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Phosphoglucomutase (PGM) (EC 5.4.2.2) (Glucose phosphomutase)

 PGM_DROME               Reviewed;         560 AA.
Q9VUY9; Q95VC1; Q9GN12; Q9GN65; Q9GN80; Q9GN99; Q9GNA0; Q9GNH5;
Q9GNJ1; Q9GQ71; Q9GQ72; Q9GQ73; Q9GQ74; Q9GQ75; Q9GQ76; Q9GQ77;
Q9GQ78; Q9GQ79; Q9GQ80;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=Phosphoglucomutase;
Short=PGM;
EC=5.4.2.2;
AltName: Full=Glucose phosphomutase;
Name=Pgm {ECO:0000312|FlyBase:FBgn0003076}; ORFNames=CG5165;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG44919.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-9; VAL-50; ILE-52;
VAL-52; TYR-64; ALA-109; LYS-197; LYS-235; LEU-240; ASP-245; SER-338;
MET-341; LYS-346; SER-465; LEU-484; THR-530 AND PHE-540.
STRAIN=B4039 {ECO:0000312|EMBL:AAG44916.1},
dpf95_100.3 {ECO:0000312|EMBL:AAG44900.1},
dpf95_13.0 {ECO:0000312|EMBL:AAG44928.1},
dpf95_2.0 {ECO:0000312|EMBL:AAG44903.1},
dpf95_2.1 {ECO:0000312|EMBL:AAG44920.1},
dpf95_23.1 {ECO:0000312|EMBL:AAG44925.1},
dpf95_29.3 {ECO:0000312|EMBL:AAG44924.1},
dpf95_3.0 {ECO:0000312|EMBL:AAG44927.1},
dpf95_36.4 {ECO:0000312|EMBL:AAG44923.1},
dpf95_38.3 {ECO:0000312|EMBL:AAG44913.1},
dpf95_4.2 {ECO:0000312|EMBL:AAG44914.1},
dpf95_4.3 {ECO:0000312|EMBL:AAG44926.1},
dpf95_44.3 {ECO:0000312|EMBL:AAG44912.1},
dpf95_48.2 {ECO:0000312|EMBL:AAG44902.1},
dpf95_53.1 {ECO:0000312|EMBL:AAG44904.1},
dpf95_54.0 {ECO:0000312|EMBL:AAG44921.1},
dpf95_56.1 {ECO:0000312|EMBL:AAG44910.1},
dpf95_56.2 {ECO:0000312|EMBL:AAG44930.1},
dpf95_73.1 {ECO:0000312|EMBL:AAG44919.1},
dpf95_77.4 {ECO:0000312|EMBL:AAG44918.1},
dpf95_84.3 {ECO:0000312|EMBL:AAG44922.1},
dpf95_85.1 {ECO:0000312|EMBL:AAG44911.1},
dpf95_90.2 {ECO:0000312|EMBL:AAG44917.1},
dpf95_94.1 {ECO:0000312|EMBL:AAG44915.1},
hfl97_1.0 {ECO:0000312|EMBL:AAG44905.1},
hfl97_13.0 {ECO:0000312|EMBL:AAG44906.1},
hfl97_15.0 {ECO:0000312|EMBL:AAG44907.1},
hfl97_50.0 {ECO:0000312|EMBL:AAG44908.1},
hfl97_93.0 {ECO:0000312|EMBL:AAG44901.1},
md90_709.1 {ECO:0000312|EMBL:AAG44909.1},
sc96_5.3 {ECO:0000312|EMBL:AAG44929.1},
zim_11S {ECO:0000312|EMBL:AAG44941.1},
zim_15S {ECO:0000312|EMBL:AAG44937.1},
zim_23H {ECO:0000312|EMBL:AAG44933.1},
zim_24S {ECO:0000312|EMBL:AAG44940.1},
zim_26H {ECO:0000312|EMBL:AAG44931.1},
zim_35S {ECO:0000312|EMBL:AAG44939.1},
zim_36H {ECO:0000312|EMBL:AAG44935.1},
zim_38H {ECO:0000312|EMBL:AAG44934.1},
zim_39H {ECO:0000312|EMBL:AAG44936.1},
zim_44H {ECO:0000312|EMBL:AAG44932.1},
zim_48S {ECO:0000312|EMBL:AAG44942.1},
zim_49S {ECO:0000312|EMBL:AAG44943.1}, and
zim_51S {ECO:0000312|EMBL:AAG44938.1};
PubMed=11102370;
Verrelli B.C., Eanes W.F.;
"Extensive amino acid polymorphism at the pgm locus is consistent with
adaptive protein evolution in Drosophila melanogaster.";
Genetics 156:1737-1752(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL08565.1}
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-6; THR-9; LEU-240 AND
ASP-245.
