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3'-phosphoadenosine 5'-phosphate phosphatase (PAP phosphatase) (EC 3.1.3.7) (3'(2'),5'-bisphosphate nucleotidase) (3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase) (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (DPNPase) (Fructose-1,6-bisphosphatase) (FBPase) (EC 3.1.3.11) (Inositol-1-monophosphatase) (I-1-Pase) (IMPase) (EC 3.1.3.25) (Inositol-1-phosphatase)

 CYSQ_MYCTU              Reviewed;         267 AA.
P9WKJ1; L0TBL8; O06244; P65163;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 32.
RecName: Full=3'-phosphoadenosine 5'-phosphate phosphatase;
Short=PAP phosphatase;
EC=3.1.3.7 {ECO:0000269|PubMed:18454554};
AltName: Full=3'(2'),5'-bisphosphate nucleotidase;
AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
AltName: Full=DPNPase;
AltName: Full=Fructose-1,6-bisphosphatase;
Short=FBPase;
EC=3.1.3.11 {ECO:0000269|PubMed:16325768, ECO:0000269|PubMed:18454554};
AltName: Full=Inositol-1-monophosphatase;
Short=I-1-Pase;
Short=IMPase;
EC=3.1.3.25 {ECO:0000269|PubMed:16325768, ECO:0000269|PubMed:18454554};
AltName: Full=Inositol-1-phosphatase;
Name=cysQ; OrderedLocusNames=Rv2131c; ORFNames=MTCY270.37;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION AS IMPASE AND FBPASE, CATALYTIC ACTIVITY, SUBSTRATE
SPECIFICITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR
METHIONINE, AND MUTAGENESIS OF ASP-40; LEU-71 AND ASP-94.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16325768; DOI=10.1016/j.bbrc.2005.11.088;
Gu X., Chen M., Shen H., Jiang X., Huang Y., Wang H.;
"Rv2131c gene product: an unconventional enzyme that is both inositol
monophosphatase and fructose-1,6-bisphosphatase.";
Biochem. Biophys. Res. Commun. 339:897-904(2006).
[3]
FUNCTION AS PAP PHOSPHATASE, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, MASS SPECTROMETRY,
AND CLEAVAGE OF INITIATOR METHIONINE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=18454554; DOI=10.1021/bi702453s;
Hatzios S.K., Iavarone A.T., Bertozzi C.R.;
"Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-
phosphoadenosine-5'-phosphatase.";
Biochemistry 47:5823-5831(2008).
[4]
DISRUPTION PHENOTYPE, AND INDUCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20167072; DOI=10.1186/1471-2180-10-50;
Movahedzadeh F., Wheeler P.R., Dinadayala P., Av-Gay Y., Parish T.,
Daffe M., Stoker N.G.;
"Inositol monophosphate phosphatase genes of Mycobacterium
tuberculosis.";
BMC Microbiol. 10:50-50(2010).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: Phosphatase with a broad specificity. Its primary
physiological function is to dephosphorylate 3'-phosphoadenosine
5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate
(PAPS). Thus, plays a role in mycobacterial sulfur metabolism,
since it can serve as a key regulator of the sulfate assimilation
pathway by controlling the pools of PAP and PAPS in the cell. To a
lesser extent, is also able to hydrolyze inositol 1-phosphate (I-
1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-
6-P)) and AMP in vitro, but this might has no significance in
vivo. Glucose-1-phosphate (G-1-P), p-nitrophenyl phosphate (pNPP),
and beta-glycerol phosphate (beta-GP) are also good substrates,
compared to I-1-P. With much lower efficiency, can also hydrolyze
inositol 2-phosphate (I-2-P) and glucose-6-phosphate (G-6-P) in
vitro, but not fructose-6-phosphate (F-6-P) and trehalose-6-
phosphate (T-6-P). {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554}.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O =
adenosine 5'-phosphate + phosphate. {ECO:0000269|PubMed:18454554}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
fructose 6-phosphate + phosphate. {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554}.
-!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
+ phosphate. {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
Note=Mg(2+). Mn(2+) can substitute for Mg(2+) for PAP phosphatase
and IMPase activities, but is less efficient (50%-60% of the
activity observed with Mg(2+)). {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
-!- ACTIVITY REGULATION: PAP phosphatase and IMPase activities are
inhibited by Li(+). To a lesser extent, PAP hydrolysis is also
inhibited by Na(+) and K(+), with IC50 values of 150 and 250 mM,
respectively, so much higher than IC50 with Li(+) (0.5 mM).
