ID   W9DNK8_9PSEU            Unreviewed;       249 AA.
AC   W9DNK8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   17-FEB-2016, entry version 16.
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   ORFNames=AmyhaDRAFT_0298 {ECO:0000313|EMBL:ETA66538.1};
OS   Amycolatopsis halophila YIM 93223.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=592678 {ECO:0000313|EMBL:ETA66538.1};
RN   [1] {ECO:0000313|EMBL:ETA66538.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YIM 93223 {ECO:0000313|EMBL:ETA66538.1};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N.,
RA   Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N.,
RA   Hua S.X., Woyke T.;
RL   Submitted (AUG-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ETA66538.1}.
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; AZAK01000001; ETA66538.1; -; Genomic_DNA.
DR   RefSeq; WP_034267196.1; NZ_KI632509.1.
DR   EnsemblBacteria; ETA66538; ETA66538; AmyhaDRAFT_0298.
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      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;  27175 MW;  8904FE12AA8767F1 CRC64;
     MGEKSTLVLL RHGQSTWNAE NLFTGWVDVP LSAQGEDEAR RGGELLAETG MLPDVVHTSL
     LRRAISTANI ALDVADRHWI DVRRDWRLNE RHYGALQGKN KKQTLDEYGE DQFMLWRRSY
     DTPPPPIEKG SEFSQDADVR YAGLGAEMPL TECLADVVAR LLPYWESAIV PDLRSGKTVL
     VAAHGNSLRA LVKHLDGISD ADIAGLNIPT GIPLRYDLDA NLAPLNPGGT YLDPDAAADA
     AAAVAAQGR
//