G6PI_CALFI
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 03-AUG-2022, entry version 75.
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}.
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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; 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; 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