G6PIB_ORYSJ
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 03-AUG-2022, entry version 127.
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; 4530.OS06T0256500-01; -.
DR iPTMnet; P42863; -.
DR PaxDb; P42863; -.
DR PRIDE; P42863; -.
DR GeneID; 4340677; -.
DR KEGG; osa:4340677; -.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_017947_4_0_1; -.
DR InParanoid; P42863; -.
DR OrthoDB; 446616at2759; -.
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 Genevisible; P42863; OS.
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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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.
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
