ID A0A0G1LT60_9BACT Unreviewed; 410 AA.
AC A0A0G1LT60;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN ORFNames=UW63_C0002G0010 {ECO:0000313|EMBL:KKT72042.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWF2_44_350.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1619000 {ECO:0000313|EMBL:KKT72042.1, ECO:0000313|Proteomes:UP000034154};
RN [1] {ECO:0000313|EMBL:KKT72042.1, ECO:0000313|Proteomes:UP000034154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
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:KKT72042.1}.
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DR EMBL; LCJB01000002; KKT72042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1LT60; -.
DR PATRIC; fig|1619000.3.peg.30; -.
DR UniPathway; UPA00109; UER00181.
DR Proteomes; UP000034154; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612}.
SQ SEQUENCE 410 AA; 45215 MW; 61BB7D78D5FB6FDF CRC64;
MNFLKYNSDN MFIGLSKNDL KKFQPKIKQA EAALKNLQAS GQQGFFNLPF DIPGAKTIEK
KAKEVQKKFS RLLVIGIGGS DLGARAVWQA CPGKKMEVVF LSNTDPDTVA MVLNLSPEEW
KKTAINVVSK SGSTVETMSN FMVARERLIR SIGQTAHRAH IYVTTEVDGK LALWATEQGY
EVLAHPKNVG GRFSVLSLVG LFPVACGGVP ITRLLAGARE VVYSEAANFA ALQFLAYKKG
QEIQVLMPYS DSLGNFPFWY RQLWAESLGK KGQGPTPIAA RGTIDQHSQI QLYNDGPNNK
TITFIEIEKF KNRIKIPKNI PGLDHVSDKD FSDLMHSELH GTAEALKKNK RMNGKISIPT
LSPESLGALF QFFILAAAFS GEFYGINAYN QPGVEEGKRL ARKELAGQKA
//
