRPVVPGG TYLDPEAAAA
VISQARP
