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PPAC_DEIRA
ID   PPAC_DEIRA              Reviewed;         314 AA.
AC   Q9RRB7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable manganese-dependent inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=ppaC; OrderedLocusNames=DR_2576;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-22.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA   Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT   "Protein recycling is a major component of post-irradiation recovery in
RT   Deinococcus radiodurans strain R1.";
RL   Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; EC=3.6.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is:
CC       4.65, its MW is: 32 kDa.
CC   -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR   EMBL; AE000513; AAF12113.1; -; Genomic_DNA.
DR   PIR; A75258; A75258.
DR   RefSeq; NP_296296.1; NC_001263.1.
DR   RefSeq; WP_010889201.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RRB7; -.
DR   SMR; Q9RRB7; -.
DR   STRING; 243230.DR_2576; -.
DR   EnsemblBacteria; AAF12113; AAF12113; DR_2576.
DR   KEGG; dra:DR_2576; -.
DR   PATRIC; fig|243230.17.peg.2822; -.
DR   eggNOG; COG1227; Bacteria.
DR   HOGENOM; CLU_025243_0_1_0; -.
DR   InParanoid; Q9RRB7; -.
DR   OMA; IMLCAIL; -.
DR   OrthoDB; 732679at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.20; -; 1.
DR   HAMAP; MF_00207; PPase_C; 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
DR   InterPro; IPR022934; Mn-dep_inorganic_PyrPase.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; SSF64182; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..314
FT                   /note="Probable manganese-dependent inorganic
FT                   pyrophosphatase"
FT                   /id="PRO_0000158571"
FT   BINDING         7
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        15
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  34039 MW;  DC5DEAB2C26C5516 CRC64;
     MLAVFGHLNP DTDAISAAMV YARLLTRQGT EAQAYRLGEP NFETAYVLRE LGLEAPPLLT
     ELPAGSKVAL VDHNESAQSL PALGELDVTR VVDHHKLGDL TTINPPYLRF EPVGCTGTIL
     LKLHREAGLS VEPQDAKLML SAILSDTLHF RSPTTTQDDR DAVAFLAPVA GVNDVEAYAL
     AMFAAKSDLG NTPAETLLRM DYKVFPFGDP VQPQNWGIGV IETTNPAYVF GRQQELLAAM
     DQVKAEDTLS GMLLSVVDIL NETNRTLVLG ATEAKVLREA FGAEAEGQVA DLGNRISRKK
     QIVPTLEKYF APEA
 
 
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