ID I4EV95_9ACTN Unreviewed; 369 AA.
AC I4EV95;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:CCH87308.1};
DE EC=5.4.2.1 {ECO:0000313|EMBL:CCH87308.1};
GN Name=gpmB {ECO:0000313|EMBL:CCH87308.1};
GN OrderedLocusNames=MODMU_1871 {ECO:0000313|EMBL:CCH87308.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH87308.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH87308.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH87308.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
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DR EMBL; FO203431; CCH87308.1; -; Genomic_DNA.
DR RefSeq; WP_014739905.1; NC_017955.1.
DR AlphaFoldDB; I4EV95; -.
DR STRING; 477641.MODMU_1871; -.
DR KEGG; mmar:MODMU_1871; -.
DR PATRIC; fig|477641.3.peg.1766; -.
DR eggNOG; COG0328; Bacteria.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_035712_0_0_11; -.
DR OMA; GRWQIKH; -.
DR OrthoDB; 5296884at2; -.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:CCH87308.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 6..139
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT ACT_SITE 177
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 250
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 369 AA; 38943 MW; 5FA0DCD56F4DC6C5 CRC64;
MSGASAGRRL IVEADGGSRG NPGPAGYGAL VRDAETGRLL AERAESVGRA TNNVAEYGGL
VAGLQAALDL DPTASVEVRM DSKLVVEQMS GRWQIKHPDM KKLAVQARDI ARQLGAVRYT
WVPRAQNGAA DALANSAMDG KPVRRDLAAE PVVLEDETQP ATEPAPVVVT TTFLLRHGRT
EHTPERRFSG SSDLPLSELG RADAAAAAQH LAGRGIDVIV ASPLQRTRQT AEAAAAVLGV
PVEVDRDLRE LDFGSWEGLT AAEAQEKSPL AFRRWSGALD VRPPGGESIA DVSTRVARAR
ARVLDRHAGK TVLVVSHVTP IKLLLAAGLG AGDGIVHRVF LEAASLSTVT WSSDGRTSVR
LVNDTSHLG
//
