ID A0QR00_MYCS2 Unreviewed; 247 AA.
AC A0QR00;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 132.
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=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN OrderedLocusNames=MSMEG_0935 {ECO:0000313|EMBL:ABK73234.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK73234.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK73234.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000380,
CC ECO:0000256|HAMAP-Rule:MF_01039, 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; CP000480; ABK73234.1; -; Genomic_DNA.
DR RefSeq; WP_003892361.1; NZ_SIJM01000010.1.
DR RefSeq; YP_885338.1; NC_008596.1.
DR AlphaFoldDB; A0QR00; -.
DR SMR; A0QR00; -.
DR STRING; 246196.MSMEG_0935; -.
DR PaxDb; 246196-MSMEI_0912; -.
DR GeneID; 66739102; -.
DR KEGG; msm:MSMEG_0935; -.
DR PATRIC; fig|246196.19.peg.925; -.
DR eggNOG; COG0588; Bacteria.
DR OrthoDB; 9781415at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000757; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 87..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 114..115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 180
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01039,
FT ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 247 AA; 27300 MW; F23FE9A3E7B4D3FC CRC64;
MATLILLRHG ESQWNEKNLF TGWVDVDLTD KGRAEAVRGG QLMAEQGVLP DVLYTSLLRR
AITTAHLALD AADRLWIPVH RDWRLNERHY GALQGLDKAE TKEKYGEEQF MAWRRSYDTP
PPPIEKGSKY SQDADPRYAD IDGGPLTECL KDVVERFVPY YESAILPDLK AGKTVLIAAH
GNSLRALVKY LDGMSDEEVV GLNIPTGIPL RYDLDENLKP VKIGGEYLDP EAAAAGAAAV
AAQGAKK
//