STRAIN=Canton-S {ECO:0000312|EMBL:AAL08568.1};
PubMed=12049662; DOI=10.1186/gb-2002-3-5-research0021;
Allikian M.J., Deckert-Cruz D., Rose M.R., Landis G.N., Tower J.;
"Doxycycline-induced expression of sense and inverted-repeat
constructs modulates phosphogluconate mutase (Pgm) gene expression in
adult Drosophila melanogaster.";
Genome Biol. 3:RESEARCH0021.1-RESEARCH0021.10(2002).
[3] {ECO:0000312|EMBL:AAF49533.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF49533.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5] {ECO:0000312|EMBL:AAQ22512.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22512.1}; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
AND TISSUE SPECIFICITY.
PubMed=44190; DOI=10.1007/BF00504306;
Fucci L., Gaudio L., Rao R., Spano A., Carfagna M.;
"Properties of the two common electrophoretic variants of
phosphoglucomutase in Drosophila melanogaster.";
Biochem. Genet. 17:825-836(1979).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[8] {ECO:0000305}
CHARACTERIZATION OF VARIANTS THR-9; GLN-17; ASN-28; MET-36; LYS-197;
LYS-235; LEU-240; ASP-245; SER-338; MET-341; LYS-346; LYS-351;
SER-465; LEU-484 AND THR-530.
PubMed=11290720;
Verrelli B.C., Eanes W.F.;
"Clinal variation for amino acid polymorphisms at the Pgm locus in
Drosophila melanogaster.";
Genetics 157:1649-1663(2001).
[9] {ECO:0000305}
CHARACTERIZATION OF VARIANTS THR-9; MET-36; VAL-52; LEU-240; ASP-245;
MET-341; SER-465; LEU-484 AND THR-530.
PubMed=11560897;
Verrelli B.C., Eanes W.F.;
"The functional impact of Pgm amino acid polymorphism on glycogen
content in Drosophila melanogaster.";
Genetics 159:201-210(2001).
-!- FUNCTION: This enzyme participates in both the breakdown and
synthesis of glucose. {ECO:0000269|PubMed:44190}.
-!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
6-phosphate. {ECO:0000269|PubMed:44190}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:44190};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:44190};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=140 uM for glucose-1-phosphate (for Pgm-A at pH 6.0)
{ECO:0000269|PubMed:44190};
KM=158 uM for glucose-1-phosphate (for Pgm-A at pH 7.4)
{ECO:0000269|PubMed:44190};
KM=4.4 uM for glucose-1,6-diphosphate (for Pgm-A at pH 6.0)
{ECO:0000269|PubMed:44190};
KM=4.4 uM for glucose-1,6-diphosphate (for Pgm-A at pH 7.4)
{ECO:0000269|PubMed:44190};
KM=142.2 uM for glucose-1-phosphate (for Pgm-B at pH 6.0)
{ECO:0000269|PubMed:44190};
KM=112.4 uM for glucose-1-phosphate (for Pgm-B at pH 7.4)
{ECO:0000269|PubMed:44190};
KM=21.7 uM for glucose-1,6-diphosphate (for Pgm-B at pH 6.0)
{ECO:0000269|PubMed:44190};
KM=4.2 uM for glucose-1,6-diphosphate (for Pgm-B at pH 7.4)
{ECO:0000269|PubMed:44190};
Vmax=32.8 umol/min/mg enzyme toward glucose-1-phosphate (for
Pgm-A at pH 6.0) {ECO:0000269|PubMed:44190};
Vmax=129 umol/min/mg enzyme toward glucose-1-phosphate (for Pgm-
A at pH 7.4) {ECO:0000269|PubMed:44190};
Vmax=20.8 umol/min/mg enzyme toward glucose-1,6-diphosphate (for
Pgm-A at pH 6.0) {ECO:0000269|PubMed:44190};
Vmax=111 umol/min/mg enzyme toward glucose-1,6-diphosphate (for
Pgm-A at pH 7.4) {ECO:0000269|PubMed:44190};
Vmax=35 umol/min/mg enzyme toward glucose-1-phosphate (for Pgm-B
at pH 6.0) {ECO:0000269|PubMed:44190};
Vmax=120.9 umol/min/mg enzyme toward glucose-1-phosphate (for
Pgm-B at pH 7.4) {ECO:0000269|PubMed:44190};
Vmax=14.5 umol/min/mg enzyme toward glucose-1,6-diphosphate (for
Pgm-B at pH 6.0) {ECO:0000269|PubMed:44190};
Vmax=100 umol/min/mg enzyme toward glucose-1,6-diphosphate (for
Pgm-B at pH 7.4) {ECO:0000269|PubMed:44190};
pH dependence:
Optimum pH is 7.4-7.6. {ECO:0000269|PubMed:44190};
Temperature dependence:
Pgm-A is more thermostable than Pgm-B.
