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Database: UniProt/TrEMBL
Entry: A0A127L285_9ENTR
LinkDB: A0A127L285_9ENTR
Original site: A0A127L285_9ENTR 
ID   A0A127L285_9ENTR        Unreviewed;       262 AA.
AC   A0A127L285;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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:AMO48604.1};
GN   ORFNames=AKI40_2201 {ECO:0000313|EMBL:AMO48604.1};
OS   Enterobacter sp. FY-07.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=1692238 {ECO:0000313|EMBL:AMO48604.1, ECO:0000313|Proteomes:UP000070309};
RN   [1] {ECO:0000313|EMBL:AMO48604.1, ECO:0000313|Proteomes:UP000070309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FY-07 {ECO:0000313|EMBL:AMO48604.1,
RC   ECO:0000313|Proteomes:UP000070309};
RX   PubMed=26911736; DOI=10.1038/srep21863;
RA   Ji K., Wang W., Zeng B., Chen S., Zhao Q., Chen Y., Li G., Ma T.;
RT   "Bacterial cellulose synthesis mechanism of facultative anaerobe
RT   Enterobacter sp. FY-07.";
RL   Sci. Rep. 6:21863-21863(2016).
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:SAAS00750973}.
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   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01039}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000256|HAMAP-Rule:MF_01039,
CC       ECO:0000256|SAAS:SAAS00750934}.
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DR   EMBL; CP012487; AMO48604.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMO48604; AMO48604; AKI40_2201.
DR   KEGG; enf:AKI40_2201; -.
DR   PATRIC; fig|1692238.3.peg.2209; -.
DR   KO; K01834; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000070309; Chromosome.
DR   GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07067; HP_PGM_like; 1.
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:UP000070309};
KW   Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_01039};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS00750950};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01039,
KW   ECO:0000256|SAAS:SAAS00750866}.
FT   REGION       22     29       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       35     36       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      101    104       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      128    129       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      197    198       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   ACT_SITE     23     23       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   ACT_SITE    101    101       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   BINDING      74     74       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   BINDING     112    112       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   SITE        196    196       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
SQ   SEQUENCE   262 AA;  29763 MW;  6F4329D8AF5C45C5 CRC64;
     MLSFNQAHRS KCMAVTKLVL VRHGESQWNN ENRFTGWYDV DLSEKGVGEA KAAGKLLKEE
     GYTFDFAYTS VLKRAIHTLW NVLDELDQAW LPVEKSWKLN ERHYGALQGL NKAETAEKYG
     DEQVKQWRRG FAVTPPALTK DDERFPGHDP RYAKLTDAEL PQTESLALTI DRVIPYWNET
     ILPRLKSGER VIIAAHGNSL RALVKYLDNM SEDEILELNI PTGVPLVYEF DENFKPLKHY
     YLGNADEIAA KAAAVANQGK AK
//
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