GenomeNet

Database: UniProt
Entry: I4F4Z6_9ACTN
LinkDB: I4F4Z6_9ACTN
Original site: I4F4Z6_9ACTN 
ID   I4F4Z6_9ACTN            Unreviewed;       249 AA.
AC   I4F4Z6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:CCH90709.1};
GN   OrderedLocusNames=MODMU_5335 {ECO:0000313|EMBL:CCH90709.1};
OS   Modestobacter marinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH90709.1, ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH90709.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC501 {ECO:0000313|EMBL:CCH90709.1,
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).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO203431; CCH90709.1; -; Genomic_DNA.
DR   RefSeq; WP_014743264.1; NC_017955.1.
DR   AlphaFoldDB; I4F4Z6; -.
DR   STRING; 477641.MODMU_5335; -.
DR   KEGG; mmar:MODMU_5335; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_033323_7_0_11; -.
DR   OMA; WCDVILR; -.
DR   OrthoDB; 5449373at2; -.
DR   Proteomes; UP000006461; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
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:SF68; GLUCOSYL-3-PHOSPHOGLYCERATE PHOSPHATASE; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT   REGION          229..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        15
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        106
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         14..21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   249 AA;  27370 MW;  81D1BE3CE4A41D66 CRC64;
     MAQSPGPSAL WLVRHGESMG NLADAQAHEQ GSGRLELDVR DPDVPLSSTG ESQADALGSW
     LAGLPAGERP TTVLSSPFTR AAATAQRAVA ASGADLTIRY DERLRERDFG AFDGMTRDGI
     REAYPDEARR RDLLGKFYYR PPGGESWADV ALRVRSLLAT EALRHDGERL LCVSHQAVVM
     VFRYVLEELT EPQLLEIDRG DQIANTSVTR YELSDGRFRL VTFNGVEHLD DHPDDEAPVT
     EENDVPSPA
//
DBGET integrated database retrieval system