ID A0A087E5D0_9BIFI Unreviewed; 224 AA.
AC A0A087E5D0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Fructose-2,6-bisphosphatase {ECO:0000313|EMBL:KFJ02981.1};
GN ORFNames=BISU_0908 {ECO:0000313|EMBL:KFJ02981.1};
OS Bifidobacterium subtile.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=77635 {ECO:0000313|EMBL:KFJ02981.1, ECO:0000313|Proteomes:UP000029055};
RN [1] {ECO:0000313|EMBL:KFJ02981.1, ECO:0000313|Proteomes:UP000029055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11597 {ECO:0000313|EMBL:KFJ02981.1,
RC ECO:0000313|Proteomes:UP000029055};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KFJ02981.1}.
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; JGZR01000007; KFJ02981.1; -; Genomic_DNA.
DR RefSeq; WP_024462950.1; NZ_JGZR01000007.1.
DR AlphaFoldDB; A0A087E5D0; -.
DR STRING; 77635.BISU_0908; -.
DR eggNOG; COG0406; Bacteria.
DR OrthoDB; 4131070at2; -.
DR Proteomes; UP000029055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000029055}.
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 9..16
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 224 AA; 25263 MW; 55E611E10E76014B CRC64;
MIVHLHLVRH GQTTFNRYNR LQGWSNAPLT DKGLADADKA GDKLRDIDFA AAYCSDTTRA
QTTAQRILDI NEQNGHKRPE LHADMHFREQ YYGYFEGQDM NVAWWAAGAP HGAPTYNAII
EQYGLGATKD FLKEADPFHD AESDEEYWQR IEGGYALIAN NQALHDGDHV LQISHGNTLL
SLMHRFAPEG YDLSERPANG SVTCFDFDTA QPIDRAFTVA SYNQ
//