ID   G6PIB_ORYSJ             Reviewed;         567 AA.
AC   P42863; Q652G2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Glucose-6-phosphate isomerase, cytosolic B {ECO:0000305};
DE            Short=GPI-B {ECO:0000305};
DE            EC=5.3.1.9 {ECO:0000269|PubMed:8722567};
DE   AltName: Full=Phosphoglucose isomerase B {ECO:0000303|PubMed:8722567};
DE            Short=PGI-B {ECO:0000303|PubMed:8722567};
DE   AltName: Full=Phosphohexose isomerase B {ECO:0000305};
DE            Short=PHI-B {ECO:0000305};
GN   OrderedLocusNames=Os06g0256500 {ECO:0000312|EMBL:AP014962},
GN   LOC_Os06g14510 {ECO:0000305};
GN   ORFNames=P0624H09.14 {ECO:0000312|EMBL:BAD46305.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=8722567; DOI=10.3109/10425179609010200;
RA   Nozue F., Umeda M., Nagamura Y., Minobe Y., Uchimiya H.;
RT   "Characterization of cDNA encoding for phosphoglucose isomerase of rice
RT   (Oryza sativa L.).";
RL   DNA Seq. 6:127-135(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Catalyzes the conversion of glucose-6-phosphate to fructose-
CC       6-phosphate, the second step in glycolysis, and the reverse reaction
CC       during gluconeogenesis. {ECO:0000305|PubMed:8722567}.
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:0000269|PubMed:8722567};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06745}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8722567}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA08149.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D45218; BAA08149.1; ALT_FRAME; mRNA.
DR   EMBL; AP005619; BAD46305.1; -; Genomic_DNA.
DR   EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; T03950; T03950.
DR   RefSeq; XP_015644261.1; XM_015788775.1.
DR   RefSeq; XP_015644262.1; XM_015788776.1.
DR   RefSeq; XP_015644263.1; XM_015788777.1.
DR   AlphaFoldDB; P42863; -.
DR   SMR; P42863; -.
DR   STRING; 39947.P42863; -.
DR   iPTMnet; P42863; -.
DR   PaxDb; 39947-P42863; -.
DR   GeneID; 4340677; -.
DR   KEGG; osa:4340677; -.
DR   eggNOG; KOG2446; Eukaryota.
DR   HOGENOM; CLU_017947_4_0_1; -.
DR   InParanoid; P42863; -.
DR   OrthoDB; 1657888at2759; -.
DR   PlantReactome; R-OSA-1119410; Ascorbate biosynthesis.
DR   PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR   PlantReactome; R-OSA-1119570; Cytosolic glycolysis.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IDA:Gramene.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:Gramene.
DR   GO; GO:0016853; F:isomerase activity; ISS:Gramene.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IEP:Gramene.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IEP:Gramene.
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; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
DR   Genevisible; P42863; OS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT   CHAIN           1..567
FT                   /note="Glucose-6-phosphate isomerase, cytosolic B"
FT                   /id="PRO_0000180567"
FT   ACT_SITE        360
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         156..157
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         212..217
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         356
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         360
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         391
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         516
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   CONFLICT        374
FT                   /note="S -> P (in Ref. 1; BAA08149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="T -> S (in Ref. 1; BAA08149)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   567 AA;  62368 MW;  57D56738888AE630 CRC64;
     MASSALICDT EQWKGLQAHV GAIQKTHLRD LMDDAERCKA MTAEYEGIFL DYSRQRATGE
     TMEKLFKLAE AAKLKEKIEK MFSGDKINST ENRSVLHVAL RAPRDEVIKS DGVNVVPEVW
     GVKDKIKQFS ETFRSGSWVG ATGKALTNVV SVGIGGSFLG PLFVHAALQT DPEAAESAKG
     RQLRFLANVD PVDVARSIKD LDPETTLVVV VSKTFTTAET MLNARTLKEW IVSSLGPDAV
     AKHMIAVSTN LELVEKFGID PKNAFAFWDW VGGRYSVCSA VGVLPLSLQY GFPIVQKFLE
     GAASIDKHFR SSSFEKNIPV LLGLLSVWNV SFLGYPARAI LPYSQALEKF APHIQQLSME
     SNGKGVSIDG VQLSFETGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK
     GEIVSNHDEL MSNFFAQPDA LAYGKTPEQL HSEKVPEHLI SHKTFQGNRP SLSLLLPSLS
     AYEIGQLLSI YEHRIAVQGF LWGINSFDQW GVELGKSLAS QVRKSLHASR MEGKPVQGFN
     SSTASLLTRY LAVEPSTPYN TTTMPKV
//