Y1317_HAEIN
ID Y1317_HAEIN Reviewed; 271 AA.
AC P44160;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000250|UniProtKB:Q03161};
DE EC=5.1.3.15 {ECO:0000250|UniProtKB:Q03161};
DE AltName: Full=Putative D-hexose-6-phosphate mutarotase {ECO:0000250|UniProtKB:Q03161};
GN OrderedLocusNames=HI_1317;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:0000250|UniProtKB:Q03161};
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC {ECO:0000305}.
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; L42023; AAC22962.1; -; Genomic_DNA.
DR PIR; G64025; G64025.
DR RefSeq; NP_439468.1; NC_000907.1.
DR STRING; 71421.HI_1317; -.
DR EnsemblBacteria; AAC22962; AAC22962; HI_1317.
DR KEGG; hin:HI_1317; -.
DR PATRIC; fig|71421.8.peg.1369; -.
DR eggNOG; COG0676; Bacteria.
DR HOGENOM; CLU_048345_4_1_6; -.
DR OMA; MWAIDEN; -.
DR PhylomeDB; P44160; -.
DR BioCyc; HINF71421:G1GJ1-1342-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IBA:GO_Central.
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 Pfam; PF01263; Aldose_epim; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome.
FT CHAIN 1..271
FT /note="Putative glucose-6-phosphate 1-epimerase"
FT /id="PRO_0000213037"
FT ACT_SITE 151
FT /evidence="ECO:0000250|UniProtKB:Q03161"
FT ACT_SITE 249
FT /evidence="ECO:0000250|UniProtKB:Q03161"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q03161"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q03161"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q03161"
SQ SEQUENCE 271 AA; 30802 MW; 1B6FB70991EFF9FB CRC64;
MKTTLLKTLT PELHLVQHND IPVPSLKTCG WNTKNFPCKG HSLSVGXPQN AKQDVLWLSE
VEPFKNGNAI RGGVPICYPW FGGVKQPAHG TARIRLWQLS HYYISVHKVR LEFELFSDLN
IIEAKVSMVF TDKCHLTFTH YGEESAQAAL HTYFNIGDIN QVEVQGLPET CFNSLNQQQE
NVPSPRHISE NVDCIYSAEN MQNQILDKSF NRTIALHHHN ASQFVLWNPW HKKTSGMSET
GYQKMLCLET ARIHHLLEFG ESLSVEISLK G
