CYSQ_MYCBO
ID CYSQ_MYCBO Reviewed; 267 AA.
AC P65164; A0A1R3Y0D2; O06244; X2BK83;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=BQ2027_MB2155C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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}.
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DR EMBL; LT708304; SIU00762.1; -; Genomic_DNA.
DR RefSeq; NP_855804.1; NC_002945.3.
DR RefSeq; WP_003411096.1; NC_002945.4.
DR AlphaFoldDB; P65164; -.
DR SMR; P65164; -.
DR EnsemblBacteria; SIU00762; SIU00762; BQ2027_MB2155C.
DR GeneID; 45426106; -.
DR PATRIC; fig|233413.5.peg.2369; -.
DR OMA; IYNRPDP; -.
DR UniPathway; UPA00097; -.
DR Proteomes; UP000001419; 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.
FT CHAIN 1..267
FT /note="3'-phosphoadenosine 5'-phosphate phosphatase"
FT /id="PRO_0000142552"
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 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ 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
