CYSQ_MYCLE
ID CYSQ_MYCLE Reviewed; 271 AA.
AC P46726; Q9CC39;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=3'-phosphoadenosine 5'-phosphate phosphatase;
DE Short=PAP phosphatase;
DE EC=3.1.3.7;
DE AltName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
DE AltName: Full=DPNPase;
DE AltName: Full=Fructose-1,6-bisphosphatase;
DE Short=FBPase;
DE EC=3.1.3.11;
DE AltName: Full=Inositol-1-monophosphatase;
DE Short=I-1-Pase;
DE Short=IMPase;
DE EC=3.1.3.25;
DE AltName: Full=Inositol-1-phosphatase;
GN Name=cysQ; OrderedLocusNames=ML1301; ORFNames=B2126_C3_229;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Phosphatase with a broad specificity. Its primary
CC physiological function is to dephosphorylate 3'-phosphoadenosine 5'-
CC phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus,
CC plays a role in mycobacterial sulfur metabolism, since it can serve as
CC a key regulator of the sulfate assimilation pathway by controlling the
CC pools of PAP and PAPS in the cell. To a lesser extent, is also able to
CC hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP)
CC (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might not
CC be significant in vivo (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17202.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00017; AAA17202.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583921; CAC31682.1; -; Genomic_DNA.
DR PIR; G87071; G87071.
DR RefSeq; NP_301935.1; NC_002677.1.
DR RefSeq; WP_010908256.1; NC_002677.1.
DR AlphaFoldDB; P46726; -.
DR SMR; P46726; -.
DR STRING; 272631.ML1301; -.
DR EnsemblBacteria; CAC31682; CAC31682; CAC31682.
DR KEGG; mle:ML1301; -.
DR PATRIC; fig|272631.5.peg.2403; -.
DR Leproma; ML1301; -.
DR eggNOG; COG1218; Bacteria.
DR HOGENOM; CLU_071517_0_0_11; -.
DR OMA; IYNRPDP; -.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR Pfam; PF00459; Inositol_P; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..271
FT /note="3'-phosphoadenosine 5'-phosphate phosphatase"
FT /id="PRO_0000142550"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 93..96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 271 AA; 29119 MW; F653420CD7858622 CRC64;
MASHDKRDYQ AELTDAALAA DLATAAGELL LEIREEIGFD QPRALGDAGD RLANSLLLSR
LRAERPGDAV LSEEAHDDRV RLQAGRVWII DPLDGTREFS TAGRTDWAVH IALWQRTTGG
VADGRREITD AAVALPARGN RVYRSDTVTA GAVTGGVPNI LRIAVSATRP PTILHRIRQK
LAIEPVAIGS AGAKAMAVVD GDVDAYLHVG GQWEWDSAAP AGVVLAAGMH ASRLDGSPLR
YNQLDPYLPD FVMCRADIAP ILLGVIREVW Q
