位置:首页 > 蛋白库 > CYSQ_MYCTO
CYSQ_MYCTO
ID   CYSQ_MYCTO              Reviewed;         267 AA.
AC   P9WKJ0; L0TBL8; O06244; P65163;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
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=MT2189;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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=AAK46473.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AE000516; AAK46473.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70576; G70576.
DR   RefSeq; WP_003411096.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKJ0; -.
DR   SMR; P9WKJ0; -.
DR   PRIDE; P9WKJ0; -.
DR   EnsemblBacteria; AAK46473; AAK46473; MT2189.
DR   GeneID; 45426106; -.
DR   KEGG; mtc:MT2189; -.
DR   PATRIC; fig|83331.31.peg.2361; -.
DR   HOGENOM; CLU_071517_0_0_11; -.
DR   UniPathway; UPA00097; -.
DR   Proteomes; UP000001020; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..267
FT                   /note="3'-phosphoadenosine 5'-phosphate phosphatase"
FT                   /id="PRO_0000427645"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024