ID   A0A076MNR5_AMYME        Unreviewed;       246 AA.
AC   A0A076MNR5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   17-FEB-2016, entry version 11.
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=gpmA {ECO:0000256|HAMAP-Rule:MF_01039,
GN   ECO:0000313|EMBL:AIJ20515.1};
GN   ORFNames=AMETH_0423 {ECO:0000313|EMBL:AIJ20515.1};
OS   Amycolatopsis methanolica 239.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ20515.1};
RN   [1] {ECO:0000313|EMBL:AIJ20515.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=239 {ECO:0000313|EMBL:AIJ20515.1};
RA   Tang B.;
RT   "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009110; AIJ20515.1; -; Genomic_DNA.
DR   RefSeq; WP_017986381.1; NZ_CP009110.1.
DR   EnsemblBacteria; AIJ20515; AIJ20515; AMETH_0423.
DR   KEGG; amq:AMETH_0423; -.
DR   KO; K01834; -.
DR   UniPathway; UPA00109; UER00186.
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   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      182    183       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        181    181       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
SQ   SEQUENCE   246 AA;  27054 MW;  8EE2D758A2C4DCDA CRC64;
     MAELGTLVLL RHGQSTWNAE NLFTGWVDVP LSELGQQEAR KGGELLAESG LLPDVVHTSL
     LRRAISTANI ALDIADRHWI PVRRDWRLNE RHYGALQGKN KKQVRDEFGE EQFMLWRRSY
     DVPPPPIERG SEFSQDTDVR YGPDAPLTEC LKDVVARLLP YWDSAIVPDL RAGKTVLVAA
     HGNSLRALVK HLDGISDDAI AGLNIPTGIP LRYDLDENLK PANPGGTYLD PEAAAAAAAA
     VANQGR
//