ID L7CN30_RHOBT Unreviewed; 551 AA.
AC L7CN30;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=RBSWK_01017 {ECO:0000313|EMBL:ELP35017.1};
OS Rhodopirellula baltica SWK14.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993516 {ECO:0000313|EMBL:ELP35017.1, ECO:0000313|Proteomes:UP000010959};
RN [1] {ECO:0000313|EMBL:ELP35017.1, ECO:0000313|Proteomes:UP000010959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWK14 {ECO:0000313|EMBL:ELP35017.1,
RC ECO:0000313|Proteomes:UP000010959};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:ELP35017.1}.
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DR EMBL; AMWG01000021; ELP35017.1; -; Genomic_DNA.
DR RefSeq; WP_007326733.1; NZ_AMWG01000021.1.
DR AlphaFoldDB; L7CN30; -.
DR PATRIC; fig|993516.3.peg.1074; -.
DR Proteomes; UP000010959; 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; 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 72..129
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 551 AA; 61266 MW; B893F96F40BB1B98 CRC64;
MTVHVFGHRN PDTDAICSAL AYADFLRRTT RPDAVAACCG PPNERTEFAL RKAKLTAPKI
IMDVRPELED ICNRDVIVAR TSDVFYEVYE RMDEHELRSI PVLDDNDQLI GLVTLLDLLE
LVFQGGVDPY RSREVRTNLD KVVSVLGGSY QHAVDSSLNE DMILTVGAMS AGGFCERMKQ
FPADRLLVVS GDRPTIQLPA LEMGVRGLVV TGGYELSSGL MELARGRGVT VINSPYDTAT
TTMRIKAAQL IEEVVNRDFL ALSAKLPVAA AKQQIYRSAQ TVFPVVDNQK LIGVLSKSDM
VHPPRPQLVL VDHNEIGQAV EGAEDSDIVE VLDHHRLGGS LKSTGPIRFI MDPVGSTCTL
VARMYRQEGL EPEPGIALCM ASGIISDTLY LRSPTTTDVD RELLEWLQGY CKVELAEYAN
EFFEIGSALR SCTPDKVVRE DCKQFEENGR RFSISQIEEI GLDLFWERQA ELSQALVRLS
EEENLEFSAL LVTDISSNGS LLLMSSEPEG WEEINYPQLE DRLYKLENVV SRKKQLLPLI
SSLLENSPEP T
//
