ID   GPMA_ALHEH              Reviewed;         232 AA.
AC   Q0A915;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, 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=Mlg_1323;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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DR   EMBL; CP000453; ABI56672.1; -; Genomic_DNA.
DR   RefSeq; YP_742162.1; -.
DR   GeneID; 4268662; -.
DR   GenomeReviews; CP000453_GR; Mlg_1323.
DR   KEGG; aeh:Mlg_1323; -.
DR   NMPDR; fig|187272.6.peg.1269; -.
DR   HOGENOM; Q0A915; -.
DR   OMA; Q0A915; FMLWRRS.
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_1000064026.
FT   ACT_SITE      9      9       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    182    182       By similarity.
FT   SITE         60     60       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
SQ   SEQUENCE   232 AA;  26825 MW;  648BEFD0EC0AD8C3 CRC64;
     MKKLVLLRHG QSIWNQENRF TGWHDVDLTE KGREEAQAAG QLMKRHGLRF DYAYTSVLKR
     AIRTLWIGLD ELDQMWIPVT KAWQLNERHY GALTGLNKAE TAEEYGAEQV HIWRRSYDTP
     PPPLDETSPY HPRHDPRYAS LKPEQLPATE SLALTLERVL PYWNERIVPT LRDCDNVLIA
     AHGNSIRALI KHLDGLDDEA IMKVEIATGD PLVYELDDAL AVVDKHYLRE RD
//