ID A0A2U1E392_9FIRM Unreviewed; 550 AA.
AC A0A2U1E392;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=C7381_10512 {ECO:0000313|EMBL:PVY94312.1};
OS Ezakiella coagulans.
OC Bacteria; Bacillota; Tissierellia; Ezakiella.
OX NCBI_TaxID=46507 {ECO:0000313|EMBL:PVY94312.1, ECO:0000313|Proteomes:UP000245793};
RN [1] {ECO:0000313|EMBL:PVY94312.1, ECO:0000313|Proteomes:UP000245793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20705 {ECO:0000313|EMBL:PVY94312.1,
RC ECO:0000313|Proteomes:UP000245793};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) 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:PVY94312.1}.
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DR EMBL; QEKV01000005; PVY94312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1E392; -.
DR Proteomes; UP000245793; 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; 3.10.310.20; 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; 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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245793}.
FT DOMAIN 76..134
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 253..310
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 550 AA; 62175 MW; 9E16A0818297FA77 CRC64;
MGDFMVKVYI TGHKVPDTDT ICSAISYAEF LKKSGRAEAE PIRLGELNNE TKFVLEHFNV
DEPRLKTSMQ LKVHDLELDE PTIIYRDTPV KRAIELLQEK KTLLLSITDE YHKLLGVLSL
SDVTKSYMNV WDDMILHRSN TPLNNIVDVL SAKVLNEAKR ELTGKMVVYA MEPDELGDRI
KKGDVVIVGD RDNAQIDAIK RDVSLIIVSG GYKMKDEILE QAREKNISVL STELNSFMAA
RLLPLSIPAE FVMTSGEINA VNINDTVDEV KEKLAKTRFR SYPVLDDEGK IVGNLSRYHL
ITGKPKKLIL VDHNEKAQSI DNIDEAEIIQ IIDHHRIEPV STNSPVFFRN EPVGSTATII
SKMFFEEGIR PTKEVAGLLS SAIISDTLYF RSPTTTDDDR RMLERMALYA EIEPEEYANE
MFKAGTSVKG KSVSELLNMD VKEFKIMEES VRIAQIFTLD KESVLELKSE IISEMKKIRE
EKGNDTFVFV VTDIFDESSI VFVCGEYGVE IAGEFGEKIE ENEFFAPGLL SRKKQMVPKV
TDAIKKAKEN
//
