ID B9Y4M2_9FIRM Unreviewed; 537 AA.
AC B9Y4M2;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=inorganic diphosphatase {ECO:0000256|ARBA:ARBA00012146};
DE EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|ARBA:ARBA00032535};
GN ORFNames=HOLDEFILI_00753 {ECO:0000313|EMBL:EEF69092.1};
OS Holdemania filiformis DSM 12042.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemania.
OX NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF69092.1, ECO:0000313|Proteomes:UP000005950};
RN [1] {ECO:0000313|EMBL:EEF69092.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69092.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF69092.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69092.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000926};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EEF69092.1}.
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DR EMBL; ACCF01000047; EEF69092.1; -; Genomic_DNA.
DR RefSeq; WP_006057963.1; NZ_GG657553.1.
DR AlphaFoldDB; B9Y4M2; -.
DR STRING; 545696.HOLDEFILI_00753; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_1_0_9; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000005950; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 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 PANTHER; PTHR12112; BNIP - RELATED; 1.
DR PANTHER; PTHR12112:SF22; MANGANESE-DEPENDENT INORGANIC PYROPHOSPHATASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01368; DHH; 2.
DR Pfam; PF02833; DHHA2; 1.
DR Pfam; PF07085; DRTGG; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01131; DHHA2; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR PROSITE; PS51371; CBS; 2.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 72..130
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 247..303
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 537 AA; 59955 MW; 73618E5808D7A68F CRC64;
MDKPVYVIGH KNPDADSICS AIAYSALKNK LGINTVAARL SAVNKETLYI LDRFRLPVPM
LLTSAKCTLA EIDMDEAMLL SKDTTMKEAL DAILSRKNKG IFVVDKKHHL EGIVSVSDLT
NLWTADEEAL EDLMSRVPLA NILKTTRASL LYEAPFHPNG KVHLMPSLGQ NSNIEAGTIV
IVGNNPEVQR SAIRQKASLI LICGENWVDS ITLEMAKQEQ VSILHTPLSA ITVAHSIFQS
PSVAEIMTRE VVVFRTSETV DGASQRIAKT RFRTYPVVNE KEEVIGAISR YHLFNYRKKQ
LILVDHNEKE QSIHDLEFAE IIEIVDHHRL GGIETQSPIS FVNQIVGSTC TIVANLYEQH
QIEIPAQIAG VLLAGLLSDT MNLKSPTTTE IDRITAEKLA QISGVDRQTL SEELVGTSDS
LMNKSFQELM YEDFKEFRIQ DSKVAIGQVV CRCPDEYQQI KPDFLAYLEE QNLQHHYDLL
LILFTDPKGS GSHFLYTGKK GWVIEEGFKT VLTNGFAPGF ISRKKQVLPV VIDTLNK
//
