ID G6PI_STRGG Reviewed; 552 AA.
AC B1W0Z7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=SGR_5578;
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350;
RX PubMed=18375553; DOI=10.1128/jb.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
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DR EMBL; AP009493; BAG22407.1; -; Genomic_DNA.
DR RefSeq; WP_012381401.1; NC_010572.1.
DR AlphaFoldDB; B1W0Z7; -.
DR SMR; B1W0Z7; -.
DR GeneID; 6214275; -.
DR KEGG; sgr:SGR_5578; -.
DR PATRIC; fig|455632.4.peg.5713; -.
DR eggNOG; COG0166; Bacteria.
DR HOGENOM; CLU_017947_3_1_11; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001685; Chromosome.
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; Gluconeogenesis; Glycolysis; Isomerase.
FT CHAIN 1..552
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125762"
FT ACT_SITE 359
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 390
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 514
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 552 AA; 60820 MW; 2E34413F7DE110F0 CRC64;
MNAASRTKLN QTPEWTALAK HREELGAPRL RELFARQPDR GTAYTLRVGD LHLDYSKHLV
TDETLRLLRE LAAATGVAEL REAMFRGEKI NTTEDRAVLH TALRAPRDAV VEVDGENVVP
AVHAVLDKMA GFAEKVRSGQ WTGHTGKPVK NIVNIGIGGS DLGPAMAYEV LRSFTDRDLT
LRFVSNVDGA DLHEAVRDLD PAETLFVIAS KTFTTIETIT NATSARDWLL TELRTGQDAV
AKHFVALSTN AEKVEEFGID TANMFEFWDW VGGRYSYDSA IGLSLMVAIG PDRFREMLEG
FHLVDEHFRT APPEENAPLL LGLLGVWYGN FFDAQSHAVL PYSHYLSKFT AYLQQLDMES
NGKSVDRDGN PVDWQTGPVV WGTPGTNGQH AYYQLIHQGT KLIPADFIGF AAPVHDLLPG
LIAQHDLLMA NFFAQTQALA FGKTPEEVRA EGVPEELVPH KTFRGNHPTT TILADKLTPS
VLGQLIALYE HKVFVQGAIW NIDSFDQWGV ELGKVLAKKI EPLLTGDGGA DAGELDSSTA
ALVDAYRTLR GR
//
