ID   A0A0H3CVH8_AMYMU        Unreviewed;       249 AA.
AC   A0A0H3CVH8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   17-FEB-2016, entry version 6.
DE   RecName: Full=2,3-bisphosphoglycerate-dependent phosphoglycerate mutase {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
DE            Short=BPG-dependent PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=PGAM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=Phosphoglyceromutase {ECO:0000256|HAMAP-Rule:MF_01039};
DE            Short=dPGM {ECO:0000256|HAMAP-Rule:MF_01039};
DE            EC=5.4.2.11 {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512};
GN   Name=gpm {ECO:0000313|EMBL:ADJ42278.1};
GN   Synonyms=gpmA {ECO:0000256|HAMAP-Rule:MF_01039};
GN   OrderedLocusNames=AMED_0456 {ECO:0000313|EMBL:ADJ42278.1};
OS   Amycolatopsis mediterranei (strain U-32).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=749927 {ECO:0000313|EMBL:ADJ42278.1, ECO:0000313|Proteomes:UP000000328};
RN   [1] {ECO:0000313|EMBL:ADJ42278.1, ECO:0000313|Proteomes:UP000000328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-32 {ECO:0000313|Proteomes:UP000000328};
RX   PubMed=20567260; DOI=10.1038/cr.2010.87;
RA   Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F.,
RA   Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N.,
RA   Zhang Z., Zhang Y., Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S.,
RA   Ding X., Zhao G.P.;
RT   "Complete genome sequence of the rifamycin SV-producing Amycolatopsis
RT   mediterranei U32 revealed its genetic characteristics in phylogeny and
RT   metabolism.";
RL   Cell Res. 20:1096-1108(2010).
CC   -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and
CC       3-phosphoglycerate. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|RuleBase:RU004512}.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC       {ECO:0000256|HAMAP-Rule:MF_01039, ECO:0000256|RuleBase:RU004512,
CC       ECO:0000256|SAAS:SAAS00055510}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|HAMAP-
CC       Rule:MF_01039, ECO:0000256|RuleBase:RU004512}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|HAMAP-Rule:MF_01039}.
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DR   EMBL; CP002000; ADJ42278.1; -; Genomic_DNA.
DR   RefSeq; WP_013222392.1; NC_014318.1.
DR   RefSeq; YP_003762680.1; NC_014318.1.
DR   ProteinModelPortal; A0A0H3CVH8; -.
DR   GeneID; 9434672; -.
DR   KEGG; amd:AMED_0456; -.
DR   KO; K01834; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000000328; Chromosome.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   HAMAP; MF_01039; PGAM_GpmA; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; PTHR11931; 1.
DR   Pfam; PF00300; His_Phos_1; 2.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000328};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS00444113};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS00444012}.
FT   REGION       11     18       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       24     25       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       90     93       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      117    118       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      185    186       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   ACT_SITE     12     12       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   ACT_SITE     90     90       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   BINDING      63     63       Substrate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   BINDING     101    101       Substrate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   SITE        184    184       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
SQ   SEQUENCE   249 AA;  27393 MW;  6B8DA933E4FE6802 CRC64;
     MGEIGTLVLL RHGQSTWNAE NLFTGWVDVP LSEQGEGEAR QGGRLLADAG LLPDVVHTSL
     LRRAISTANI ALDAADRHWI PVKRDWRLNE RHYGALQGKD KKQTLAEFGE EQFMLWRRSY
     DTPPPPIDPQ DEWSQVGDPR YAGLGDQAPL TECLKDVVER LLPYWESEIV PDLRAGKTVL
     VAAHGNSLRA LVKHLDGISD ADIAGLNIPT GIPLRYDLTE DLQPVKPGGE YLDPDAAKEA
     AAAVANQGR
//