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APGM_DEIGD
ID   APGM_DEIGD              Reviewed;         408 AA.
AC   Q1IW58;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Dgeo_2232;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) 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; CP000359; ABF46526.1; -; Genomic_DNA.
DR   RefSeq; WP_011531347.1; NC_008025.1.
DR   AlphaFoldDB; Q1IW58; -.
DR   SMR; Q1IW58; -.
DR   STRING; 319795.Dgeo_2232; -.
DR   EnsemblBacteria; ABF46526; ABF46526; Dgeo_2232.
DR   KEGG; dge:Dgeo_2232; -.
DR   eggNOG; COG3635; Bacteria.
DR   HOGENOM; CLU_034906_2_0_0; -.
DR   OMA; IAFRCNF; -.
DR   OrthoDB; 1293048at2; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000002431; 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; Reference proteome.
FT   CHAIN           1..408
FT                   /note="Probable 2,3-bisphosphoglycerate-independent
FT                   phosphoglycerate mutase"
FT                   /id="PRO_1000068378"
SQ   SEQUENCE   408 AA;  43879 MW;  A0C9103980C6DC98 CRC64;
     MDLIETVRPL AKKTDSKILM VVLDGVGGLP LTVNGETELA TAKTPHLDAL AAESQLGLVE
     LVAAGITPGS GPGHLSLFGY DPLKYVVGRG ALSAVGIGVK LNAGDVAVRG NFASLGESRL
     IIDRRAGRPS NEKNAEVVAK LRAAIPEIDG TPVEIYSESE HRFVVVFRAT GTPLGADVSD
     VDPQVTGVPP RTAMAHDPAS ERTAHLVNAF VTRAEAALAD ESQVNGVLFR GYSDVPHFPN
     FDEIYQLRAA CIASYPMYKG LASLVGMDVL PVEGEEDALA GKVAALKEHW HDYDFFYWHV
     KKTDSTGEDG DFAAKVKKIE LFDALLPELR ALQPDVLCIV GDHSTPSKLA SHSWHPVPLL
     INSRYGRKDL AQRYTEEEAQ KGSLGLRRGT DVMPLLMANA LKLQKYGA
 
 
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