ID   APGM2_METTH             Reviewed;         402 AA.
AC   O26518;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2;
DE            Short=BPG-independent PGAM 2;
DE            Short=Phosphoglyceromutase 2;
DE            Short=aPGAM 2;
DE            EC=5.4.2.12;
GN   Name=apgM2; OrderedLocusNames=MTH_418;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC       phosphoglycerate. {ECO:0000250}.
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;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000666; AAB84924.1; -; Genomic_DNA.
DR   PIR; D69154; D69154.
DR   AlphaFoldDB; O26518; -.
DR   SMR; O26518; -.
DR   STRING; 187420.MTH_418; -.
DR   EnsemblBacteria; AAB84924; AAB84924; MTH_418.
DR   KEGG; mth:MTH_418; -.
DR   PATRIC; fig|187420.15.peg.388; -.
DR   HOGENOM; CLU_034906_2_0_2; -.
DR   OMA; FRCNLIT; -.
DR   BioCyc; MetaCyc:MON-14535; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000005223; 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_A; ApgM_A; 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.
DR   TIGRFAMs; TIGR02535; hyp_Hser_kinase; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..402
FT                   /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT                   mutase 2"
FT                   /id="PRO_0000138140"
SQ   SEQUENCE   402 AA;  44100 MW;  EB5EF3B8A18E7617 CRC64;
     MITMKHVILV GDGMADYPLD ELDGKTPLQV ADKPNMDQLA GMGACGLLRT VPEGMEAGSD
     VANLSIMGYD PRRYYTGRGP LEAASIGVEL GDDDVAFRCN LINADERIVD FNAGHIETAE
     ASSLIDALNH ELETRGRFYA GVSYRNLFVI EGRGYTSVRV EPPHDIVGES VAAHLPSGSE
     EADHIRELML ESAGVLRSHE VNLKRESMGK RPATMIWLWG QGLRPSMEPF SERYGIRGAT
     ITAVDLIKGL GVYAGLENIH VPGATGYLDT DYRAKGRYAA GALEEYDFLY VHVEAPDEAG
     HAGDAEEKIR AIENIDRFVL GRLLDALSDH EHRIAVLPDH PTPIEIRTHV PDPVPCILAG
     DGVDADQVKS YDEFTVREGS LGTWEAHRLM EIMMDPAARL RQ