ID A0A2P6TU56_CHLSO Unreviewed; 1786 AA.
AC A0A2P6TU56;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Inosine triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE Short=ITPase {ECO:0000256|HAMAP-Rule:MF_03148};
DE Short=Inosine triphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE EC=3.6.1.9 {ECO:0000256|HAMAP-Rule:MF_03148};
DE AltName: Full=Non-canonical purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE AltName: Full=Non-standard purine NTP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE AltName: Full=Nucleoside-triphosphate diphosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE AltName: Full=Nucleoside-triphosphate pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_03148};
DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_03148};
GN ORFNames=C2E21_3297 {ECO:0000313|EMBL:PRW57605.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW57605.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW57605.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC nucleotides such as inosine triphosphate (ITP), deoxyinosine
CC triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their
CC respective monophosphate derivatives. The enzyme does not distinguish
CC between the deoxy- and ribose forms. Probably excludes non-canonical
CC purines from RNA and DNA precursor pools, thus preventing their
CC incorporation into RNA and DNA and avoiding chromosomal lesions.
CC {ECO:0000256|HAMAP-Rule:MF_03148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + ITP = diphosphate + H(+) + IMP; Xref=Rhea:RHEA:29399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + XTP = diphosphate + H(+) + XMP; Xref=Rhea:RHEA:28610,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57464, ChEBI:CHEBI:61314; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dITP + H2O = dIMP + diphosphate + H(+); Xref=Rhea:RHEA:28342,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61194, ChEBI:CHEBI:61382; EC=3.6.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03148};
CC Note=Binds 1 divalent metal cation per subunit; can use either Mg(2+)
CC or Mn(2+). {ECO:0000256|HAMAP-Rule:MF_03148};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03148}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148}.
CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000256|HAMAP-
CC Rule:MF_03148}.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRW57605.1}.
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DR EMBL; LHPG02000006; PRW57605.1; -; Genomic_DNA.
DR STRING; 3076.A0A2P6TU56; -.
DR OrthoDB; 1203747at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035870; F:dITP diphosphatase activity; IEA:RHEA.
DR GO; GO:0036220; F:ITP diphosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0036222; F:XTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0009204; P:deoxyribonucleoside triphosphate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00515; HAM1; 1.
DR CDD; cd00143; PP2Cc; 2.
DR Gene3D; 3.90.950.10; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 4.
DR HAMAP; MF_03148; HAM1_NTPase; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR027502; ITPase.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013857; NADH-UbQ_OxRdtase-assoc_prot30.
DR InterPro; IPR008030; NmrA-like.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR002637; RdgB/HAM1.
DR PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF08547; CIA30; 1.
DR Pfam; PF01725; Ham1p_like; 1.
DR Pfam; PF13460; NAD_binding_10; 1.
DR Pfam; PF05368; NmrA; 1.
DR Pfam; PF00481; PP2C; 4.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52972; ITPase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF81606; PP2C-like; 2.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03148};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03148};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03148};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_03148};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03148}; Nucleotide metabolism {ECO:0000256|HAMAP-Rule:MF_03148};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03148};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899}.
