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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   23-MAY-2018, 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   ECO:0000313|EMBL:SBL84138.1};
GN   Synonyms=gpmA_1 {ECO:0000313|EMBL:SBL42827.1};
GN   ORFNames=AB185_27375 {ECO:0000313|EMBL:AKL37392.1}, C2U42_18550
GN   {ECO:0000313|EMBL:AUW11102.1}, C2U44_21495
GN   {ECO:0000313|EMBL:AUV93440.1}, CPZ29_22350
GN   {ECO:0000313|EMBL:PDO71997.1}, SAMEA2273575_01611
GN   {ECO:0000313|EMBL:SBL84138.1}, SAMEA2273639_00649
GN   {ECO:0000313|EMBL:SBL42827.1};
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|EMBL:SBL84138.1, ECO:0000313|Proteomes:UP000077674, ECO:0000313|Proteomes:UP000077706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2880STDY5682490 {ECO:0000313|EMBL:SBL84138.1,
RC   ECO:0000313|Proteomes:UP000077674}, and 2880STDY5682563
RC   {ECO:0000313|EMBL:SBL42827.1, ECO:0000313|Proteomes:UP000077706};
RG   Pathogen Informatics;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PDO71997.1, ECO:0000313|Proteomes:UP000229935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNM {ECO:0000313|EMBL:PDO71997.1,
RC   ECO:0000313|Proteomes:UP000229935};
RA   Yang S., Hemarajata P.;
RT   "Unusual Carbapenem Resistant but Ceftriaxone and Cefepime Susceptible
RT   Klebsiella oxytoca Isolated from a Blood Culture: a Case Report and
RT   Whole-genome Sequencing Investigation.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUV93440.1, ECO:0000313|Proteomes:UP000236441, ECO:0000313|Proteomes:UP000236461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KONIH2 {ECO:0000313|EMBL:AUW11102.1,
RC   ECO:0000313|Proteomes:UP000236441}, and KONIH4
RC   {ECO:0000313|EMBL:AUV93440.1, ECO:0000313|Proteomes:UP000236461};
RA   Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA   Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA   NISC Comparative Sequencing Program C., Henderson D.K., Palmore T.N.,
RA   Segre J.A., Frank K.M.;
RT   "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT   Bacterial Plasmids Conferring Carbapenem Resistance.";
RL   Submitted (JAN-2018) 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}.
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DR   EMBL; CP011636; AKL37392.1; -; Genomic_DNA.
DR   EMBL; CP026269; AUV93440.1; -; Genomic_DNA.
DR   EMBL; CP026285; AUW11102.1; -; Genomic_DNA.
DR   EMBL; PCMV01000017; PDO71997.1; -; Genomic_DNA.
DR   EMBL; FLAH01000002; SBL42827.1; -; Genomic_DNA.
DR   EMBL; FKYU01000005; SBL84138.1; -; Genomic_DNA.
DR   RefSeq; WP_004100351.1; NZ_PQKQ01000007.1.
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; UP000229935; Unassembled WGS sequence.
DR   Proteomes; UP000236441; Chromosome.
DR   Proteomes; UP000236461; 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:UP000035545,
KW   ECO:0000313|Proteomes:UP000077674, ECO:0000313|Proteomes:UP000077706,
KW   ECO:0000313|Proteomes:UP000229935};
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
//
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