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Database: UniProt
Entry: A0A2A3H878_9ACTN
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ID   A0A2A3H878_9ACTN        Unreviewed;       137 AA.
AC   A0A2A3H878;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
GN   ORFNames=BKI49_08045 {ECO:0000313|EMBL:PBC64647.1};
OS   Streptomyces sp. Tue6028.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2036037 {ECO:0000313|EMBL:PBC64647.1, ECO:0000313|Proteomes:UP000217789};
RN   [1] {ECO:0000313|EMBL:PBC64647.1, ECO:0000313|Proteomes:UP000217789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tue6028 {ECO:0000313|EMBL:PBC64647.1,
RC   ECO:0000313|Proteomes:UP000217789};
RA   Greule A., Flemming S., Bechthold A.;
RT   "The Draft Genome Sequence of Streptomyces sp. Tue6028 - Producer of
RT   Polyketomycin and Foxicin.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:PBC64647.1}.
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DR   EMBL; MLCE01000009; PBC64647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3H878; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000217789; 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; cd05016; SIS_PGI_2; 1.
DR   Gene3D; 1.10.1390.10; -; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
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; PS00174; P_GLUCOSE_ISOMERASE_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217789}.
SQ   SEQUENCE   137 AA;  15062 MW;  02BFC254ABABC66B CRC64;
     MDDLQPGLVA QHDLLMANFF AQTQALAFGK TPDEVRAEGV PEELVPHKTF RGNHPTTTIL
     ARELTPSVLG QLIALYEHKV FVQGAVWNID SFDQWGVELG KVLAKKIEPA LTEGTDVPGL
     DASTQALVAK YRELRGR
//
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