APGM_THET8
ID APGM_THET8 Reviewed; 406 AA.
AC Q5SM27;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-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=TTHA0116;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; AP008226; BAD69939.1; -; Genomic_DNA.
DR RefSeq; WP_011227721.1; NC_006461.1.
DR RefSeq; YP_143382.1; NC_006461.1.
DR AlphaFoldDB; Q5SM27; -.
DR SMR; Q5SM27; -.
DR STRING; 300852.55771498; -.
DR EnsemblBacteria; BAD69939; BAD69939; BAD69939.
DR GeneID; 3167950; -.
DR KEGG; ttj:TTHA0116; -.
DR PATRIC; fig|300852.9.peg.114; -.
DR eggNOG; COG3635; Bacteria.
DR HOGENOM; CLU_034906_2_0_0; -.
DR OMA; IAFRCNF; -.
DR PhylomeDB; Q5SM27; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000000532; 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; Reference proteome.
FT CHAIN 1..406
FT /note="Probable 2,3-bisphosphoglycerate-independent
FT phosphoglycerate mutase"
FT /id="PRO_0000138157"
SQ SEQUENCE 406 AA; 44384 MW; AAD0B363520670BB CRC64;
MDLFPVLKEL AQKTPSKILL IVLDGVGGLP LEPGGPTELE AAKTPNLDRL AEESALGLLT
PVYPGLAPGS GPGHLALFGY DPFRYVVGRG ALSALGLGAD FREGDVALRG NFATLDPEGK
VVDRRAGRPP TEENQRVIAK LKEAIPRIED VEVLFYTESE HRFLVILRGE GLEDKVTDTD
PQKTGLPPLK AKALDEASER TARLVNLLSE RIREVLKDEP RMNGALFRGA SKKPSFPRMQ
EVYKLTPAAI ASYPMYKGLA SLVGMEVLPV EGEGDALEGK LKALKENWGR YDFFYFHVKK
TDAMGEDGNF HGKVEKVELF DALLPEILAL GPDVLAITGD HSTPALLKAH SWHPVPLLLK
APYLRADEAR RFTEREAQRG SLGHLRGVEL MPLLLAHAGK LLKYGA
