ID   GPMA_BLOPB              Reviewed;         232 AA.
AC   Q492W5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase;
DE            Short=Phosphoglyceromutase;
DE            Short=PGAM;
DE            Short=BPG-dependent PGAM;
DE            Short=dPGM;
DE            EC=5.4.2.1;
GN   Name=gpmA; OrderedLocusNames=BPEN_352;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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DR   EMBL; CP000016; AAZ40977.1; -; Genomic_DNA.
DR   RefSeq; YP_277852.1; -.
DR   GeneID; 3562809; -.
DR   GenomeReviews; CP000016_GR; BPEN_352.
DR   KEGG; bpn:BPEN_352; -.
DR   HOGENOM; Q492W5; -.
DR   OMA; Q492W5; RVLPYWY.
DR   BioCyc; CBLO291272:BPEN_352-MON; -.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphogl...; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   HAMAP; MF_01039; -; 1.
DR   InterPro; IPR001345; PG/BPGM_mutase.
DR   InterPro; IPR013078; PG_mutase.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; Phosphogly_mut1; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Isomerase.
FT   CHAIN         1    232       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_0000229107.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    185    185       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
SQ   SEQUENCE   232 AA;  26998 MW;  2AD8184F9C118E06 CRC64;
     MHITKLVLIR HGESQWNKEN RFTGWVDVDL SEKGRSEAQC AGRILKKNGF FFNYGYTSVL
     KRAIHTLWII LDQLDQAWLP IEKSWRLNER HYGALQGLNK DEAIKEYGYK TIQKWRRSFN
     VIPPNICGGN NQFIATNDNR YANISTDELP SSESLELTLK RVIPYWNQSI IPHIKKGQTI
     IIVAHGNSIR AIIKFLNHLN ESEIFQINVP TGVPLIYEFD KKANTVQHYY LK
//