ID A0A1Y4DN60_9ACTN Unreviewed; 555 AA.
AC A0A1Y4DN60;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=B5F73_06780 {ECO:0000313|EMBL:OUO59139.1};
OS Olsenella sp. An270.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1965615 {ECO:0000313|EMBL:OUO59139.1, ECO:0000313|Proteomes:UP000195449};
RN [1] {ECO:0000313|Proteomes:UP000195449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An270 {ECO:0000313|Proteomes:UP000195449};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO59139.1}.
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DR EMBL; NFJF01000005; OUO59139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4DN60; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000195449; 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; 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 255..313
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 555 AA; 60907 MW; 135F63E482D05850 CRC64;
MPEGIRKINV IGHLHPDTDS ICSAIAYAHL KNEVEHTNIY EPRRAGAINR ETAFVLRHFG
FEEPQLITSV TPQIKDTEIQ RQGGIDGEMS LFSAWNLMRE AKTDTLCITD EENNLEGLIA
VKDIANANMD VFDTSVIGES HTCYANIIDT LKGEMILGDP TARVDGGNVR VGTTPELMED
TVEPGDIVLT TNRYETQQFA VECDARCLIV CCSAHISHRV IASAERHGCA IITTPYDTYA
AARLVSMSIP VRAKMLSEGI LKVSVNTAID DARKMMAHTR HRFFPVIDEN SKYVGLVSSP
NLLSAKRKHV ILVDHNERSQ SVEGLEQAEI MEIIDHHRIG SIETSGPAYF RNMPVGCTCT
IVHMMYRENG VRIPKDIAGL MLSAILSDTL AFRSPTCTQV DRDAAAALAE IAGVDIESYA
DAMFEAGADL TGRTAEEVFG ADFKVFSRGN VKFGVGQGSY MTEKSRKAAE ALVGPYLAEA
AREEELPLVF YLFTDVKSSS SEILWYGEGA ESIVARAFDV DPHDGMALLP GVVSRKKQVI
PSLMATLQSI QEDQD
//
