ID   APGM_METBU              Reviewed;         401 AA.
AC   Q12UL5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Mbur_1982;
OS   Methanococcoides burtonii (strain DSM 6242).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
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   Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcoides burtonii DSM 6242.";
RL   Submitted (MAR-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 BPG-independent phosphoglycerate mutase
CC       family. A-PGAM subfamily.
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DR   EMBL; CP000300; ABE52861.1; -; Genomic_DNA.
DR   RefSeq; YP_566611.1; -.
DR   GeneID; 3996934; -.
DR   GenomeReviews; CP000300_GR; Mbur_1982.
DR   KEGG; mbu:Mbur_1982; -.
DR   NMPDR; fig|259564.8.peg.1894; -.
DR   HOGENOM; Q12UL5; -.
DR   OMA; Q12UL5; GATGYLD.
DR   BioCyc; MBUR259564:MBUR_1982-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    401       2,3-bisphosphoglycerate-independent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_1000068381.
SQ   SEQUENCE   401 AA;  43174 MW;  D131D7F35BE291C4 CRC64;
     MKYIILIGDG MADHPLEELG GMTALQKANT PNMDQMTKNG LAGLAINVPE GYSPGSDVAN
     MSVMGYDPAL YYSGRAPLEA ASMGIPLEVN DVAFRCNLIT IRDGLITDHS AGHITSEEAR
     ELIEAVDAEL GSEGLKFYPG ISYRHLLVAS NGLGANADCT PPHDVIDGEI NDHMPRGDGS
     DVLGKLIEGS IPILEGHPIN EKRISEGKNP GNSVWFWGQG YAPSFRTFED LYGLTGSVIS
     AVDLIMGLGI YAGLDVIEVP GATGYLDTNY VGKAEFAMAS LKDKDFVVVH VEAPDEAGHM
     GDIEAKLQAI EDFDEKVVGT VLRAARESDE DYTIVVLPDH PTPIALRTHT SEPVPFVMYS
     TLEDEVDDVE TFDEDAMKKG SLGIVRGCDL VQLMMERAKQ A
//