ID A0A139TQ71_9BACT Unreviewed; 563 AA.
AC A0A139TQ71;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=HMPREF3039_02050 {ECO:0000313|EMBL:KXU53805.1};
OS Akkermansia sp. KLE1798.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=1574265 {ECO:0000313|EMBL:KXU53805.1, ECO:0000313|Proteomes:UP000070454};
RN [1] {ECO:0000313|EMBL:KXU53805.1, ECO:0000313|Proteomes:UP000070454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1798 {ECO:0000313|EMBL:KXU53805.1,
RC ECO:0000313|Proteomes:UP000070454};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:KXU53805.1}.
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DR EMBL; LTZM01000040; KXU53805.1; -; Genomic_DNA.
DR RefSeq; WP_067572689.1; NZ_KQ971083.1.
DR AlphaFoldDB; A0A139TQ71; -.
DR PATRIC; fig|1574265.3.peg.1994; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000070454; 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); 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; 1.
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; 1.
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 80..137
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 563 AA; 62389 MW; 2FC2D5109A5C9143 CRC64;
MIPEQTERRP IYVIGHQNPD TDAICSAIGN AEFLRTHGEP DAIAARCGEM TLRTSWVLEK
AGVPEPVLIH DVTPTAGTIC RRDVISVSPD DTFLTAYRRM TENSLQTIPV IDADRNLHGL
LRYFDLLSLL MPLNMTEMNV RSVFSSLSNI AGTIDGKCLT GEMLSEEETQ NILLVGASSE
PSVRTRLANY KRKGIVQDLV VICGDRPNVQ LYAVEHGVRA LVTTAGSSPS LDIIETAQAT
GTCILSTPWD TASVGQLIRC SRKVREQVHT DYAVFPENMP LPELRQAAVK RKQALFPVMS
VKTNKMIGVL SKTDLVDPPR TQVALVDHNE FSQAVKGVEE AEIVEVMDHH RLGTQLSTRD
PIRFLNEPVG STSTLVARRF YHRDVEPSRS TAICLCAGIL SDTLNLTSPT TARADREMLE
WLTGIAKIDA KKFTEEFFAT GSLLRSKTAP SAIVQADRKT FTEYGHKISI SQIEEIGMYG
LKEVQEGLLE ELRKLEKEED LKLACLLVTD IVTHDSMLLA VGDEEVLEHI EYERLGPNLF
AAKDVVSRKK QLFPAISRAL KVL
//