FT DOMAIN 23..473
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 517..944
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1004..1009
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 1036
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 1048
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 1064..1065
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 1064
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 1140..1143
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 1163
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
FT BINDING 1168..1169
FT /ligand="ITP"
FT /ligand_id="ChEBI:CHEBI:61402"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03148"
SQ SEQUENCE 1786 AA; 190280 MW; 2AC747131CB1D82D CRC64;
MGAYLSSPIR DKETGEGEND AFKFGVSAMQ GWRTDMEDAH AAILDLPDGS TKAALFAVLD
GHGGAEVARF VANHLAQELL STEGYQANDM EVALRQAYLR MDELLVKEEH REELKSLRAK
ESEEEGDSGP MVINGASLPE SLLEALGMPS GGGFQIKLVR SGPGARGISI DDIEEEGEDS
DRSGTTFLEL VQGDPEEEGE GEEAGKGEED EGEAEEAAAA AGPSGGERAS ASKRKREEKQ
AGMEVDAGAA EGGSKEGGAA EQQLAAGGGG GDAQDDPEAE DVEDVMERTP EKGDDDYMGP
SAGCTAVCAL VRNGELYVAN AGDSRCVLSR GGRAVAMTQD HKPMDADEYA RIMKAGGFVA
DGRVNGSLNL SRALGDLEYK QTKDLGPEEQ MVTAMPEIRK ETLQPGDDFL VLACDGIWDV
LTNQEAVDFV RERLAAGKTP REICEEMCDH CLAPDTGGCG KGCDNMSVIV VQLKDYVPKL
LARAGQAAFP CTEGMGQYLS APATAKESEE GHNDTLGYGL SAMQGWRVSM EDAHIAALDL
DPATKTSLFS VFDGHGGRAV SQFCAAHLAE EFVRSDAYRR GDLAAAITEA YYRLDVRLDS
EEGKAELRQF VADTKPSREP VAGLFTDVES KLAGAAAAHE ERVRNSQQSE ASGEAVPLAG
GAAADTSSSS GEAAGGGSGA SSKEALAEKL ASKMGGTKDF LESHLMRASV LTPLEPDDPA
SPVPAAAPGA QAIGGGKAAG DGAAAGAAAN GAASAAAASC EEDEEDMHHA AGMGATAVSV
VVRGNKVIVA NTGDSRCVLS RRGQARALTL DHKPILFEEA KRIIKAGGFV RDNRINGALN
VSRTIGDLDF KRNSELPHTE QMVVATPDIE QFTLEEGDEF LILACDGIWD VLTNQEAVDF
VRKRLKAGEG LRAICEAMCD ACLAPDLKGL CRGADNMSVV LVLFKKHAKL GGFWSSLLAA
CGMSSSYKRA PSSNEMRRRP PAAMSAAAAP AAARPPPPTI YFATGNKKKL EEVVAILEAG
HPLPFEVQPA AMDLPELQGE PEEIAAQKCR LAAQQLGAAV MVEDTCLCFN ALKGLPGPYI
KHFLQRLGHD GLNRMLAGFE DKTAYAQCTF AYSEGPGHEP IVFVGRTDGR IVPARGPPDF
GWDPIFEAEN FGQTYAEMDN EIKNGISHRY RALDKLRAYL LDGHAAAAAA ADGAAGGQQR
AEQRRRGAAV QPRAEQQDGS GGSGGREADD LPVPDVPKQR RRRRKQEQQA KEFTIDDLNP
ISMGRKSREV FDDVWTQLQR IGNPARSVQA SERITRLVGE AEFESPDAAD TTVLVTGATG
RVGRVLVRKL LLRGYKVKAL VRQREGGAAA AEAAVAAPAA AVDSSASVDG SEGQEGLPQA
AELVYGDVAD YKACRQAVKG VDKVICCSGA RTTLTADLAR VDDVGVANLA KAFMDELNAR
ARRQGQLAPA AKRELADFGN ESYHEAWNVV AVGTPTPPEG EEGMSKAKRR AIKRATARDT
AEAYIDEENH LVFEGAVYSR GGLAEVGAPL QLPYEDHAAL DGAEALVVRL MADEHPYTCV
LRTRGGITYT ARFSTRHGYN TVRLPFNTFR PVVMDDPPLQ PGEVEYIGFR FEPRIKVLEE
VTEPGQSMFD LSANRFKLMV DWIKTLPGGV ETNFVLLSCS GAPRADLAPA TRDKIVTYKR
KGEAALRNSG LGYTIVRPGP LVEEAGGYKA LVFDQGNRIT QGISCADVAD VCLKALHNPE
ARNKTFEVCF EYQPEEGLEL YELISHLPDK SNNYLTPALA PLAKNT
//
