ID A0A1S2PH99_9ACTN Unreviewed; 555 AA.
AC A0A1S2PH99;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BIV23_38015 {ECO:0000313|EMBL:OIJ93141.1};
OS Streptomyces monashensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678012 {ECO:0000313|EMBL:OIJ93141.1, ECO:0000313|Proteomes:UP000179642};
RN [1] {ECO:0000313|EMBL:OIJ93141.1, ECO:0000313|Proteomes:UP000179642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 1 {ECO:0000313|EMBL:OIJ93141.1,
RC ECO:0000313|Proteomes:UP000179642};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 1.";
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:OIJ93141.1}.
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DR EMBL; MLYO01000076; OIJ93141.1; -; Genomic_DNA.
DR RefSeq; WP_071385540.1; NZ_MLYO01000076.1.
DR AlphaFoldDB; A0A1S2PH99; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000179642; 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:UP000179642}.
FT ACT_SITE 361
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 392
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT ACT_SITE 516
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ SEQUENCE 555 AA; 61341 MW; BBD9069618C885B6 CRC64;
MAATQRTGFP QLTHRPEWTA LADHRAEGRP HLRELFAQDP GRAERYVVRV GDLYIDYSKH
LITDETLALL QELATATDVF GLRDAMFRGE KINVTEDRAV LHTALRAPRD AVIEVDGENV
VPKVHAVLDT MARFADRVRS GEWTGHTGRR IRNVVNIGIG GSDLGPAMAY EALRPYTARE
LTFRFVSNVD GADLHEATRD LDPAETLFIV ASKTFTTIET ITNATSARSW LLRAFDGDDK
AVAKHFVALS TNAGKVTEFG IDPDNMFEFW DWVGGRYSYD SAIGLSLMIA IGPDRFREML
DGFHLVDEHF RTAPAEANAP LLLGLLGVWY GDFFDAQSHA VLPYSHYLSK FTAYLQQLDM
ESNGKSVQRD GRPVEWQTGP VVWGTPGTNG QHAYYQLIHQ GTKLIPADFI GFARPAGELS
GELRAQHDLL MANFFAQTQA LAFGKSAEEV RAEGVAEEQV AHRTFHGDHP TTTILAGEPT
PSVLGQLIAL YEHKVFVQGA IWNIDSFDQW GVELGKVLAK RVEPALTEGA DVPGLDPSSK
ALVAAYRTLK NATEN
//
