ID Q4K7T7_PSEF5 Unreviewed; 284 AA.
AC Q4K7T7;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN OrderedLocusNames=PFL_4612 {ECO:0000313|EMBL:AAY93859.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY93859.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY93859.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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}.
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DR EMBL; CP000076; AAY93859.1; -; Genomic_DNA.
DR RefSeq; WP_011062866.1; NC_004129.6.
DR AlphaFoldDB; Q4K7T7; -.
DR STRING; 220664.PFL_4612; -.
DR KEGG; pfl:PFL_4612; -.
DR PATRIC; fig|220664.5.peg.4717; -.
DR eggNOG; COG0676; Bacteria.
DR HOGENOM; CLU_048345_4_2_6; -.
DR Proteomes; UP000008540; Chromosome.
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 159
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 257
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 284 AA; 32388 MW; A61A9012F75F0E97 CRC64;
MHEHPLQRFF RSLRERPVFA WERYQLRDVL VIDHPLCQAV FSRQGAQLLH FQPAGQKPWL
WCAAKWPQVG AIRGGVPVCW PWYGRHPSEN AWPSHGWARL LDWKLLDSSS DEEGVRLHWQ
LQLCDWKVDL HARLGQSMDL RLSTEHQDTE PCQLSQALHA YWRIGDVGEI ALSGLDGAQG
YDQLNRQVCQ QQGELRVEGG CQRVFQHEGE LQLKDHAWQR ELCIDTGDHA DTVVWHPGTR
PLLGVSWNEV SRFICVEAAV GGTDSLRLAP GEQAHLSLQA RAAG
//