APGM_THESQ
ID APGM_THESQ Reviewed; 401 AA.
AC B1LAP9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01402};
DE Short=aPGAM {ECO:0000255|HAMAP-Rule:MF_01402};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01402};
GN Name=apgM {ECO:0000255|HAMAP-Rule:MF_01402}; OrderedLocusNames=TRQ2_1050;
OS Thermotoga sp. (strain RQ2).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC unclassified Thermotoga.
OX NCBI_TaxID=126740;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RQ2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga sp. RQ2.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000255|HAMAP-Rule:MF_01402};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01402}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000255|HAMAP-Rule:MF_01402}.
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DR EMBL; CP000969; ACB09397.1; -; Genomic_DNA.
DR RefSeq; WP_012310909.1; NC_010483.1.
DR AlphaFoldDB; B1LAP9; -.
DR SMR; B1LAP9; -.
DR PRIDE; B1LAP9; -.
DR EnsemblBacteria; ACB09397; ACB09397; TRQ2_1050.
DR KEGG; trq:TRQ2_1050; -.
DR HOGENOM; CLU_034906_2_0_0; -.
DR OMA; IAFRCNF; -.
DR OrthoDB; 1293048at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001687; Chromosome.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.40.720.10; -; 2.
DR HAMAP; MF_01402_B; ApgM_B; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR PANTHER; PTHR31209; PTHR31209; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR TIGRFAMs; TIGR00306; apgM; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase.
FT CHAIN 1..401
FT /note="Probable 2,3-bisphosphoglycerate-independent
FT phosphoglycerate mutase"
FT /id="PRO_1000145453"
SQ SEQUENCE 401 AA; 44265 MW; 28D607F727742F99 CRC64;
MFDKQEFVSK LVTEEKAKIV LLVMDGLGDI PVNGKTPLQA ANTPNLDNLA KESDLGQTIP
VLPGITPGSG PGHLSLFGYD PIKYQIGRGI LEALGIGVEV GEKDVVARAN FATWDGKVVL
DRRAGRPATE ESAKVVQLLS EKIKKIEDVE ITFYPGKEHR FVVKFTGEGL GDKVTDADPQ
KEGHPMAWAE GLDEPSKKTA RIVNELIKKI AEVLKDNSKI NFALIRGFSK YPDLPKFPQV
YKMKAGAIAT YPMYRGLAKL VGMEIIETGQ TVADEIKTLK EKWNDYDFFY VHVKKTDSYG
EDGKFEEKVK VIEEVDAIIP EIVSLNPDVL VITGDHSTPV PLKAHSWHPV PLLIWSKYTR
RGLSQAFNEF ECARGTLGTI HASDVMTLAL AYAGRLEKFG A
