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G6PIA_ORYSJ
ID   G6PIA_ORYSJ             Reviewed;         567 AA.
AC   P42862; A0A0P0W3M8; Q10DK3; Q8H8M6;
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 A {ECO:0000305};
DE            Short=GPI-A {ECO:0000305};
DE            EC=5.3.1.9 {ECO:0000269|PubMed:8722567};
DE   AltName: Full=Phosphoglucose isomerase A {ECO:0000303|PubMed:8722567};
DE            Short=PGI-A {ECO:0000303|PubMed:8722567};
DE   AltName: Full=Phosphohexose isomerase A {ECO:0000305};
DE            Short=PHI-A {ECO:0000305};
GN   OrderedLocusNames=Os03g0776000 {ECO:0000312|EMBL:BAF13348.1},
GN   LOC_Os03g56460 {ECO:0000312|EMBL:ABF99132.1};
GN   ORFNames=OsJ_12779 {ECO:0000312|EMBL:EEE60024.1},
GN   OSJNBa0070N04.5 {ECO:0000312|EMBL:AAN65024.1};
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=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [3]
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   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
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).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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}.
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DR   EMBL; D45217; BAA08148.1; -; mRNA.
DR   EMBL; AC091494; AAN65024.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99131.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99132.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13348.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS86635.1; -; Genomic_DNA.
DR   EMBL; CM000140; EEE60024.1; -; Genomic_DNA.
DR   PIR; T03948; T03948.
DR   RefSeq; XP_015632584.1; XM_015777098.1.
DR   RefSeq; XP_015632585.1; XM_015777099.1.
DR   AlphaFoldDB; P42862; -.
DR   SMR; P42862; -.
DR   STRING; 4530.OS03T0776000-01; -.
DR   iPTMnet; P42862; -.
DR   PaxDb; P42862; -.
DR   PRIDE; P42862; -.
DR   EnsemblPlants; Os03t0776000-01; Os03t0776000-01; Os03g0776000.
DR   GeneID; 4334290; -.
DR   Gramene; Os03t0776000-01; Os03t0776000-01; Os03g0776000.
DR   KEGG; osa:4334290; -.
DR   eggNOG; KOG2446; Eukaryota.
DR   HOGENOM; CLU_017947_4_0_1; -.
DR   InParanoid; P42862; -.
DR   OMA; VERCKAM; -.
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 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; P42862; 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; IDA:Gramene.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IDA:Gramene.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IDA: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 A"
FT                   /id="PRO_0000180566"
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="P -> S (in Ref. 1; BAA08148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        377
FT                   /note="S -> T (in Ref. 1; BAA08148)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   567 AA;  62524 MW;  E01202380A9A9C8E CRC64;
     MASSALICDT EQWKGLQAHV GEIQKTHLRH LMHDVERCKA MTAEYEGIYL DYSRQRATGE
     TMEKLFKLAE AAKLKEKIEK MFRGDKINST ENRSVLHVAL RAPRDEVINS NGVNVVPEVW
     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 VQLPFESGEI DFGEPGTNGQ HSFYQLIHQG RVIPCDFIGV VKSQQPVYLK
     GEIVSNHDEL MSNFFAQPDA LAYGKTPEQL HSEKVPEHLI PHKTFQGNRP SLSLLLPSLS
     AYEIGQLLAI YEHRIAVQGF LWGINSFDQW GVELGKSLAS QVRKSLHASR VEGKPVLGFN
     SSTTSLLTRY LAVEPSTPYN TTTLPKV
 
 
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