ID A4HB57_LEIBR Unreviewed; 301 AA.
AC A4HB57;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 13-SEP-2023, entry version 75.
DE RecName: Full=glucose-6-phosphate 1-epimerase {ECO:0000256|ARBA:ARBA00012083, ECO:0000256|PIRNR:PIRNR016020};
DE EC=5.1.3.15 {ECO:0000256|ARBA:ARBA00012083, ECO:0000256|PIRNR:PIRNR016020};
GN ORFNames=LBRM_20_2970 {ECO:0000313|EMBL:CAM38643.1};
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM38643.1, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM38643.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM38643.1,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
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; FR798994; CAM38643.1; -; Genomic_DNA.
DR RefSeq; XP_001564577.1; XM_001564527.1.
DR AlphaFoldDB; A4HB57; -.
DR STRING; 5660.A4HB57; -.
DR GeneID; 5415128; -.
DR KEGG; lbz:LBRM_20_2970; -.
DR VEuPathDB; TriTrypDB:LbrM.20.2970; -.
DR VEuPathDB; TriTrypDB:LBRM2903_200043200; -.
DR InParanoid; A4HB57; -.
DR OMA; RNMNWSI; -.
DR Proteomes; UP000007258; Chromosome 20.
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:UP000007258}.
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ SEQUENCE 301 AA; 32810 MW; 54EB3E025B69FB8D CRC64;
MFAFAPDPRG RNSITLHNED GSSITVYEQG AHLSSWKTKD EKEHLYLSPA AIYADGTALR
GGVPLIFPQF NAYGPMKPPH GFARIRPWNI EDVQNGKATF SLSTSLCELL PEGCSLAGAA
TNAVNLLYTI CFSNTELKLR MKVTNTSEEH SAPFQFAFHT YFAVSDISQT VINGVNRSPF
IDNGKACGNP HTEPSPPEPL WTIQGEHDRI YPGQSCAIVL QDLGAKAALQ ISSPNLCDVC
LWNPGAVKCA AMKDMPADGY KRFVCVEHGS MLKKIVVTPC SSWTGSQEIT ITTQSPQESN
I
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