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Database: UniProt
Entry: Q2Q4Z3_COLEU
LinkDB: Q2Q4Z3_COLEU
Original site: Q2Q4Z3_COLEU 
ID   Q2Q4Z3_COLEU            Unreviewed;       486 AA.
AC   Q2Q4Z3;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00018388, ECO:0000256|RuleBase:RU000612};
DE            EC=5.3.1.9 {ECO:0000256|ARBA:ARBA00011952, ECO:0000256|RuleBase:RU000612};
DE   Flags: Fragment;
GN   Name=PGI {ECO:0000313|EMBL:ABB76194.1};
OS   Colias eurytheme (Orange sulphur butterfly) (Alfalfa caterpillar).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Pieridae; Coliadinae; Colias.
OX   NCBI_TaxID=42296 {ECO:0000313|EMBL:ABB76194.1};
RN   [1] {ECO:0000313|EMBL:ABB76194.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3IJ {ECO:0000313|EMBL:ABB76194.1};
RX   PubMed=16292000; DOI=10.1093/molbev/msj062;
RA   Wheat C.W., Watt W.B., Pollock D.D., Schulte P.M.;
RT   "From DNA to fitness differences: sequences and structures of adaptive
RT   variants of Colias phosphoglucose isomerase (PGI).";
RL   Mol. Biol. Evol. 23:499-512(2006).
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   -!- 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   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|RuleBase:RU000612}.
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DR   EMBL; DQ205069; ABB76194.1; -; mRNA.
DR   UniPathway; UPA00109; UER00181.
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:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
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; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   2: Evidence at transcript level;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432,
KW   ECO:0000256|RuleBase:RU000612};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000612};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000612}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABB76194.1"
FT   NON_TER         486
FT                   /evidence="ECO:0000313|EMBL:ABB76194.1"
SQ   SEQUENCE   486 AA;  54082 MW;  CE48C309116839D8 CRC64;
     KVNLKQDPAY QKLQEYYNNN ADKINILQLF QQDADRFNKY SLRIPTPNDG EILLDYSKNR
     IDDTTFSLLL NLAKSRNVEK ARDAMFAGEK INFTEDRAVL HVALRNRQNR PIMVNGKDVT
     PDVNAVLAHM KEFSTQVISG AWKGYTGKXI TDVINIGIGG SDLGPLMVTE ALKPYANHLK
     VHFVSNIDGT HLAEVLKRLN PETALFIIAS KTFTTQETIT NATSAKTWFL EAAKDPAAVS
     KHFVALSTNG EKVTAFGIDP KNMFGFWDWV GGRYSLWSAI GLSISLYIGF ENFEKLLDGA
     NFMDNHFCTA PLEKNAPVIL ALLGVWYGNF YGAETHALLP YDQYLHRFAA YFQQGDMESN
     GKYVTRSGAT VXYSTGPVVW GEPGTNGQHA FYQLVHQGTR LIPCDFLAPA QTHNPIANGA
     HHKILLANFL AQTEALMKGK TDAEAKAELE KSGMXPEAIX KILPHKVFKG NRPTNSIVVK
     KFTPFT
//
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