Exhibits about 50% residual IMPase activity at 5 mM Li(+) and
about 10% at 30 mM Li(+). Na(+) and K(+) have no significant
effect on IMPase activity between 0 and 200 mM.
{ECO:0000269|PubMed:16325768, ECO:0000269|PubMed:18454554}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8.1 uM for 3'-phosphoadenosine 5'-phosphate (at pH 9.0 and 30
degrees Celsius) {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
KM=0.22 mM for inositol-1-phosphate (at pH 9.3 and 37 degrees
Celsius) {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
KM=0.45 mM for fructose 1,6-bisphosphate (at pH 9.3 and 37
degrees Celsius) {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
Vmax=6.9 umol/min/mg enzyme for IMPase activity (at pH 9.3 and
37 degrees Celsius) {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
Note=The second-order rate constant for PAP was determined to be
over 3 orders of magnitude greater than those determined for IMP
and FBP.;
pH dependence:
Optimum pH is 8.5-9.5 for PAP phosphatase activity, 9.3 for
IMPase activity, and about 10 for FBPase activity. IMPase
activity shows a dramatic decrease at low pH. In contrast,
IMPase activity is highly stable at alkaline pH, with more than
60% activity remaining at pH 12. {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
Temperature dependence:
Optimum temperature is 62 degrees Celsius for IMPase activity.
After preincubation at 70 degrees Celsius for 2 minutes and then
being assayed at 37 degrees Celsius, more than 95% activities of
IMPase and FBPase are lost. {ECO:0000269|PubMed:16325768,
ECO:0000269|PubMed:18454554};
-!- PATHWAY: Sulfur metabolism; sulfate assimilation.
{ECO:0000269|PubMed:18454554}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16325768}.
-!- INDUCTION: When comparing gene expression levels of the four
IMPase family genes in exponential cultures of M.tuberculosis, the
level of cysQ is the highest, almost equal to sigA; impA and impC
are expressed at approximately 40% of this level, while suhB is
lowest, at 12% of the cysQ level. {ECO:0000269|PubMed:20167072}.
-!- MASS SPECTROMETRY: Mass=30584; Method=Electrospray; Range=2-267;
Evidence={ECO:0000269|PubMed:16325768};
-!- MASS SPECTROMETRY: Mass=30578; Mass_error=1; Method=Electrospray;
Range=2-267; Evidence={ECO:0000269|PubMed:18454554};
-!- DISRUPTION PHENOTYPE: Strains lacking this gene show normal
growth, do not require exogenous inositol for growth, and show no
differences in levels of phosphatidylinosotol mannosides (PIMs),
lipomannan (LM), lipoarabinomannan (LAM) or mycothiol (in the
absence of exogenous inositol). {ECO:0000269|PubMed:20167072}.
-!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AL123456; CCP44906.1; -; Genomic_DNA.
PIR; G70576; G70576.
RefSeq; NP_216647.1; NC_000962.3.
RefSeq; WP_003411096.1; NZ_KK339370.1.
PDB; 5DJF; X-ray; 1.70 A; A=2-267.
PDB; 5DJG; X-ray; 1.95 A; A=2-267.
PDB; 5DJH; X-ray; 1.45 A; A=2-267.
PDB; 5DJI; X-ray; 1.66 A; A=2-267.
PDB; 5DJJ; X-ray; 1.50 A; A=2-267.
PDB; 5DJK; X-ray; 1.80 A; A=2-267.
PDBsum; 5DJF; -.
PDBsum; 5DJG; -.
PDBsum; 5DJH; -.
PDBsum; 5DJI; -.
PDBsum; 5DJJ; -.
PDBsum; 5DJK; -.
ProteinModelPortal; P9WKJ1; -.
SMR; P9WKJ1; -.
STRING; 83332.Rv2131c; -.
PaxDb; P9WKJ1; -.
EnsemblBacteria; CCP44906; CCP44906; Rv2131c.
GeneID; 888142; -.
KEGG; mtu:Rv2131c; -.
KEGG; mtv:RVBD_2131c; -.
PATRIC; fig|83332.111.peg.2375; -.
TubercuList; Rv2131c; -.
eggNOG; ENOG4108RM3; Bacteria.
eggNOG; COG1218; LUCA.
KO; K01082; -.
OMA; VFHTSEV; -.
PhylomeDB; P9WKJ1; -.
