ID   GPMA1_NITEU             Reviewed;         234 AA.
AC   Q82XS4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1;
DE            Short=Phosphoglyceromutase 1;
DE            Short=PGAM 1;
DE            Short=BPG-dependent PGAM 1;
DE            Short=dPGM 1;
DE            EC=5.4.2.1;
GN   Name=gpmA1; OrderedLocusNames=NE0178;
OS   Nitrosomonas europaea.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / IFO 14298;
RX   MEDLINE=22586410; PubMed=12700255;
RX   DOI=10.1128/JB.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and
RT   obligate chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84089.1; -; Genomic_DNA.
DR   RefSeq; NP_840272.1; -.
DR   HSSP; P31217; 1E58.
DR   GeneID; 1081105; -.
DR   GenomeReviews; AL954747_GR; NE0178.
DR   KEGG; neu:NE0178; -.
DR   NMPDR; fig|228410.1.peg.171; -.
DR   HOGENOM; Q82XS4; -.
DR   OMA; Q82XS4; ILPEIRQ.
DR   BioCyc; NEUR228410:NE0178-MON; -.
DR   BRENDA; 5.4.2.1; 444.
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    234       2,3-bisphosphoglycerate-dependent
FT                                phosphoglycerate mutase 1.
FT                                /FTId=PRO_0000179897.
FT   ACT_SITE     15     15       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    188    188       By similarity.
FT   SITE         66     66       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
SQ   SEQUENCE   234 AA;  26889 MW;  40D612055414EF38 CRC64;
     MNEIQEPIRL VLLRHGQSIW NQDRHFTGWG DIVLSPQGEQ EALRAGHLLK QAGFTFDACF
     CSELQRASDT LAIVQSVMGL NHLSTYRTWR LNERHYGALE GMRPWAAIRK FGIWSTMKSQ
     IRFDAAPPLL MPDDPRAPVN QPRYAAVDRT QLPLAESMQQ TLERVRPLWQ ETILPEIRQG
     KRLLIVSHQN LLKTLVMQLE GLTGAQIMRL SITTGHPLCY ELDHSLVPVK RYYL
//