{ECO:0000269|PubMed:44190};
-!- TISSUE SPECIFICITY: Localized primarily to fat bodies in third
instar larvae. {ECO:0000269|PubMed:44190}.
-!- POLYMORPHISM: The polymorphisms show clinal variations. There are
2 common electrophoretic variants, Pgm-A and Pgm-B, which differ
in their kinetic and stability parameters. Variations in Pgm are
associated with differences in enzyme activity and glycogen
content.
-!- SIMILARITY: Belongs to the phosphohexose mutase family.
{ECO:0000269|PubMed:44190}.
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EMBL; AF290313; AAG44900.1; -; Genomic_DNA.
EMBL; AF290314; AAG44901.1; -; Genomic_DNA.
EMBL; AF290315; AAG44902.1; -; Genomic_DNA.
EMBL; AF290316; AAG44903.1; -; Genomic_DNA.
EMBL; AF290317; AAG44904.1; -; Genomic_DNA.
EMBL; AF290318; AAG44905.1; -; Genomic_DNA.
EMBL; AF290319; AAG44906.1; -; Genomic_DNA.
EMBL; AF290320; AAG44907.1; -; Genomic_DNA.
EMBL; AF290321; AAG44908.1; -; Genomic_DNA.
EMBL; AF290322; AAG44909.1; -; Genomic_DNA.
EMBL; AF290323; AAG44910.1; -; Genomic_DNA.
EMBL; AF290324; AAG44911.1; -; Genomic_DNA.
EMBL; AF290325; AAG44912.1; -; Genomic_DNA.
EMBL; AF290326; AAG44913.1; -; Genomic_DNA.
EMBL; AF290327; AAG44914.1; -; Genomic_DNA.
EMBL; AF290328; AAG44915.1; -; Genomic_DNA.
EMBL; AF290329; AAG44916.1; -; Genomic_DNA.
EMBL; AF290330; AAG44917.1; -; Genomic_DNA.
EMBL; AF290331; AAG44918.1; -; Genomic_DNA.
EMBL; AF290332; AAG44919.1; -; Genomic_DNA.
EMBL; AF290333; AAG44920.1; -; Genomic_DNA.
EMBL; AF290334; AAG44921.1; -; Genomic_DNA.
EMBL; AF290335; AAG44922.1; -; Genomic_DNA.
EMBL; AF290336; AAG44923.1; -; Genomic_DNA.
EMBL; AF290337; AAG44924.1; -; Genomic_DNA.
EMBL; AF290338; AAG44925.1; -; Genomic_DNA.
EMBL; AF290339; AAG44926.1; -; Genomic_DNA.
EMBL; AF290340; AAG44927.1; -; Genomic_DNA.
EMBL; AF290341; AAG44928.1; -; Genomic_DNA.
EMBL; AF290342; AAG44929.1; -; Genomic_DNA.
EMBL; AF290343; AAG44930.1; -; Genomic_DNA.
EMBL; AF290344; AAG44931.1; -; Genomic_DNA.
EMBL; AF290345; AAG44932.1; -; Genomic_DNA.
EMBL; AF290346; AAG44933.1; -; Genomic_DNA.
EMBL; AF290347; AAG44934.1; -; Genomic_DNA.
EMBL; AF290348; AAG44935.1; -; Genomic_DNA.
