ID E6W1M4_DESIS Unreviewed; 552 AA.
AC E6W1M4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=Selin_1846 {ECO:0000313|EMBL:ADU66573.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU66573.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU66573.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) 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};
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DR EMBL; CP002432; ADU66573.1; -; Genomic_DNA.
DR RefSeq; WP_013506453.1; NC_014836.1.
DR AlphaFoldDB; E6W1M4; -.
DR STRING; 653733.Selin_1846; -.
DR KEGG; din:Selin_1846; -.
DR eggNOG; COG1227; Bacteria.
DR eggNOG; COG3448; Bacteria.
DR HOGENOM; CLU_025243_1_0_0; -.
DR InParanoid; E6W1M4; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000002572; Chromosome.
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; 3.10.310.20; 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); 2.
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; 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; 1.
DR Pfam; PF02833; DHHA2; 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; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADU66573.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572}.
FT DOMAIN 253..309
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 552 AA; 62079 MW; EEF2E577634CA0B4 CRC64;
MQDTIVIGHK NPDTDSICSA IAYAQLKSQL APDTSFVAGR CGQLNKQTRY ILERFGVAAP
RFLRDVHPRV RDALQEEAVW AHCNTPIFQV MRNIDEKRIR ITPIVDDHGI FNGVVSILEV
AEFFLEKDTV HHPNFLIRPE NFPAVLPGTF HREGELEEFP ARIFAAAMPS ERAVERFERM
QSDDILLITG KRRDILEYAI RKQFPAIILT GIEGPDDLDI DFSNYRGWVY ISQWDTAETL
RRCTLAVPCK SIMNRDVPVA TPEMLFEEAR DIVASSEHKG LPVLDEQRRL LGMVTRTNFL
HRPQPRLVLM DHNELAQAVD GAENARIVEI VDHHRLGSLK TTHPIHVLAK PVGSTCTLVY
QQYRFHGITP DPVTAGLLLC GILSDTVITK SPTTTVEDTD ALERLATLAG VDSQKLGLEI
FSASDSLANA EPRAVVNGDL KIYSEFGVSV GIAQVEVVTL SEPAEIYQQL QAALDDLRSS
RKLDWTMLLI TDIIKEESIL LTSAYPCGEQ RLSYGRRDDH VYHLPGVLSR KKQLLPEILR
ILEECGNETL RK
//