ID   APGM_METST              Reviewed;         409 AA.
AC   Q2NES7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
DE            Short=Phosphoglyceromutase;
DE            Short=BPG-independent PGAM;
DE            Short=aPGAM;
DE            EC=5.4.2.1;
GN   Name=apgM; OrderedLocusNames=Msp_1299;
OS   Methanosphaera stadtmanae (strain DSM 3091).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H.,
RA   Hedderich R., Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this
RT   human intestinal archaeon is restricted to methanol and H2 for methane
RT   formation and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
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.
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DR   EMBL; CP000102; ABC57676.1; -; Genomic_DNA.
DR   RefSeq; YP_448319.1; -.
DR   GeneID; 3856132; -.
DR   GenomeReviews; CP000102_GR; Msp_1299.
DR   KEGG; mst:Msp_1299; -.
DR   NMPDR; fig|339860.6.peg.1246; -.
DR   HOGENOM; Q2NES7; -.
DR   OMA; Q2NES7; ITGDHST.
DR   BioCyc; MSTA339860:MSP_1299-MON; -.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phospho...; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_01402; -; 1.
DR   InterPro; IPR004456; APGAM_arc.
DR   InterPro; IPR019304; bisP-indep_Pglycerate_Mutase.
DR   InterPro; IPR006124; Metalloenzyme.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   Pfam; PF10143; PhosphMutase; 1.
DR   PIRSF; PIRSF006392; IPGAM_arch; 1.
DR   ProDom; PD004704; APGAM_DeoB; 1.
DR   TIGRFAMs; TIGR00306; apgM; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Isomerase.
FT   CHAIN         1    409       2,3-bisphosphoglycerate-independent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_1000087366.
SQ   SEQUENCE   409 AA;  44482 MW;  45BF3DC89E05587D CRC64;
     MKGIIFVIDG MGDRPVKELG DKTPLENART PAMDKMVEEG ITGIMDTIRP GVRPGSDTAH
     LTLLGYDPYE VYTGRGPFEA AGINVEVKPG DIAFRCNFST ADENLIITDR RAGRIQSGTD
     KLAEVINNEV KLDDVEVIFK ESDGHRGVLV LRGNGLSDKI TDADPKHEGN KPKTVKPLDD
     SEEAKFTADI VNKFVEQSYE LLKDHPVNIE RIENGENPAN IILPRGVGAV PHVTPFEELY
     GLKGVCVAET GLIKGIAKIA GMDTIDIPGA TGGIDTDIDS VHKYIVDTIK SNKYDFILVN
     VDGADEAGHD GDIFGKRDFI EKVDNIMADL KDMDDIVLFV TADHSTPVSV KDHSGDPVPV
     FIKAPGLRVD DVKEYGERAA AKGGLCRIRG TDVLYIIRDL MNVTQKFGA
//