EMBL; AF290349; AAG44936.1; -; Genomic_DNA.
EMBL; AF290350; AAG44937.1; -; Genomic_DNA.
EMBL; AF290351; AAG44938.1; -; Genomic_DNA.
EMBL; AF290352; AAG44939.1; -; Genomic_DNA.
EMBL; AF290353; AAG44940.1; -; Genomic_DNA.
EMBL; AF290354; AAG44941.1; -; Genomic_DNA.
EMBL; AF290355; AAG44942.1; -; Genomic_DNA.
EMBL; AF290356; AAG44943.1; -; Genomic_DNA.
EMBL; AF416981; AAL08565.1; -; mRNA.
EMBL; AF416982; AAL08566.1; -; mRNA.
EMBL; AF416983; AAL08567.1; -; mRNA.
EMBL; AF416984; AAL08568.1; -; mRNA.
EMBL; AE014296; AAF49533.1; -; Genomic_DNA.
EMBL; BT010043; AAQ22512.1; -; mRNA.
RefSeq; NP_524675.1; NM_079936.3.
UniGene; Dm.1872; -.
ProteinModelPortal; Q9VUY9; -.
SMR; Q9VUY9; -.
BioGrid; 68773; 5.
IntAct; Q9VUY9; 7.
MINT; MINT-1564518; -.
STRING; 7227.FBpp0075247; -.
iPTMnet; Q9VUY9; -.
PaxDb; Q9VUY9; -.
PRIDE; Q9VUY9; -.
EnsemblMetazoa; FBtr0075492; FBpp0075247; FBgn0003076.
GeneID; 44010; -.
KEGG; dme:Dmel_CG5165; -.
CTD; 44010; -.
FlyBase; FBgn0003076; Pgm.
eggNOG; KOG0625; Eukaryota.
eggNOG; COG0033; LUCA.
GeneTree; ENSGT00390000011831; -.
InParanoid; Q9VUY9; -.
KO; K01835; -.
OMA; DIYKIYA; -.
OrthoDB; EOG091G0HZ0; -.
PhylomeDB; Q9VUY9; -.
ChiTaRS; Pgm; fly.
GenomeRNAi; 44010; -.
PRO; PR:Q9VUY9; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0003076; -.
Genevisible; Q9VUY9; DM.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004614; F:phosphoglucomutase activity; IDA:FlyBase.
GO; GO:0004619; F:phosphoglycerate mutase activity; IMP:FlyBase.
GO; GO:0060361; P:flight; IMP:FlyBase.
GO; GO:0019388; P:galactose catabolic process; IBA:GO_Central.
GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
GO; GO:0005978; P:glycogen biosynthetic process; IMP:FlyBase.
GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
Gene3D; 3.30.310.50; -; 1.
InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
InterPro; IPR005843; A-D-PHexomutase_C.
InterPro; IPR036900; A-D-PHexomutase_C_sf.
InterPro; IPR016066; A-D-PHexomutase_CS.
InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
Pfam; PF02878; PGM_PMM_I; 1.
Pfam; PF02879; PGM_PMM_II; 1.
Pfam; PF02880; PGM_PMM_III; 1.
Pfam; PF00408; PGM_PMM_IV; 1.
PRINTS; PR00509; PGMPMM.
SUPFAM; SSF53738; SSF53738; 3.
SUPFAM; SSF55957; SSF55957; 1.
PROSITE; PS00710; PGM_PMM; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Glucose metabolism;
Isomerase; Magnesium; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 560 Phosphoglucomutase.
/FTId=PRO_0000147789.
REGION 116 117 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
REGION 292 293 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
REGION 376 378 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
ACT_SITE 116 116 Phosphoserine intermediate.
{ECO:0000250|UniProtKB:P00949}.
METAL 116 116 Magnesium; via phosphate group.
{ECO:0000250|UniProtKB:P00949}.
METAL 288 288 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
METAL 290 290 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
METAL 292 292 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
BINDING 20 20 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 24 24 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 129 129 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 357 357 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 389 389 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 515 515 Substrate.
{ECO:0000250|UniProtKB:P00949}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VARIANT 6 6 E -> G. {ECO:0000269|PubMed:12049662}.
VARIANT 9 9 A -> T (in strain: dpf95_94.1 and
zim_26H). {ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897,
ECO:0000269|PubMed:12049662}.
