ID C2GST1_BIFLN Unreviewed; 304 AA.
AC C2GST1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=HMPREF0175_0077 {ECO:0000313|EMBL:EEI81610.1};
OS Bifidobacterium longum subsp. longum ATCC 55813.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=548480 {ECO:0000313|EMBL:EEI81610.1, ECO:0000313|Proteomes:UP000004443};
RN [1] {ECO:0000313|EMBL:EEI81610.1, ECO:0000313|Proteomes:UP000004443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55813 {ECO:0000313|EMBL:EEI81610.1,
RC ECO:0000313|Proteomes:UP000004443};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:EEI81610.1}.
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DR EMBL; ACHI01000005; EEI81610.1; -; Genomic_DNA.
DR AlphaFoldDB; C2GST1; -.
DR HOGENOM; CLU_048345_4_0_11; -.
DR Proteomes; UP000004443; 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}.
FT ACT_SITE 170
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 304 AA; 32937 MW; 71FAFC1200095684 CRC64;
MKNIAYATEE ETLMGNGVNL RTLTNDGGSA VISDYGAHLL RWAPAGQPDV IWTPRTWHFE
AGQPVGGGVP VCFPWFGPGF VHGGQTAKRP IHGFARLRQW ALDEEAFTGA RVRYVLDSER
LTTGEVPWIE DEPNVRFHAA YEVCASDTLT MTLTVTNTGG EPMSYEAALH SYLHVGDVLG
ARLVGLRGAT YLDATEAGFP PKLQEQPSVM FGDQPVDRVY YSDAALELQD HVLGRVIRIG
KTGSPQTVVW NPGEQGGNAI AHAKTGEWRG FVAVEAAACR DRIVALSPGE SYMLSQSIAV
MPLG
//
