ID A0A075KGJ2_9FIRM Unreviewed; 169 AA.
AC A0A075KGJ2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|ARBA:ARBA00031828, ECO:0000256|PIRNR:PIRNR004682};
DE EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR004682};
GN ORFNames=UFO1_3329 {ECO:0000313|EMBL:AIF52872.1};
OS Pelosinus sp. UFO1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF52872.1, ECO:0000313|Proteomes:UP000027983};
RN [1] {ECO:0000313|EMBL:AIF52872.1, ECO:0000313|Proteomes:UP000027983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFO1 {ECO:0000313|EMBL:AIF52872.1};
RX PubMed=25189589;
RA Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT Single-Molecule Real-Time DNA Sequencing Technology.";
RL Genome Announc. 2:e00881-14(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR004682-4};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR004682-4};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR004682}.
CC -!- SIMILARITY: Belongs to the gmhB family.
CC {ECO:0000256|PIRNR:PIRNR004682}.
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DR EMBL; CP008852; AIF52872.1; -; Genomic_DNA.
DR RefSeq; WP_038672634.1; NZ_CP008852.1.
DR AlphaFoldDB; A0A075KGJ2; -.
DR STRING; 484770.UFO1_3329; -.
DR KEGG; puf:UFO1_3329; -.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_085077_3_2_9; -.
DR OrthoDB; 9801899at2; -.
DR Proteomes; UP000027983; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07503; HAD_HisB-N; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004446; Heptose_bisP_phosphatase.
DR InterPro; IPR006543; Histidinol-phos.
DR NCBIfam; TIGR00213; GmhB_yaeD; 1.
DR NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR NCBIfam; TIGR01656; Histidinol-ppas; 1.
DR PANTHER; PTHR42891; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR PANTHER; PTHR42891:SF1; D-GLYCERO-BETA-D-MANNO-HEPTOSE-1,7-BISPHOSPHATE 7-PHOSPHATASE; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR PIRSF; PIRSF004682; GmhB; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR004682};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR004682};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR004682};
KW Magnesium {ECO:0000256|PIRSR:PIRSR004682-4};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004682-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000027983};
KW Zinc {ECO:0000256|PIRSR:PIRSR004682-4}.
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT ACT_SITE 12
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-1"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-4"
FT SITE 52
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 109
FT /note="Contributes to substrate recognition"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
FT SITE 110
FT /note="Stabilizes the phosphoryl group"
FT /evidence="ECO:0000256|PIRSR:PIRSR004682-3"
SQ SEQUENCE 169 AA; 19115 MW; 7D690B19DDAB8575 CRC64;
MKKQPAVFFD RDGVLNVDKG YISKREEMVW MPGAIDAIKL LNDKGYFVFV VTNQSGIARG
YFQEEDVYEF HSYMADEVEK QEAVIHSFYF CPHHPEGIIE PYSTVCNCRK PLPGLIGQAC
QEWPVDLSAS FLIGDMQRDL DAAKGAGIPG YLFSGGNLYD FVQDILNNR
//
