GPMA_CHLT2
ID GPMA_CHLT2 Reviewed; 226 AA.
AC B0B8U8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=CTL0091;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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 -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01039}.
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DR EMBL; AM884176; CAP03535.1; -; Genomic_DNA.
DR RefSeq; WP_009873325.1; NC_010287.1.
DR RefSeq; YP_001654182.1; NC_010287.1.
DR AlphaFoldDB; B0B8U8; -.
DR SMR; B0B8U8; -.
DR EnsemblBacteria; CAP03535; CAP03535; CTL0091.
DR KEGG; ctb:CTL0091; -.
DR PATRIC; fig|471472.4.peg.99; -.
DR HOGENOM; CLU_033323_1_4_0; -.
DR OMA; RMLPYWY; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000795; 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; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..226
FT /note="2,3-bisphosphoglycerate-dependent phosphoglycerate
FT mutase"
FT /id="PRO_1000135935"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT ACT_SITE 109
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 21..22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 109..112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 136..137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT BINDING 180..181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
FT SITE 179
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01039"
SQ SEQUENCE 226 AA; 25832 MW; 20F0E0CC734948FB CRC64;
MTLLILLRHG QSVWNQKNLF TGWVDIPLSQ QGIQEAIAAG ESIKHLPIDC IFTSTLVRSL
MTALLAMTNH SSQKVPYIVH EERPDMSRIH SQKEMEQMIP LFQSSALNER MYGELQGKNK
QEVAVQFGEE QVKLWRRSYR IAPPQGESLF DTGQRTLPYF QERIFPLLQQ GKNIFISAHG
NSLRSLIMDL EKLSEEQVLS LELPTGQPIV YEWTGQKFTK HAPSLG
