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Database: UniProt/TrEMBL
Entry: G0TPJ6_MYCCP
LinkDB: G0TPJ6_MYCCP
Original site: G0TPJ6_MYCCP 
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
//
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