VARIANT 17 17 K -> Q. {ECO:0000269|PubMed:11290720}.
VARIANT 28 28 K -> N. {ECO:0000269|PubMed:11290720}.
VARIANT 36 36 T -> M. {ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897}.
VARIANT 50 50 A -> V (in strain: zim_38H).
{ECO:0000269|PubMed:11102370}.
VARIANT 52 52 A -> I (in strain: zim_36H).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11560897}.
VARIANT 52 52 A -> V (in strain: dpf95_48.2,
dpf95_100.3 and hfl97_93.0).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11560897}.
VARIANT 64 64 F -> Y (in strain: zim_36H).
{ECO:0000269|PubMed:11102370}.
VARIANT 109 109 G -> A (in strain: B4039).
{ECO:0000269|PubMed:11102370}.
VARIANT 197 197 E -> K (in strain: dpf95_56.1).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720}.
VARIANT 235 235 E -> K (in strain: dpf95_13.0).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720}.
VARIANT 240 240 R -> L (in strain: dpf95_38.3 and
dpf95_4.2). {ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897,
ECO:0000269|PubMed:12049662}.
VARIANT 245 245 E -> D (in strain: dpf95_38.3 and
dpf95_4.2). {ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897,
ECO:0000269|PubMed:12049662}.
VARIANT 338 338 A -> S (in strain: dpf95_36.4).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720}.
VARIANT 341 341 V -> M (in strain: B4039, dpf95_77.4 and
dpf95_90.2).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897}.
VARIANT 346 346 R -> K (in strain: dpf95_90.2, hfl97_1.0,
hfl97_13.0, hfl97_15.0, hfl97_50.0,
md90_709.1, zim_36H and zim_39H).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720}.
VARIANT 351 351 E -> K. {ECO:0000269|PubMed:11290720}.
VARIANT 465 465 T -> S (in strain: dpf95_29.3).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897}.
VARIANT 484 484 V -> L (in strain: dpf95_38.3, dpf95_4.2,
dpf95_44.3, dpf95_48.2, dpf95_53.1,
dpf95_56.1, dpf95_85.1, hfl97_1.0,
hfl97_13.0, hfl97_15.0, hfl97_50.0,
hfl97_93.0, md90_709.1, zim_11S, zim_23H,
zim_35S, zim_36H, zim_38H, zim_39H,
zim_44H, zim_48S and zim_49S).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897}.
VARIANT 530 530 A -> T (in strain: dpf95_44.3, dpf95_53.1
and dpf95_85.1).
{ECO:0000269|PubMed:11102370,
ECO:0000269|PubMed:11290720,
ECO:0000269|PubMed:11560897}.
VARIANT 540 540 I -> F (in strain: zim_48S).
{ECO:0000269|PubMed:11102370}.
SEQUENCE 560 AA; 60766 MW; 10320D78D41C1BEC CRC64;
MSLTVEIVAT KPYEGQKPGT SGLRKKVKVF TQPNYTENFV QAILEANGAA LAGSTLVVGG
DGRFYCKEAA ELIVRLSAAN GVSKLLVGQN GILSTPAVSS LIRHNKALGG IVLTASHNPG
GPENDFGIKF NCENGGPAPD AFTNHIYKIT TEIKEYKLVR NLQIDISKVG VTSFDIAGKP
FTVEVIDSVA NYVRHMEEIF DFAKLKDFVS GKATGKPLKM RIDAMNGVTG SYVREIFLNR
LGATESSVVH TTPLPDFGGL HPDPNLTYAK DLVDTVAQGD YDIGAAFDGD GDRNMIIGSK
AFFVTPSDSL AVIAHYLEAI PYFQKNGVQG FARSMPTASA VDLVGRKLGK EVFEVPTGWK
YFGNLMDAGR LCLCGEESFG TGSNHIREKD GIWAVLAWIS VMQHTGKGIE DILKQHWSVY
GRNYFTRYDY EECASDPCNE MVATMEKTIT APEFVGKSYS SGGKTYKVKE ADNFSYTDPV
DKSVATKQGL RIVFEDGSRI VVRLSGTGSS GATVRLYIDS YEKENVLGQA SVMLKPLIDI
ALEISQLPKF TGRNAPTVIT


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