ID A0A087CNS2_9BIFI Unreviewed; 252 AA.
AC A0A087CNS2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Putative phosphoglycerate mutase {ECO:0000313|EMBL:KFI84922.1};
DE EC=3.1.3.37 {ECO:0000313|EMBL:KFI84922.1};
GN ORFNames=BREU_2261 {ECO:0000313|EMBL:KFI84922.1};
OS Bifidobacterium reuteri DSM 23975.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI84922.1, ECO:0000313|Proteomes:UP000028984};
RN [1] {ECO:0000313|EMBL:KFI84922.1, ECO:0000313|Proteomes:UP000028984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI84922.1,
RC ECO:0000313|Proteomes:UP000028984};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI84922.1}.
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DR EMBL; JGZK01000014; KFI84922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087CNS2; -.
DR STRING; 1437610.BREU_2261; -.
DR eggNOG; COG0406; Bacteria.
DR Proteomes; UP000028984; Unassembled WGS sequence.
DR GO; GO:0050278; F:sedoheptulose-bisphosphatase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF15; SEDOHEPTULOSE 1,7-BISPHOSPHATASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KFI84922.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028984}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 42
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 117
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 54..55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 117..120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 206
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 252 AA; 27337 MW; 89AAFAEF75E67650 CRC64;
MAKVESGARR DYSGGMSEQN QNGTVAVESS RGGTGFLVLL RHGQTVWSES GQHTGRTDIP
LTEVGRQQAR EAGQRLRDAF PGGFADGCVF SSPLKRARQT AALAGFENCG VLDGIAEWDY
GPAEGRTRQQ VSEACGFQWD IWRDGPRSLG ADMQGDWVET LPSGEQVAVH NGPGETLEEA
AARAKGAIDE VLPLLEGGHN VLLVAHAHIL RILTSQWLGV DPHFARLLRL DTAHYSVLSV
YKGDHVIERW NA
//