ID   GPMA_BORA1              Reviewed;         250 AA.
AC   Q2L0A6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=BAV0243;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(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.
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DR   EMBL; AM167904; CAJ47848.1; -; Genomic_DNA.
DR   RefSeq; YP_784781.1; -.
DR   GeneID; 6264588; -.
DR   GenomeReviews; AM167904_GR; BAV0243.
DR   KEGG; bav:BAV0243; -.
DR   NMPDR; fig|521.1.peg.2638; -.
DR   HOGENOM; Q2L0A6; -.
DR   OMA; Q2L0A6; 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    250       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_1000064032.
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   250 AA;  28377 MW;  B316A962F1CE1A32 CRC64;
     MYKLVLMRHG ESQWNLENRF TGWTDVDLTE VGREQARRAG ELLKREGYTF DLAYASVLKR
     AIRTLWIALD AMDAMYTPVG LNWRLNERHY GQLQGLNKAE TAAKYGDEQV LIWRRAYAIA
     PEPLDIDDPR HPRFDSRYAK IPAEQLPATE CLRDTVARVL PFWNESIAPA IRAGRRVLVA
     AHGNSLRALI KHLDNISDDA IVELNIPTGQ PLVYELDENL RPIRHYYLGD AAEIEAAMAA
     VAAQGKAKKD
//