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PPAC_METJA
ID   PPAC_METJA              Reviewed;         307 AA.
AC   Q58025;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Manganese-dependent inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
GN   Name=ppaC; OrderedLocusNames=MJ0608;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-5, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RX   PubMed=10898947; DOI=10.1006/abbi.2000.1860;
RA   Kuhn N.J., Wadeson A., Ward S., Young T.W.;
RT   "Methanococcus jannaschii ORF mj0608 codes for a class C inorganic
RT   pyrophosphatase protected by Co(2+) or Mn(2+) ions against fluoride
RT   inhibition.";
RL   Arch. Biochem. Biophys. 379:292-298(2000).
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         Evidence={ECO:0000269|PubMed:10898947};
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.
CC   -!- MASS SPECTROMETRY: Mass=34169; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10898947};
CC   -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98601.1; -; Genomic_DNA.
DR   PIR; H64375; H64375.
DR   RefSeq; WP_010870112.1; NC_000909.1.
DR   PDB; 2EB0; X-ray; 2.20 A; A/B=1-307.
DR   PDBsum; 2EB0; -.
DR   AlphaFoldDB; Q58025; -.
DR   SMR; Q58025; -.
DR   STRING; 243232.MJ_0608; -.
DR   EnsemblBacteria; AAB98601; AAB98601; MJ_0608.
DR   GeneID; 1451473; -.
DR   KEGG; mja:MJ_0608; -.
DR   eggNOG; arCOG01567; Archaea.
DR   HOGENOM; CLU_025243_0_1_2; -.
DR   InParanoid; Q58025; -.
DR   OMA; IMLCAIL; -.
DR   OrthoDB; 57518at2157; -.
DR   PhylomeDB; Q58025; -.
DR   EvolutionaryTrace; Q58025; -.
DR   Proteomes; UP000000805; Chromosome.
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   3D-structure; Cobalt; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..307
FT                   /note="Manganese-dependent inorganic pyrophosphatase"
FT                   /id="PRO_0000158599"
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         66
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           12..25
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          80..89
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           109..118
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           122..125
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           134..148
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   TURN            149..152
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           158..171
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           176..188
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           189..192
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           195..199
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          202..208
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          211..221
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           224..243
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          247..255
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   TURN            256..259
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          260..267
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           269..275
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   STRAND          282..287
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           293..296
FT                   /evidence="ECO:0007829|PDB:2EB0"
FT   HELIX           298..305
FT                   /evidence="ECO:0007829|PDB:2EB0"
SQ   SEQUENCE   307 AA;  34113 MW;  EF7EDD1610668D9A CRC64;
     MRYVVGHKNP DTDSIASAIV LAYFLDCYPA RLGDINPETE FVLRKFGVME PELIESAKGK
     EIILVDHSEK SQSFDDLEEG KLIAIIDHHK VGLTTTEPIL YYAKPVGSTA TVIAELYFKD
     AIDLIGGKKK ELKPDLAGLL LSAIISDTVL FKSPTTTDLD KEMAKKLAEI AGISNIEEFG
     MEILKAKSVV GKLKPEEIIN MDFKNFDFNG KKVGIGQVEV IDVSEVESKK EDIYKLLEEK
     LKNEGYDLIV FLITDIMKEG SEALVVGNKE MFEKAFNVKV EGNSVFLEGV MSRKKQVVPP
     LERAYNG
 
 
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