IPYR_HALVD
ID IPYR_HALVD Reviewed; 177 AA.
AC D4GT97; L9UQG2;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000303|PubMed:26546423};
DE Short=PPA {ECO:0000303|PubMed:26546423};
DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423};
DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00209};
DE Short=PPase {ECO:0000255|HAMAP-Rule:MF_00209};
GN Name=ipp {ECO:0000312|EMBL:ADE03387.1};
GN Synonyms=ppa {ECO:0000255|HAMAP-Rule:MF_00209};
GN OrderedLocusNames=HVO_0729 {ECO:0000312|EMBL:ADE03387.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=26546423; DOI=10.1128/aem.03055-15;
RA McMillan L.J., Hepowit N.L., Maupin-Furlow J.A.;
RT "Archaeal inorganic pyrophosphatase displays robust activity under high-
RT salt conditions and in organic solvents.";
RL Appl. Environ. Microbiol. 82:538-548(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC forming two phosphate ions (By similarity) (PubMed:26546423). The
CC hydrolysis of PPi by inorganic pyrophosphatase releases a considerable
CC amount of energy that can drive unfavorable biochemical transformations
CC to completion (Probable). Is not active on nucleoside triphosphates
CC (ATP, TTP, GTP, or CTP) or nucleoside diphosphate (ADP)
CC (PubMed:26546423). {ECO:0000255|HAMAP-Rule:MF_00209,
CC ECO:0000269|PubMed:26546423, ECO:0000305|PubMed:26546423}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00209, ECO:0000269|PubMed:26546423};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00209,
CC ECO:0000269|PubMed:26546423};
CC -!- ACTIVITY REGULATION: Inhibited by sodium fluoride (NaF) in vitro,
CC similarly to other class A type inorganic pyrophosphatases.
CC {ECO:0000269|PubMed:26546423}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.55 mM for diphosphate (at 42 degrees Celsius)
CC {ECO:0000269|PubMed:26546423};
CC KM=0.26 mM for diphosphate (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:26546423};
CC Vmax=465 umol/min/mg enzyme (at 42 degrees Celsius)
CC {ECO:0000269|PubMed:26546423};
CC Vmax=53 umol/min/mg enzyme (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:26546423};
CC Note=Displays non-Michaelis-Menten kinetics for PPi hydrolysis. Hill
CC coefficients indicate cooperative binding to PPi and Mg(2+).
CC {ECO:0000269|PubMed:26546423};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:26546423};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius. Is moderately
CC thermostable, with a half-life of thermal inactivation of 2 hours at
CC 65 degrees Celsius, and retains 82% activity after incubation for 2
CC hours at 42 degrees Celsius. {ECO:0000269|PubMed:26546423};
CC -!- SUBUNIT: Homohexamer (By similarity) (PubMed:26546423). Also forms
CC homotrimers, but the trimeric form is 23% less active than the hexamer.
CC In fact, likely forms a dimer of trimers (PubMed:26546423).
CC {ECO:0000255|HAMAP-Rule:MF_00209, ECO:0000269|PubMed:26546423}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}.
CC -!- BIOTECHNOLOGY: Inorganic pyrophosphatases are used in a wide variety of
CC biotechnology applications based on the ability of these enzymes to
CC drive reactions forward and generate an easily assayed product. Since
CC HvPPA displays robust activity under high-salt conditions and in
CC organic solvents, it could be a valuable tool for use in bioindustry.
CC {ECO:0000269|PubMed:26546423}.
CC -!- MISCELLANEOUS: A unique feature of H.volcanii PPA (HvPPA) is its high
CC tolerance to organic solvents, with little if any enzyme inactivation
CC after 2 hours of incubation in buffers supplemented with 50% (vol/vol)
CC dimethyl sulfoxide (DMSO), dimethylformamide (DMF), ethanol, or
CC methanol. The catalytic activity of HvPPA is also found to be robust
CC when assayed in organic solvents. Moreover, HvPPA is fully active over
CC a wide range of salt concentrations. {ECO:0000269|PubMed:26546423}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00209}.
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DR EMBL; CP001956; ADE03387.1; -; Genomic_DNA.
DR RefSeq; WP_004044208.1; NZ_AOHU01000097.1.
DR AlphaFoldDB; D4GT97; -.
DR SMR; D4GT97; -.
DR STRING; 309800.C498_15088; -.
DR EnsemblBacteria; ADE03387; ADE03387; HVO_0729.
DR GeneID; 8925075; -.
DR KEGG; hvo:HVO_0729; -.
DR PATRIC; fig|309800.29.peg.2912; -.
DR eggNOG; arCOG01711; Archaea.
DR HOGENOM; CLU_073198_1_2_2; -.
DR OMA; DEPTFPG; -.
DR OrthoDB; 103587at2157; -.
DR BRENDA; 3.6.1.1; 2561.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
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 HAMAP; MF_00209; Inorganic_PPase; 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.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..177
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000446107"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
SQ SEQUENCE 177 AA; 20372 MW; 714D01074DADBF0B CRC64;
MVNLWEDMET GPNAPDEIYA VVECLKGERN KYEYDKDIPG VVLDRVLHSN VHYPSDYGFI
PQTYYDDEDP FDVLVLVEDQ TFPGCVIEAR PVALMKMDDD GEQDDKVIAV PVEDPRYDHI
EDLDDIPQQT LDEIDEFFAT YKNLEAGKEV ETLGWEDKQA AKDAIEHAMD LYEENFA