Reactome; R-MTU-936635; Sulfate assimilation.
UniPathway; UPA00097; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:MTBBASE.
GO; GO:0050897; F:cobalt ion binding; IDA:MTBBASE.
GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:MTBBASE.
GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:MTBBASE.
GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:MTBBASE.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
GO; GO:0000103; P:sulfate assimilation; TAS:Reactome.
InterPro; IPR020583; Inositol_monoP_metal-BS.
InterPro; IPR000760; Inositol_monophosphatase-like.
Pfam; PF00459; Inositol_P; 1.
PROSITE; PS00629; IMP_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000305|PubMed:16325768,
ECO:0000305|PubMed:18454554}.
CHAIN 2 267 3'-phosphoadenosine 5'-phosphate
phosphatase.
/FTId=PRO_0000142551.
REGION 93 96 Substrate binding. {ECO:0000250}.
METAL 73 73 Magnesium 1. {ECO:0000250}.
METAL 91 91 Magnesium 1. {ECO:0000250}.
METAL 91 91 Magnesium 2. {ECO:0000250}.
METAL 93 93 Magnesium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 94 94 Magnesium 2. {ECO:0000250}.
METAL 212 212 Magnesium 2. {ECO:0000250}.
BINDING 73 73 Substrate. {ECO:0000250}.
BINDING 212 212 Substrate. {ECO:0000250}.
MUTAGEN 40 40 D->N: Less than 2% of wild-type IMPase
and FBPase activities.
{ECO:0000269|PubMed:16325768}.
MUTAGEN 71 71 L->A: No effect on IMPase and FBPase
activities. Much less sensitive to
inhibition by Li(+).
{ECO:0000269|PubMed:16325768}.
MUTAGEN 94 94 D->N: Less than 3% of wild-type IMPase
and FBPase activities.
{ECO:0000269|PubMed:16325768}.
HELIX 15 37 {ECO:0000244|PDB:5DJH}.
STRAND 39 41 {ECO:0000244|PDB:5DJH}.
HELIX 42 64 {ECO:0000244|PDB:5DJH}.
STRAND 68 72 {ECO:0000244|PDB:5DJH}.
HELIX 80 83 {ECO:0000244|PDB:5DJH}.
STRAND 85 94 {ECO:0000244|PDB:5DJH}.
HELIX 96 99 {ECO:0000244|PDB:5DJH}.
STRAND 108 115 {ECO:0000244|PDB:5DJH}.
STRAND 118 120 {ECO:0000244|PDB:5DJF}.
STRAND 123 131 {ECO:0000244|PDB:5DJH}.
TURN 132 136 {ECO:0000244|PDB:5DJH}.
STRAND 137 140 {ECO:0000244|PDB:5DJH}.
TURN 141 143 {ECO:0000244|PDB:5DJH}.
STRAND 155 165 {ECO:0000244|PDB:5DJH}.
HELIX 169 173 {ECO:0000244|PDB:5DJH}.
TURN 174 176 {ECO:0000244|PDB:5DJH}.
STRAND 179 185 {ECO:0000244|PDB:5DJH}.
HELIX 187 195 {ECO:0000244|PDB:5DJH}.
STRAND 200 204 {ECO:0000244|PDB:5DJH}.
HELIX 210 222 {ECO:0000244|PDB:5DJH}.
STRAND 226 228 {ECO:0000244|PDB:5DJH}.
STRAND 243 245 {ECO:0000244|PDB:5DJF}.
STRAND 247 250 {ECO:0000244|PDB:5DJH}.
HELIX 252 254 {ECO:0000244|PDB:5DJH}.
HELIX 255 264 {ECO:0000244|PDB:5DJH}.
SEQUENCE 267 AA; 28447 MW; AFF7347E34129AF6 CRC64;
MVSPAAPDLT DDLTDAELAA DLAADAGKLL LQVRAEIGFD QPWTLGEAGD RQANSLLLRR
LQAERPGDAV LSEEAHDDLA RLKSDRVWII DPLDGTREFS TPGRDDWAVH IALWRRSSNG
QPEITDAAVA LPARGNVVYR TDTVTSGAAP AGVPGTLRIA VSATRPPAVL HRIRQTLAIQ
PVSIGSAGAK AMAVIDGYVD AYLHAGGQWE WDSAAPAGVM LAAGMHASRL DGSPLRYNQL
DPYLPDLLMC RAEVAPILLG AIADAWR


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