IPYR_KLULA
ID IPYR_KLULA Reviewed; 287 AA.
AC P13998; Q6CMU3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=IPP1; Synonyms=IPP; OrderedLocusNames=KLLA0E17721g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2538971; DOI=10.1002/yea.320050106;
RA Stark M.J.R., Milner J.S.;
RT "Cloning and analysis of the Kluyveromyces lactis TRP1 gene: a chromosomal
RT locus flanked by genes encoding inorganic pyrophosphatase and histone H3.";
RL Yeast 5:35-50(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP SIMILARITY TO E.COLI AND YEAST PPASES.
RX PubMed=2160278; DOI=10.1016/0167-4838(90)90246-c;
RA Lahti R., Kolakowski L.F. Jr., Heinonen J., Vihinen M., Pohjanoksa K.,
RA Cooperman B.S.;
RT "Conservation of functional residues between yeast and E. coli inorganic
RT pyrophosphatases.";
RL Biochim. Biophys. Acta 1038:338-345(1990).
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=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG99833.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X14230; CAA32446.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99833.1; ALT_INIT; Genomic_DNA.
DR PIR; S07894; PWVKL.
DR RefSeq; XP_454746.1; XM_454746.1.
DR AlphaFoldDB; P13998; -.
DR SMR; P13998; -.
DR STRING; 28985.XP_454746.1; -.
DR PRIDE; P13998; -.
DR EnsemblFungi; CAG99833; CAG99833; KLLA0_E17667g.
DR GeneID; 2894279; -.
DR KEGG; kla:KLLA0_E17667g; -.
DR eggNOG; KOG1626; Eukaryota.
DR HOGENOM; CLU_040684_0_1_1; -.
DR InParanoid; P13998; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; SSF50324; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..287
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137583"
FT BINDING 79
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 287 AA; 32165 MW; FE36751C88C87934 CRC64;
MSYTTRQVGA KNSLDYKVYI EKDGKPISAF HDIPLYADEA NGIFNMVVEI PRWTNAKLEI
TKEEPLNPII QDTKKGKLRF VRNCFPHHGY IHNYGAFPQT WEDPNESHPE TKAVGDNDPL
DVLEIGEQVA YTGQVKQVKV LGVMALLDEG ETDWKVIAID INDPLAPKLN DIEDVEKHLP
GLLRATNEWF RIYKIPDGKP ENQFAFSGEA KNKKYTLDVI RECNEAWKKL ISGKSADAKK
IDLTNTTLSD TATYSAEAAS AVPAANVLPD EPIDKSIDKW FFISGSA
