ID W7U929_9STRA Unreviewed; 1636 AA.
AC W7U929;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|RuleBase:RU000612};
DE EC=5.3.1.9 {ECO:0000256|RuleBase:RU000612};
GN Name=IPS {ECO:0000313|EMBL:EWM29429.1};
GN ORFNames=Naga_100305g6 {ECO:0000313|EMBL:EWM29429.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM29429.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM29429.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM29429.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate;
CC Xref=Rhea:RHEA:10716, ChEBI:CHEBI:58401, ChEBI:CHEBI:61548;
CC EC=5.5.1.4; Evidence={ECO:0000256|ARBA:ARBA00000113};
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:0000256|ARBA:ARBA00029321,
CC ECO:0000256|RuleBase:RU000612};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|RuleBase:RU000612}.
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005117}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC {ECO:0000256|ARBA:ARBA00010813}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWM29429.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZIL01000166; EWM29429.1; -; Genomic_DNA.
DR EnsemblProtists; EWM29429; EWM29429; Naga_100305g6.
DR OrthoDB; 35034at2759; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00823; UER00787.
DR Proteomes; UP000019335; Chromosome 3.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR029056; Ribokinase-like.
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; PF01658; Inos-1-P_synth; 1.
DR Pfam; PF07994; NAD_binding_5; 1.
DR Pfam; PF00294; PfkB; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW Inositol biosynthesis {ECO:0000256|ARBA:ARBA00022550};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612};
KW Reference proteome {ECO:0000313|Proteomes:UP000019335};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 262..365
FT /note="Myo-inositol-1-phosphate synthase GAPDH-like"
FT /evidence="ECO:0000259|Pfam:PF01658"
FT DOMAIN 685..832
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT REGION 913..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1636 AA; 176923 MW; AD74A91E998BB99F CRC64;
MSETSSFGIL IVGLGGNNGV TLLAGLRANQ LGLEWEAPTG KVKANYLGCI TQLPKKGGKG
GYKEAYELAD ANRAAVGGWD IRSTPLGDAL YASHVLDYDL VRQVRASLNQ VEKWKGVWDP
SFIGESQHAT ATNAVDLSTT THAQALALLR ADIRRFRRLH NIPLAGHITV IWSASVERPS
LGDYPTATAL LAGIEANDPE VSPSLLYAAA ACLEGCSFVN GGSQNTLCPG LTELAASRAQ
LHTPNGPVKA RCYVLGTDFK AGQTKFKTAA VEYLRALGLA PTVIASSNHL GNNDMLNLTS
KKTLDAKMRV KSDIFAGWEE AIDHQVRVMY TPFMGDEKRD VVEYTSLGFL GAPHTMLTYT
RCMDSILCVP LMLDVAVWCD YFARKNVPPR RVALATAYLF KVPEGAAKGT DPGFFHQMAA
LEDVLAETKE GGREGGVGRG LTRKGLVKDV EGGGGMTEPW VGGVLCVGLS CLDLMLVGAS
GDGETFGAIN TFQTQVFCPG GAAPQASVAL ADMLGMGGRE GGREGERECA FTTSIVHVLT
KMGRDVHGDE LLRQLEQAGT DTSLVIRDAQ HCTSLAVLPI LASSGARGCF VNLQANDSFT
PGEALAALRE GVRAGEVQGV AAFHFGYPHL MINFQGPALR DFFQAAAEIL DGVNGGEKEV
GRRPARRRLL ISMDLNGVTT RNSEPDVLAE AWAMTDVLHL NQEEAGLLLD WEATGLGAFD
EVLSLPSLRA VGDALLQNGL GVVALTLGEQ GAYVKVTNDE KRLQASATLA WQAAKWVGQE
AFLPPFPVQA GAEVNTNGAG DAFIAGLLAA MLCKTESLSL KQATCFALLT ARERVDSLRR
ASTPKASYNE LLAEAMNLKG NRALRLQRMR RRRPSWLYRG ISAFSTVMLC VNVVHATPSR
GFSRHDLPPH SSAFIPRLPV SRACQGPDRG PATDKNTRRS SIRKMAMSIN HRKPPRKYRG
PIQGYRDEPL HHIPPPQSAP RPIPTPSSSS PSPPSSARAP RIAASIPLSK AASAAAASPF
EPLHPSLSHF PPSSPSTSPS AAGAATQGSH PTYKLPSQTV EWQRLVRHAA EIKALHLRHL
VQDPVRSDAL CVDYDGVYMD YSRQQMTMET RTLLIELAKR TQVGEKVAAM ARGEKINHTE
GRAVLHMATR AGREESVVVD GVDVVRQVHR VLDKVKAFSE GVRQGTIRGA TGKRIRNIVA
VGIGGSYLGP ACIHEVFKTE EEGSQSCRDF RLRFLSNVDP VDVARAQEKL DPEETLVVVV
SKSFATAETM LNARTMRQWL WDGMGTHPDV CAKHMAACAS ASATQLVEAF GIPGERLFEF
WDWVGGRYSV CASPGALPIS LKFGFSVFEK FLAGARSMDR HFLTAPFEKN LPVLMGLLGV
WNMSFLGYRC RTIIPYAEAM MKFPAHIQQV DMESNGKHVT VDGEEINYDI GEIDFGEPGT
NGQHSFFQLL HMGQVVPVDF IGFAESQKAL HVAGEELSSH DELMCNFFAQ PDALAVGKTG
AELLAEGIPP DHVPHRTFKG NRPSLSLLLP RLNAYSMGQL LALYEHRTAV QGFVWHVNSF
DQWGVELGKQ LAKSVREEMK LARTGQAPNL HALVPATARI LQRYWRGGGG KGGKERSLGA
RRVWGKAGRN GRGSGM
//
