G6PI_ARATH
ID G6PI_ARATH Reviewed; 560 AA.
AC P34795; Q546J1; Q94JT1; Q9FE90; Q9FXM6; Q9FXM7; Q9FXM8; Q9FXM9; Q9FXN0;
AC Q9FXN1; Q9FXN2; Q9FXN3; Q9FXN4; Q9FXN5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glucose-6-phosphate isomerase, cytosolic;
DE Short=GPI;
DE EC=5.3.1.9;
DE AltName: Full=Phosphoglucose isomerase;
DE Short=PGI;
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI;
GN Name=PGIC; OrderedLocusNames=At5g42740; ORFNames=MJB21.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8293986; DOI=10.1093/genetics/135.3.895;
RA Thomas B.R., Ford V.S., Pichersky E., Gottlieb L.D.;
RT "Molecular characterization of duplicate cytosolic phosphoglucose isomerase
RT genes in Clarkia and comparison to the single gene in Arabidopsis.";
RL Genetics 135:895-905(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=12200488; DOI=10.1093/oxfordjournals.molbev.a004223;
RA Gottlieb L.D., Ford V.S.;
RT "The 5' leader of plant PgiC has an intron: the leader shows both the loss
RT and maintenance of constraints compared with introns and exons in the
RT coding region.";
RL Mol. Biol. Evol. 19:1613-1623(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Many cultivars;
RX PubMed=12716977; DOI=10.1093/molbev/msg124;
RA Kawabe A., Miyashita N.T.;
RT "DNA polymorphism in active gene and pseudogene of the cytosolic
RT phosphoglucose isomerase (PgiC) loci in Arabidopsis halleri ssp.
RT gemmifera.";
RL Mol. Biol. Evol. 20:1043-1050(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=18599644; DOI=10.1104/pp.108.123703;
RA Quettier A.-L., Shaw E., Eastmond P.J.;
RT "SUGAR-DEPENDENT6 encodes a mitochondrial flavin adenine dinucleotide-
RT dependent glycerol-3-p dehydrogenase, which is required for glycerol
RT catabolism and post germinative seedling growth in Arabidopsis.";
RL Plant Physiol. 148:519-528(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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;
CC -!- ACTIVITY REGULATION: Inhibited by glycerol-3-P (G3P).
CC {ECO:0000269|PubMed:18599644}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- POLYMORPHISM: Was sequenced in many cultivars; Ag-0, Bl-1, Bus-1, Ci-0,
CC Cvi-0, Dra-0, Edi-0, Hau-0, Hiroshima, In-0, Ita-0, Kas-1, Mr-0, Nok-4,
CC Ost-0, Pog-0, Rou-0, Su-0, Ts-1 and Ws-0.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR EMBL; X69195; CAA48940.1; -; Genomic_DNA.
DR EMBL; AJ419524; CAD11677.1; -; mRNA.
DR EMBL; AB044948; BAB17635.1; -; Genomic_DNA.
DR EMBL; AB044949; BAB17636.1; -; Genomic_DNA.
DR EMBL; AB044950; BAB17637.1; -; Genomic_DNA.
DR EMBL; AB044951; BAB17638.1; -; Genomic_DNA.
DR EMBL; AB044952; BAB17639.1; -; Genomic_DNA.
DR EMBL; AB044953; BAB17640.1; -; Genomic_DNA.
DR EMBL; AB044954; BAB17641.1; -; Genomic_DNA.
DR EMBL; AB044955; BAB17642.1; -; Genomic_DNA.
DR EMBL; AB044956; BAB17643.1; -; Genomic_DNA.
DR EMBL; AB044957; BAB17644.1; -; Genomic_DNA.
DR EMBL; AB044958; BAB17645.1; -; Genomic_DNA.
DR EMBL; AB044959; BAB17646.1; -; Genomic_DNA.
DR EMBL; AB044960; BAB17647.1; -; Genomic_DNA.
DR EMBL; AB044961; BAB17648.1; -; Genomic_DNA.
DR EMBL; AB044962; BAB17649.1; -; Genomic_DNA.
DR EMBL; AB044963; BAB17650.1; -; Genomic_DNA.
DR EMBL; AB044964; BAB17651.1; -; Genomic_DNA.
DR EMBL; AB044965; BAB17652.1; -; Genomic_DNA.
DR EMBL; AB044966; BAB17653.1; -; Genomic_DNA.
DR EMBL; AB044967; BAB17654.1; -; Genomic_DNA.
DR EMBL; AB007647; BAB10630.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94855.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70583.1; -; Genomic_DNA.
DR EMBL; AF372970; AAK50107.1; -; mRNA.
DR EMBL; AY093962; AAM16223.1; -; mRNA.
DR PIR; S41808; S41808.
