ID D4BL96_BIFBR Unreviewed; 286 AA.
AC D4BL96;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=BIFBRE_02828 {ECO:0000313|EMBL:EFE90084.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE90084.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE90084.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE90084.1,
RC ECO:0000313|Proteomes:UP000003191};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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:EFE90084.1}.
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DR EMBL; ACCG02000002; EFE90084.1; -; Genomic_DNA.
DR RefSeq; WP_003827812.1; NZ_JDUD01000007.1.
DR AlphaFoldDB; D4BL96; -.
DR STRING; 1685.RY69_2092; -.
DR KEGG; bbrd:BBBR_1882; -.
DR PATRIC; fig|518634.20.peg.1967; -.
DR HOGENOM; CLU_048345_4_0_11; -.
DR Proteomes; UP000003191; 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:UP000003191}.
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 286 AA; 31132 MW; 84D8095D439C3575 CRC64;
MTDFVFRNID NSAGSATISD RGAHLLRWRP LSQATDVVFA PSSVVVAEGR PLGGGVPVIF
PWFGPGFADG HGLGKKPNHG FVRTRQWHLD AESFSNSYAH YSLTEADVPS DMLPWFEGDA
VPSFRADYEV HVADTLTMTL TVTNTGATPF SYEAALHTYF HVSDVSQIRL TGLEHAHYED
ATNGFAPCEQ PDEAVTFDGP VDRVYASTAA VELHDEGFGR TIHVAKSGSA QTVVWNPAEP
YGVLVNDSVN EEWRHFVCCE AAACREHAVR LEPGESHALT QTLSAA
//
