ID D2NQY7_ROTMD Unreviewed; 429 AA.
AC D2NQY7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Fructose-2,6-bisphosphatase {ECO:0000313|EMBL:BAI64063.1};
GN OrderedLocusNames=RMDY18_02310 {ECO:0000313|EMBL:BAI64063.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64063.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64063.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64063.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64063.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64063.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
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DR EMBL; AP011540; BAI64063.1; -; Genomic_DNA.
DR RefSeq; WP_012902838.1; NC_013715.1.
DR AlphaFoldDB; D2NQY7; -.
DR STRING; 680646.RMDY18_02310; -.
DR KEGG; rmu:RMDY18_02310; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_598374_0_0_11; -.
DR Proteomes; UP000001883; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 2.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 2.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 2.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT ACT_SITE 242
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 318
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 241..248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 318..321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 429 AA; 47075 MW; 1D68D2979AF63AAC CRC64;
MTDAQNTPII TPVADPEAGT RIIFLRHGQT DWNIDHRFQG GTDIPLNDTG REQVRTAIGA
LKQAAAEGTT VDAIVSSPLS RAVESAEIVA EGLGVPYRGA VDGFQERSFG DLEGQIATRE
LILASRQSNN AFNVEPKKDF LARSLAALNR VRREYEGQTV VVAAHGMLIA MTMTALVAER
HPELLNEDGI YPIPVNASLT EVPLQYLDNA IDRLVVQHLE PELGPEEVPA GAENTTLTLI
RHGQTDWNKA NLMQGITDIP LNDTGREQAR TTGKKLADMG LEFTVLVSSP LSRAHETAQL
VGEHFDLQVH KTYPELVERA YGAGEGLDIP APERRAPERY YPNVESERDV YIRAVRTLRN
IVRELSEGSG DQKIIAVSHG SFIRRALSAA AGEEWTVTVP NAEPLTIDVP GLFAWDSTKQ
FDEVGRLVW
//
