ID Q1AY42_RUBXD Unreviewed; 501 AA.
AC Q1AY42;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=D,D-heptose 1,7-bisphosphate phosphatase {ECO:0000256|ARBA:ARBA00031828};
GN OrderedLocusNames=Rxyl_0716 {ECO:0000313|EMBL:ABG03686.1};
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG03686.1, ECO:0000313|Proteomes:UP000006637};
RN [1] {ECO:0000313|EMBL:ABG03686.1, ECO:0000313|Proteomes:UP000006637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC {ECO:0000313|Proteomes:UP000006637};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) 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}.
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DR EMBL; CP000386; ABG03686.1; -; Genomic_DNA.
DR RefSeq; WP_011563704.1; NC_008148.1.
DR AlphaFoldDB; Q1AY42; -.
DR STRING; 266117.Rxyl_0716; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; rxy:Rxyl_0716; -.
DR eggNOG; COG0241; Bacteria.
DR eggNOG; COG1216; Bacteria.
DR HOGENOM; CLU_546152_0_0_11; -.
DR OrthoDB; 9781367at2; -.
DR Proteomes; UP000006637; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
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; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 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; PF00535; Glycos_transf_2; 1.
DR Pfam; PF13242; Hydrolase_like; 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 Hydrolase {ECO:0000313|EMBL:ABG03686.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006637}.
FT DOMAIN 8..160
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 501 AA; 52575 MW; 0996275692A77548 CRC64;
MSRPAVDVVV PTAGRPSLRA LLEALARQPP PGRLLLVDDR RNPGGPLLPE GPPAGLAGRV
EVLRGPARGP AAARNAGWRA SGAGWVAFLD DDVVPEPGWT RDLLRDLSGL GPRVAASQGQ
LRVPLPAGRR PTDAERGVKG LETARWITAN IAYRREVLER LGGFDERFPR AYREDVELGL
RAVRSGLRIV GGERTVLHPA RPAGPLESVR RQAGNADDAL MLLLHGRAWR REAGVPPGRR
PRHLLVTAAG AAALAALAAG RRRDAALGAL LWLLGTTEFA ASRILPGPRT LPEVSSLLLS
SALIPPAASA CFALGLLRAR RLAPGGARRL PEAVLFDRDG TLVHDVPYNG DPEKVVPVPG
ARRALRRLRA AGVPAGVISN QSGVGRGLIS AEQVARVNRR VEELLGPFGA WALCCHRPED
GCGCRKPAPG LVLRAAAQLG ADPRRCVVIG DIGADVEAAR AAGARGILVP TPATRPEEVE
AAPEVAPDLE SAVELALGGG A
//
