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Database: UniProt
Entry: Q4K7T7_PSEF5
LinkDB: Q4K7T7_PSEF5
Original site: Q4K7T7_PSEF5 
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
//
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