PPAC_THEMA
ID PPAC_THEMA Reviewed; 548 AA.
AC Q9WZ56;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=TM_0587;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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 -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD35672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000512; AAD35672.1; ALT_INIT; Genomic_DNA.
DR PIR; D72359; D72359.
DR RefSeq; NP_228397.1; NC_000853.1.
DR AlphaFoldDB; Q9WZ56; -.
DR SMR; Q9WZ56; -.
DR STRING; 243274.THEMA_01730; -.
DR EnsemblBacteria; AAD35672; AAD35672; TM_0587.
DR KEGG; tma:TM0587; -.
DR PATRIC; fig|243274.5.peg.596; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1227; Bacteria.
DR InParanoid; Q9WZ56; -.
DR OMA; TIIANMF; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.310.20; -; 1.
DR Gene3D; 3.40.1390.20; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR InterPro; IPR010766; DRTGG.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
DR Pfam; PF07085; DRTGG; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01131; DHHA2; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
DR SUPFAM; SSF75138; SSF75138; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..548
FT /note="Probable manganese-dependent inorganic
FT pyrophosphatase"
FT /id="PRO_0000158597"
FT DOMAIN 77..132
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 254..311
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..74
FT /note="PPase part 1"
FT REGION 306..548
FT /note="PPase part 2"
FT BINDING 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 548 AA; 61364 MW; D1CF282F70EA56DE CRC64;
MKALERVYVI GHKNPDTDSV CSAIGYAHFK NNVEKGKTFI PARSGDLTNE SLFVLKYFGM
NPPLHIETLE PTVEDLELKN PIFVTPDTSA YDVAMLMESR GIKNVPVVSK EKMIGVVTES
NIARVYVRRL KIEPLVIHPV PFDQLVRILK AEVVCDYMKE KTVSGKVHIA VDALHVLLGK
IEIGDVVIVG DNEPAQIALL EKGAKLMIVV NNAPVSNRVL EIAKEKNAAV LRVKFDAFSA
AKLINLSLPV TLVMSKKFPT VTKKDTLEEV KEIVFTSKIR AAFVEDEKGR LCGVITRTDL
LKDVRKKVIL VDHNEITQAP EGVEKAEILE IIDHHRLGGL STLNPVFFYN EPVGSTSTIV
AEFFLKNGVK MEREIAGILL SGIVSDTLFF KLSTTTEKDR KMANFLADVA KLDLEKFAKK
LLKEGMKIPE DVDPAELLKR DVKVYEMGEE SFAVSQIMTS DFSTLLKEKE RFMNTLKTLK
GEFGVKHFFV LFTNPVEEAS LLMMDGDQKL VEKAFNAEKK DGLFLLKGVM SRKKDFVPKI
GEVLRRER
