APGM_THET2
ID APGM_THET2 Reviewed; 406 AA.
AC Q72GG0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=TT_C1888;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS82230.1; -; Genomic_DNA.
DR RefSeq; WP_011174240.1; NC_005835.1.
DR AlphaFoldDB; Q72GG0; -.
DR SMR; Q72GG0; -.
DR STRING; 262724.TT_C1888; -.
DR EnsemblBacteria; AAS82230; AAS82230; TT_C1888.
DR KEGG; tth:TT_C1888; -.
DR eggNOG; COG3635; Bacteria.
DR HOGENOM; CLU_034906_2_0_0; -.
DR OMA; IAFRCNF; -.
DR OrthoDB; 1293048at2; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000592; 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; 3.30.70.2130; -; 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 InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
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..406
FT /note="Probable 2,3-bisphosphoglycerate-independent
FT phosphoglycerate mutase"
FT /id="PRO_0000138156"
SQ SEQUENCE 406 AA; 44283 MW; EFFAF2712A6BB30A CRC64;
MDLFPVLKEL AQKTPSKILL IVLDGVGGLP LEPGGPTELE AAKTPNLDRL AEESALGLLT
PVYPGLAPGS GPGHLALFGY DPFRYVVGRG ALSALGLGAD FREGDVALRG NFATLDPEGK
VVDRRAGRPP TEENQRVVAK LKEAIPRIED VEVHFYTESE HRFLVVLRGE GLGDAVTDTD
PQKTGLPPLK AKALDEASER TARLVNLLSE RIREVLKDEP RMNGALFRGA SKKPSFPRMQ
EVYKLTPAAI ASYPMYKGLA SLVGMEVLPV EGEGDALEGK LKALKENWGR YDFFYFHVKK
TDAMGEDGNF HGKVEKVELF DALLPEILAL GPDVLAITGD HSTPALLKAH SWHPVPLLLK
APYLRADEAR RFTEREAQRG SLGHLRGMEL MPLLLAHAGK LLKYGA