DR RefSeq; NP_001332180.1; NM_001344462.1.
DR RefSeq; NP_199088.1; NM_123638.5.
DR AlphaFoldDB; P34795; -.
DR SMR; P34795; -.
DR BioGRID; 19533; 5.
DR STRING; 3702.AT5G42740.1; -.
DR iPTMnet; P34795; -.
DR MetOSite; P34795; -.
DR PaxDb; P34795; -.
DR PRIDE; P34795; -.
DR ProteomicsDB; 228960; -.
DR EnsemblPlants; AT5G42740.1; AT5G42740.1; AT5G42740.
DR EnsemblPlants; AT5G42740.2; AT5G42740.2; AT5G42740.
DR GeneID; 834283; -.
DR Gramene; AT5G42740.1; AT5G42740.1; AT5G42740.
DR Gramene; AT5G42740.2; AT5G42740.2; AT5G42740.
DR KEGG; ath:AT5G42740; -.
DR Araport; AT5G42740; -.
DR TAIR; locus:2165462; AT5G42740.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_017947_4_0_1; -.
DR InParanoid; P34795; -.
DR OrthoDB; 446616at2759; -.
DR PhylomeDB; P34795; -.
DR BRENDA; 5.3.1.9; 399.
DR UniPathway; UPA00109; UER00181.
DR PRO; PR:P34795; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P34795; baseline and differential.
DR Genevisible; P34795; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 Acetylation; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..560
FT /note="Glucose-6-phosphate isomerase, cytosolic"
FT /id="PRO_0000180550"
FT ACT_SITE 361
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 392
FT /evidence="ECO:0000250"
FT ACT_SITE 517
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VARIANT 3
FT /note="S -> P (in strain: cv. Bus-1)"
FT VARIANT 5
FT /note="T -> P (in strain: cv. Ag-0, cv. Bus-1, cv. Dra-0,
FT cv. Hiroshima and cv. Kas-1)"
FT VARIANT 36
FT /note="A -> V (in strain: cv. Bus-1)"
FT VARIANT 73
FT /note="S -> A (in strain: cv. Bl-1 and cv. In-0)"
FT VARIANT 95
FT /note="S -> A (in strain: cv. Bl-1 and cv. In-0)"
FT VARIANT 99
FT /note="V -> I (in strain: cv. Bus-1 and cv. Kas-1)"
FT VARIANT 105
FT /note="K -> E (in strain: cv. Hiroshima)"
FT VARIANT 114
FT /note="M -> K (in strain: cv. Bl-1 and cv. In-0)"
FT VARIANT 119
FT /note="E -> D (in strain: cv. Nok-4)"
FT VARIANT 198
FT /note="N -> S (in strain: cv. Bus-1)"
FT VARIANT 295
FT /note="M -> T (in strain: cv. Cvi-0)"
FT VARIANT 355
FT /note="I -> T (in strain: cv. WS-0)"
FT VARIANT 425
FT /note="Missing (in strain: cv. Cvi-0)"
FT VARIANT 431
FT /note="L -> F (in strain: cv. Pog-0)"
FT VARIANT 432
FT /note="M -> I (in strain: cv. In-0)"
FT VARIANT 528
FT /note="H -> Q (in strain: cv. Ost-0)"
FT CONFLICT 216
FT /note="F -> S (in Ref. 6; AAK50107/AAM16223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 61718 MW; C4F5C7D8FE5F193B CRC64;
MASSTALICD TEAWKDLKGH VEDIKKTHLR DLMSDANRCQ SMMMEFDGLL LDYSRQRATV
ETMDKLLNLA KASQLTEKIS RMFNGEHINS TENRSVLHVA LRAPKDAVIK ADGMNVVPEV
WNVLDKIKEF SDKIRSGSWV GATGKPLKDV IAIGIGGSFL GPLFVHTALQ TDPEALESAK
GRQLRFLANI DPVDVARNIS GLNPETTLVV VVSKTFTTAE TMLNARTLRE WITAALGASA
VAKHMVAVST NLALVEKFGI DPNNAFAFWD WVGGRYSVCS AVGVLPLSLQ YGFSMVEKFL
KGASSIDQHF QSTPFEKNIP VLLGLLSVWN VSFLGYPARA ILPYSQALEK FAPHIQQVSM
ESNGKGVSID GLPLPFETGE IDFGEPGTNG QHSFYQLIHQ GRVIPCDFIG IVKSQQPVYL
KGEVVSNHDE LMSNFFAQPD ALAYGKTPEQ LQKENVSENL IPHKTFSGNR PSLSLLLPEL
TAYNVGQLLA IYEHRVAVQG FVWGINSFDQ WGVELGKVLA TQVRKQLHSS RTQGTAPEGF
NYSTTTLLKR YLETSSEPQM
