GPMA_MYCTU
ID GPMA_MYCTU Reviewed; 249 AA.
AC P9WIC9; L0T6M6; P0A5R6; Q11140;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:15735341};
DE Short=BPG-dependent PGAM {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:15735341};
DE Short=PGAM {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:15735341};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000303|PubMed:15735341};
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}; Synonyms=gpm, gpm1, pgm;
GN OrderedLocusNames=Rv0489; ORFNames=MTCY20G9.15;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP AND SUBUNIT.
RX PubMed=15735341; DOI=10.1107/s0907444904033190;
RA Muller P., Sawaya M.R., Pashkov I., Chan S., Nguyen C., Wu Y., Perry L.J.,
RA Eisenberg D.;
RT "The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis
RT phosphoglycerate mutase.";
RL Acta Crystallogr. D 61:309-315(2005).
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:0000269|PubMed:15735341}.
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; AL123456; CCP43223.1; -; Genomic_DNA.
DR PIR; D70744; D70744.
DR RefSeq; WP_003402379.1; NZ_NVQJ01000002.1.
DR RefSeq; YP_177731.1; NC_000962.3.
DR PDB; 1RII; X-ray; 1.70 A; A/B/C/D=1-249.
DR PDBsum; 1RII; -.
DR AlphaFoldDB; P9WIC9; -.
DR SMR; P9WIC9; -.
DR STRING; 83332.Rv0489; -.
DR PaxDb; P9WIC9; -.
DR DNASU; 887183; -.
DR GeneID; 45424450; -.
DR GeneID; 887183; -.
DR KEGG; mtu:Rv0489; -.
DR TubercuList; Rv0489; -.
DR eggNOG; COG0588; Bacteria.
DR OMA; RMLPYWY; -.
DR PhylomeDB; P9WIC9; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
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; Reference proteome.
FT CHAIN 1..249
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_0000179893"
FT ACT_SITE 12
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 11..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:15735341"
FT BINDING 24..25
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:15735341"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:15735341"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039,
FT ECO:0000269|PubMed:15735341"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 117..118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 183
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:1RII"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1RII"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:1RII"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1RII"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1RII"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1RII"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1RII"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:1RII"
SQ SEQUENCE 249 AA; 27216 MW; 7063E6B91CDFF339 CRC64;
MANTGSLVLL RHGESDWNAL NLFTGWVDVG LTDKGQAEAV RSGELIAEHD LLPDVLYTSL
LRRAITTAHL ALDSADRLWI PVRRSWRLNE RHYGALQGLD KAETKARYGE EQFMAWRRSY
DTPPPPIERG SQFSQDADPR YADIGGGPLT ECLADVVARF LPYFTDVIVG DLRVGKTVLI
VAHGNSLRAL VKHLDQMSDD EIVGLNIPTG IPLRYDLDSA MRPLVRGGTY LDPEAAAAGA
AAVAGQGRG
