ID A0A1J4NU57_9ACTN Unreviewed; 548 AA.
AC A0A1J4NU57;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN ORFNames=WN71_027200 {ECO:0000313|EMBL:OIJ64781.1};
OS Streptomyces mangrovisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ64781.1, ECO:0000313|Proteomes:UP000034196};
RN [1] {ECO:0000313|EMBL:OIJ64781.1, ECO:0000313|Proteomes:UP000034196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000256|HAMAP-Rule:MF_00473}.
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|ARBA:ARBA00029321,
CC ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473,
CC ECO:0000256|RuleBase:RU000612}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|HAMAP-Rule:MF_00473, 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:OIJ64781.1}.
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DR EMBL; LAVA02000071; OIJ64781.1; -; Genomic_DNA.
DR RefSeq; WP_046590740.1; NZ_LAVA02000071.1.
DR AlphaFoldDB; A0A1J4NU57; -.
DR STRING; 1428628.WN71_027200; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034196; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 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; 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; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00473};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473};
KW Reference proteome {ECO:0000313|Proteomes:UP000034196}.
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 389
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 513
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 548 AA; 60382 MW; 8B99BDE323F33FAD CRC64;
MTDTPRLDRR PEWTALEDHR AHWQDHLREL FAADPGRAER YVVRVGDLRI DYSKHLITDE
TLALLRELAA ATDVFGLRDA MFRGARINVT EDRAVLHTAL RAPRDAVVEV DGENVVPGVH
AVLDKMADFA GRVRSGEWTG HTGKRIRNVV NIGIGGSDLG PAMAYEVLRP FTARELTFRF
VSNVDGADLH EAVRDLDPAE TLFIVASKTF TTIETITNAT SARTWLLEGP HGLGDEKAVA
RHFVALSTNA GKVTDFGIDP DNMFEFWDWV GGRYSYDSAI GLSLMIAIGP ERFREMLDGF
HLVDEHFRTA PAEANAPLIL GLLGIWYGNF FDAQSHAVLP YSHYLSKFTA YLQQLDMESN
GKSVDRDGEP VDWQTGPVVW GTPGTNGQHA YYQLIHQGTK LIPADFIGFA RPVGELSDVL
KAQHDLLMAN FFAQTQALAF GKTADEVRAE GVAEAQVSPR TFQGNHPTTT ILAAELTPSV
LGQLVALYEH KVFVQGAVWD IDSFDQWGVE LGKVLAKRIE PALTEGADVP GLDPSTAALV
AAYRELGK
//
