ID Q2JD27_FRACC Unreviewed; 378 AA.
AC Q2JD27;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ABD10815.1};
GN OrderedLocusNames=Francci3_1438 {ECO:0000313|EMBL:ABD10815.1};
OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD10815.1, ECO:0000313|Proteomes:UP000001937};
RN [1] {ECO:0000313|EMBL:ABD10815.1, ECO:0000313|Proteomes:UP000001937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45818 / CECT 9043 / CcI3
RC {ECO:0000313|Proteomes:UP000001937};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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DR EMBL; CP000249; ABD10815.1; -; Genomic_DNA.
DR RefSeq; WP_011435880.1; NZ_LRTJ01000010.1.
DR AlphaFoldDB; Q2JD27; -.
DR STRING; 106370.Francci3_1438; -.
DR KEGG; fra:Francci3_1438; -.
DR eggNOG; COG0328; Bacteria.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_035712_0_0_11; -.
DR OrthoDB; 5296884at2; -.
DR PhylomeDB; Q2JD27; -.
DR Proteomes; UP000001937; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd09279; RNase_HI_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR014636; RNaseH/PGlycerate_mutase.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF13456; RVT_3; 1.
DR PIRSF; PIRSF036922; RNaseH_PGAM; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001937}.
FT DOMAIN 3..144
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT ACT_SITE 183
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 252
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 378 AA; 40534 MW; DAE31A69A7C3B39D CRC64;
MGTVRRLVIE ADGGSRGNPG PAGYGAVVRD AGSGKLLAER ADSIGRATNN VAEYSGLIAG
LRAAAEIAPD AELEVRMDSK LVVEQMSGRW KVKHPAMRPL VAEATELAAR FPAVRFQWVP
RARNADADRL ANEAMDAAAA GRAWEPAVPQ SPDPVPHHAP TTNRLSGWMA PPAPPTTTVL
LRHGQTPLSV EKRFSGTVEA ALTDVGLGQA AAVANRLRDE PFDLVVSSPL KRARQTAEAL
GRDYVVVDDL RETDFGAWEG LTFAEVREKF PDELNAWLAD PHVPPPGGES LIATVARVAR
VRDRLLAEQP GGRVLIVSHV TPIKGLAQLA LAAEPAVLYR LHLDLVSMTT IDWYSDGPAV
LRGFNDTHHL AGQTIYGE
//
