ID A0A261FET6_9BIFI Unreviewed; 297 AA.
AC A0A261FET6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN ORFNames=BTIS_1334 {ECO:0000313|EMBL:OZG57681.1};
OS Bifidobacterium tissieri.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1630162 {ECO:0000313|EMBL:OZG57681.1, ECO:0000313|Proteomes:UP000216444};
RN [1] {ECO:0000313|EMBL:OZG57681.1, ECO:0000313|Proteomes:UP000216444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100201 {ECO:0000313|EMBL:OZG57681.1,
RC ECO:0000313|Proteomes:UP000216444};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC EC=5.1.3.15; Evidence={ECO:0000256|ARBA:ARBA00001096};
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC {ECO:0000256|ARBA:ARBA00005866, ECO:0000256|PIRNR:PIRNR016020}.
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:OZG57681.1}.
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DR EMBL; MWWV01000007; OZG57681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FET6; -.
DR Proteomes; UP000216444; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd09020; D-hex-6-P-epi_like; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR025532; G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR PANTHER; PTHR11122; APOSPORY-ASSOCIATED PROTEIN C-RELATED; 1.
DR PANTHER; PTHR11122:SF39; GLUCOSE-6-PHOSPHATE 1-EPIMERASE; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PIRNR:PIRNR016020};
KW Reference proteome {ECO:0000313|Proteomes:UP000216444}.
FT ACT_SITE 161
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 271
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 297 AA; 32521 MW; B44C2816C97D9C87 CRC64;
MLMNDCFISR DFVNDDANAT ISDYGAHVLE WAPNGQPSVL WHPKAVHLSA GTAIRGGIPV
IFPWFNSGFV DGHIASKNPK HGFGRISFWH YDKDTSTDAF ARYTLDSADG HPDWLATLSG
STERPAAFNA TYEVHCGAEF QASLTVTNTG DMPFIYESAL HTYFAIGDIE HVQVSGLEGT
EFLDTTLDDD PKRVQADEPI TFDGNMVDRI YFAGGENRHD VVRILDERLG RMITVGKSGS
KNTVVWNPGE DAGNAIGDME AGEWRSFVCV EAANCRDNAT TLNPGESATL SQTIHVE
//
