ID   GPMA_BAUCH              Reviewed;         237 AA.
AC   Q1LTL3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=BCI_0251;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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 phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000238; ABF13818.1; -; Genomic_DNA.
DR   RefSeq; YP_588701.1; -.
DR   GeneID; 4056147; -.
DR   GenomeReviews; CP000238_GR; BCI_0251.
DR   KEGG; bci:BCI_0251; -.
DR   HOGENOM; Q1LTL3; -.
DR   OMA; Q1LTL3; 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    237       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_1000064031.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    184    184       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
SQ   SEQUENCE   237 AA;  27619 MW;  0CFFDEFBF8DCCFF9 CRC64;
     MTLNKLVLIR HGESKWNNEN RFTGWTDIDL SDQGRIEAKN AGQLLKQAGF IFDFAYTSVL
     KRAIHTLWYI LDELDQAWLP VEKSWRLNER HYGALQGLNK KKITVEYGEE QVQQWRRSLN
     ITPPELSDND KRLPIYDIRY AKLSLDQLPK AESLAMTINR IIPYWKGEIL PRINNGERVI
     IAAHGNSIRA IITLLDQLSE NELIQLNIPT GVPIIYEFNS QIKTIKHYYL SIVNKDY
//