ID   APGM_METBF              Reviewed;         398 AA.
AC   Q46E58;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
DE            Short=Phosphoglyceromutase;
DE            Short=BPG-independent PGAM;
DE            Short=aPGAM;
DE            EC=5.4.2.1;
GN   Name=apgM; OrderedLocusNames=Mbar_A0860;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(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 BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily.
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DR   EMBL; CP000099; AAZ69834.1; -; Genomic_DNA.
DR   RefSeq; YP_304414.1; -.
DR   GeneID; 3627272; -.
DR   GenomeReviews; CP000099_GR; Mbar_A0860.
DR   KEGG; mba:Mbar_A0860; -.
DR   NMPDR; fig|269797.3.peg.334; -.
DR   HOGENOM; Q46E58; -.
DR   OMA; Q46E58; GATGYLD.
DR   BioCyc; MBAR269797:MBAR_A0860-MON; -.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phospho...; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   HAMAP; MF_01402; -; 1.
DR   InterPro; IPR004456; APGAM_arc.
DR   InterPro; IPR019304; bisP-indep_Pglycerate_Mutase.
DR   InterPro; IPR013371; Homoserine_kin_put.
DR   InterPro; IPR006124; Metalloenzyme.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   Pfam; PF10143; PhosphMutase; 1.
DR   PIRSF; PIRSF006392; IPGAM_arch; 1.
DR   ProDom; PD004704; APGAM_DeoB; 1.
DR   TIGRFAMs; TIGR00306; apgM; 1.
DR   TIGRFAMs; TIGR02535; hyp_Hser_kinase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Isomerase.
FT   CHAIN         1    398       2,3-bisphosphoglycerate-independent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_1000068380.
SQ   SEQUENCE   398 AA;  42895 MW;  11A2604B38A2AF2A CRC64;
     MKYAVLIGDG MADYPIDKLG GKTILQAAQT PAMDYIAAHG KIGLAKTIPD GLPAGSDVAN
     MSILGYDPAV YYSGRAPLEA ASMGVALASD DVAFRCNLVT IEHGRIKDYS AGHISSEEAR
     ILIETLDAEL GNEELSFYPG ISYRHLLIAK DNLGAETECT PPHDITGKKI EEYLPGGKEG
     DFFSDLIKKS MIVLELHPVN LRRIEEGKNP ANSIWVWGQG SAPKFTPFRE LYEKTGAVIS
     AVDLLKGIGV YAGMDVIEVQ GATGYLDTNY EGKASAAIEV LKTRDLVFVH VEAPDEAGHE
     GSIDKKLKAV EDFDSRIVAP ILKHAKTSDE PFTILVLPDH PTPISIKTHA RDPVPFAVYR
     TDKTDSDSAE AFDEESAKKG SLGLVKASDL IGILVKAK
//