ID G0TPJ6_MYCCP Unreviewed; 249 AA.
AC G0TPJ6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN Name=gpm1 {ECO:0000313|EMBL:CCC42829.1};
GN Synonyms=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN OrderedLocusNames=MCAN_04891 {ECO:0000313|EMBL:CCC42829.1};
OS Mycobacterium canettii (strain CIPT 140010059).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1048245 {ECO:0000313|EMBL:CCC42829.1, ECO:0000313|Proteomes:UP000008896};
RN [1] {ECO:0000313|EMBL:CCC42829.1, ECO:0000313|Proteomes:UP000008896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC42829.1,
RC ECO:0000313|Proteomes:UP000008896};
RX PubMed=22389744; DOI=10.1371/journal.pntd.0001552;
RA Bentley S.D., Comas I., Bryant J.M., Walker D., Smith N.H., Harris S.R.,
RA Thurston S., Gagneux S., Wood J., Antonio M., Quail M.A., Gehre F.,
RA Adegbola R.A., Parkhill J., de Jong B.C.;
RT "The Genome of Mycobacterium Africanum West African 2 Reveals a Lineage-
RT Specific Locus and Genome Erosion Common to the M. tuberculosis Complex.";
RL PLoS Negl. Trop. Dis. 6:e1552-e1552(2012).
RN [2] {ECO:0000313|EMBL:CCC42829.1, ECO:0000313|Proteomes:UP000008896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC42829.1,
RC ECO:0000313|Proteomes:UP000008896};
RX PubMed=23291586; DOI=10.1038/ng.2517;
RA Supply P., Marceau M., Mangenot S., Roche D., Rouanet C., Khanna V.,
RA Majlessi L., Criscuolo A., Tap J., Pawlik A., Fiette L., Orgeur M.,
RA Fabre M., Parmentier C., Frigui W., Simeone R., Boritsch E.C., Debrie A.S.,
RA Willery E., Walker D., Quail M.A., Ma L., Bouchier C., Salvignol G.,
RA Sayes F., Cascioferro A., Seemann T., Barbe V., Locht C., Gutierrez M.C.,
RA Leclerc C., Bentley S.D., Stinear T.P., Brisse S., Medigue C., Parkhill J.,
RA Cruveiller S., Brosch R.;
RT "Genomic analysis of smooth tubercle bacilli provides insights into
RT ancestry and pathoadaptation of Mycobacterium tuberculosis.";
RL Nat. Genet. 45:172-179(2013).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039,
CC ECO:0000256|RuleBase:RU004512}.
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:0000256|HAMAP-Rule:MF_01039,
CC ECO:0000256|RuleBase:RU004512};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_01039,
CC ECO:0000256|RuleBase:RU004512}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC ECO:0000256|HAMAP-Rule:MF_01039}.
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DR EMBL; HE572590; CCC42829.1; -; Genomic_DNA.
DR RefSeq; WP_003402379.1; NC_015848.1.
DR AlphaFoldDB; G0TPJ6; -.
DR SMR; G0TPJ6; -.
DR GeneID; 45424450; -.
DR KEGG; mce:MCAN_04891; -.
DR HOGENOM; CLU_033323_1_1_11; -.
DR OMA; RMLPYWY; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000008896; 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; Phosphoglycerate mutase-like; 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 NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01039};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01039}.
FT ACT_SITE 12
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 11..18
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 24..25
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 117..118
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 184..185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 183
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-3"
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
//