ID   G6PI_CALFI              Reviewed;         304 AA.
AC   P46479;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   22-FEB-2023, entry version 77.
DE   RecName: Full=Glucose-6-phosphate isomerase;
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;
DE   Flags: Fragment;
GN   Name=PGI;
OS   Calanus finmarchicus (Calanus tonsus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Hexanauplia; Copepoda; Calanoida; Calanidae; Calanus.
OX   NCBI_TaxID=6837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7670600;
RA   Crawford D.L.;
RT   "Nuclear genes from the copepod Calanus finmarchicus.";
RL   Mol. Mar. Biol. Biotechnol. 4:241-247(1995).
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:0000255|PROSITE-ProRule:PRU00796};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000255|PROSITE-ProRule:PRU00796}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00796}.
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; U21239; AAA85286.1; -; mRNA.
DR   AlphaFoldDB; P46479; -.
DR   SMR; P46479; -.
DR   UniPathway; UPA00109; UER00181.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; ISS:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
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   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           <1..>304
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180542"
FT   ACT_SITE        146
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00796"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00796"
FT   NON_TER         1
FT   NON_TER         304
SQ   SEQUENCE   304 AA;  34460 MW;  520F95811054FCF7 CRC64;
     FTTQETITNA NTAKQWFLKS AKDSKFVANH FVALSTNAKL VQEFGIDKAN MFEFWDWVGG
     RYSLWSAIGM SIALNIGFEN FEHLLSGAHW MDNHFKSTPI ERNIPVILAV LGIWYGNFYG
     AETQALLPYD QYMHRFAAYF QQGDMESNGK YVVRAGDKVN YSTGPIVWGE PGTNGQHAFY
     QLIHQVPHHP CDFNSPVKSH NSELRDGLHH TILLSNFLAQ TEALMKGKDR QTVEKELKAA
     GKSEDEIKSI GPHKEFTGNR PTNSIMVDTV TPFTLGAMIA MYEHKIFTQG IIWDINSYDQ
     WGVE
//