ID   APGM_SULAC              Reviewed;         413 AA.
AC   Q4JAH5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Saci_0837;
OS   Sulfolobus acidocaldarius.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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.
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; CP000077; AAY80204.1; -; Genomic_DNA.
DR   RefSeq; YP_255497.1; -.
DR   GeneID; 3472708; -.
DR   GenomeReviews; CP000077_GR; Saci_0837.
DR   KEGG; sai:Saci_0837; -.
DR   NMPDR; fig|330779.3.peg.817; -.
DR   HOGENOM; Q4JAH5; -.
DR   OMA; Q4JAH5; ITGDHST.
DR   BioCyc; SACI330779:SACI_0837-MON; -.
DR   BRENDA; 5.4.2.1; 434.
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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Isomerase.
FT   CHAIN         1    413       2,3-bisphosphoglycerate-independent
FT                                phosphoglycerate mutase.
FT                                /FTId=PRO_0000138147.
SQ   SEQUENCE   413 AA;  45166 MW;  DEF8323941B0FA1D CRC64;
     MKQYKILLFI ADGLGDRPVT KLEHKTPLEA VEKPNIGELL KNSIAGLMDP ISPGIVPGSD
     TSHLAIFGID PFKYYRGRGA FEAIGAGARL KAGDVAFRGN FATVDNNLTV IDRRAGRKVD
     EAKDLVQELN SKIGEIDGVQ VKFYHGTEHR VAVVLSGKGL SDKISDTDPH ETGVKVKKSE
     ATDDTREAKI TAEVLNKLTN RIYDILSSSE LNKKRIERGE LPANIVLLRG AAQYVDLPKF
     YDYTKINAAA VSATALIKGI CSQIGMNVVT PKGATGGLDT NYIGKAEEAS KLLKEYDMVF
     LHLKATDAAS HDGNIDGKLY AISMIDKMIG RVLDIYGSEL IIAITGDHAT PVEVKEHTGD
     PVPFLLYVPY NIVADNVDDF NEKQLRKGSL RIKGLDVINL LLNYSYRYEK FGA
//