ID D1PHS6_9BACT Unreviewed; 433 AA.
AC D1PHS6;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|ARBA:ARBA00031828};
GN Name=gmhB {ECO:0000313|EMBL:EFB33742.1};
GN ORFNames=PREVCOP_06796 {ECO:0000313|EMBL:EFB33742.1};
OS Segatella copri DSM 18205.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=537011 {ECO:0000313|EMBL:EFB33742.1, ECO:0000313|Proteomes:UP000004477};
RN [1] {ECO:0000313|EMBL:EFB33742.1, ECO:0000313|Proteomes:UP000004477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18205 {ECO:0000313|EMBL:EFB33742.1,
RC ECO:0000313|Proteomes:UP000004477};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the GmhB family.
CC {ECO:0000256|ARBA:ARBA00005628}.
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:EFB33742.1}.
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DR EMBL; ACBX02000059; EFB33742.1; -; Genomic_DNA.
DR RefSeq; WP_006849461.1; NZ_VZAC01000086.1.
DR AlphaFoldDB; D1PHS6; -.
DR STRING; 537011.PREVCOP_06796; -.
DR PaxDb; 537011-PREVCOP_06796; -.
DR GeneID; 69848430; -.
DR HOGENOM; CLU_028110_0_0_10; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000004477; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd07503; HAD_HisB-N; 1.
DR CDD; cd04181; NTP_transferase; 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 InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
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 Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000004477}.
FT DOMAIN 2..244
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 433 AA; 48266 MW; 2712FC1348846D90 CRC64;
MKTILMAGGR GTRIAELFPN IPKPLIPVAG MPILEREIKS LCAQGFKDII LTVGYLADKI
IAYFGDGSQF GAKIDYFVEE SPLGNAGALF RLREKLGDEP FLLLNADAAF DVDFNRMVAF
HKNHGGLVTL FTHPNSHPYD SGLIIADENG HVEKWLAKED ERPQWYDNRV NAGLHVIDPK
ALDIGLKSLE INKESGFPQG KVDLDRQILK PLCGSNMMFC YDSPEYVKDM GTPERFHQVE
ADYKNGVVQA KNLTNKQKAI FLDRDGTINK YVGFLRNIDD FELIEGVAEA IKLINQSGYL
AIVVTNQPVI ARGEVTWEEL NEIHKKMATL LGKEGAYVDG IYICPHHPDK GFEGERPEYK
IDCDCRKPKP GLLLQAARDF NIDLAESYMI GDSHRDVEAG ENAGVKKSIK VEENKAGTLT
HIAAVFDEKL KDS
//
