GenomeNet

Database: UniProt/TrEMBL
Entry: A0A181XLS1_KLEOX
LinkDB: A0A181XLS1_KLEOX
Original site: A0A181XLS1_KLEOX 
ID   A0A181XLS1_KLEOX        Unreviewed;       250 AA.
AC   A0A181XLS1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-SEP-2017, entry version 9.
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:SBL84138.1};
GN   Synonyms=gpmA_1 {ECO:0000313|EMBL:SBL42827.1};
GN   ORFNames=AB185_27375 {ECO:0000313|EMBL:AKL37392.1}, SAMEA2273575_01611
GN   {ECO:0000313|EMBL:SBL84138.1}, SAMEA2273639_00649
GN   {ECO:0000313|EMBL:SBL42827.1}, SAMEA2273697_01928
GN   {ECO:0000313|EMBL:SBL60740.1};
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=571 {ECO:0000313|EMBL:SBL84138.1, ECO:0000313|Proteomes:UP000077674};
RN   [1] {ECO:0000313|EMBL:AKL37392.1, ECO:0000313|Proteomes:UP000035545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAV1374 {ECO:0000313|EMBL:AKL37392.1,
RC   ECO:0000313|Proteomes:UP000035545};
RA   Sheppard A.E., Stoesser N., Wilson D., Sebra R., Kasarskis A.,
RA   Anson L., Giess A., Pankhurst L., Vaughan A., Grim C.J., Cox H.,
RA   Yeh A., Sifri C.D., Walker S., Peto T.E., Crook D.W., Mathers A.J.;
RT   "Rapid spread of a carbapenem resistance gene driven by multiple
RT   levels of genetic mobility.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000077674, ECO:0000313|Proteomes:UP000077706, ECO:0000313|Proteomes:UP000077898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2880STDY5682490 {ECO:0000313|EMBL:SBL84138.1,
RC   ECO:0000313|Proteomes:UP000077674}, 2880STDY5682563
RC   {ECO:0000313|EMBL:SBL42827.1, ECO:0000313|Proteomes:UP000077706}, and
RC   2880STDY5682622 {ECO:0000313|EMBL:SBL60740.1,
RC   ECO:0000313|Proteomes:UP000077898};
RG   Pathogen Informatics;
RL   Submitted (MAY-2016) 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: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}.
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; CP011636; AKL37392.1; -; Genomic_DNA.
DR   EMBL; FLAH01000002; SBL42827.1; -; Genomic_DNA.
DR   EMBL; FLAB01000004; SBL60740.1; -; Genomic_DNA.
DR   EMBL; FKYU01000005; SBL84138.1; -; Genomic_DNA.
DR   RefSeq; WP_004100351.1; NZ_MKCU01000013.1.
DR   EnsemblBacteria; SBL42827; SBL42827; SAMEA2273639_00649.
DR   EnsemblBacteria; SBL60740; SBL60740; SAMEA2273697_01928.
DR   EnsemblBacteria; SBL84138; SBL84138; SAMEA2273575_01611.
DR   GeneID; 29382203; -.
DR   KEGG; koc:AB185_27375; -.
DR   PATRIC; fig|571.108.peg.1696; -.
DR   KO; K01834; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000035545; Chromosome.
DR   Proteomes; UP000077674; Unassembled WGS sequence.
DR   Proteomes; UP000077706; Unassembled WGS sequence.
DR   Proteomes; UP000077898; Unassembled WGS sequence.
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:UP000035545,
KW   ECO:0000313|Proteomes:UP000077674, ECO:0000313|Proteomes:UP000077706,
KW   ECO:0000313|Proteomes:UP000077898};
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, ECO:0000313|EMBL:SBL84138.1}.
FT   REGION       10     17       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       23     24       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION       89     92       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01039}.
FT   REGION      116    117       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     11     11       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   ACT_SITE     89     89       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
FT   BINDING      62     62       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01039}.
FT   SITE        184    184       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01039}.
SQ   SEQUENCE   250 AA;  28288 MW;  B8968761C81A4E5D CRC64;
     MAVTKLVLVR HGESQWNNEN RFTGWYDVDL SEKGVGEAKA AGKLLKEEGF SFDFAYTSVL
     KRAIHTLWNV LDELDQAWLP VEKSWKLNER HYGALQGLNK AETAEKYGDE QVKQWRRGFA
     VTPPELTKDD ERYPGHDPRY AKLTDAELPT TESLALTIDR VVPYWNETIL PRLKSGERVI
     IAAHGNSLRA LVKYLDNMGE AEILELNIPT GVPLVYEFDE NFKPIKHYYL GNADEIAAKA
     AAVANQGKAK
//
DBGET integrated database retrieval system