ID G6PI_PROMT Reviewed; 524 AA.
AC Q46L16;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=GPI {ECO:0000255|HAMAP-Rule:MF_00473};
DE EC=5.3.1.9 {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PGI {ECO:0000255|HAMAP-Rule:MF_00473};
DE AltName: Full=Phosphohexose isomerase {ECO:0000255|HAMAP-Rule:MF_00473};
DE Short=PHI {ECO:0000255|HAMAP-Rule:MF_00473};
GN Name=pgi {ECO:0000255|HAMAP-Rule:MF_00473}; OrderedLocusNames=PMN2A_0320;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC to fructose-6-phosphate. {ECO:0000255|HAMAP-Rule:MF_00473}.
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|HAMAP-Rule:MF_00473};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000255|HAMAP-
CC Rule:MF_00473}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ57812.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000095; AAZ57812.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011293854.1; NC_007335.2.
DR AlphaFoldDB; Q46L16; -.
DR SMR; Q46L16; -.
DR STRING; 59920.PMN2A_0320; -.
DR KEGG; pmn:PMN2A_0320; -.
DR HOGENOM; CLU_033288_0_0_3; -.
DR PhylomeDB; Q46L16; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002535; Chromosome.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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; 2.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Reference proteome.
FT CHAIN 1..524
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000230926"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 351
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 453
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 524 AA; 58233 MW; EA6E01B3F90E16D7 CRC64;
MNNNDKWARY CDLLYSDDSL GFWLDISRMD VAINDFEDFN EIYSKAFDAL ESLENGSIAN
IDEGRQVGHY WLRNPKVAPS PEISDSITKE IQDISKFGSS ILNGEITNSD GEKYTDVFWI
GIGGSGLGPL LIKESFKRES IGLDLHFLDN VDPEGISHKL NSILPNLNST LFVVVSKSGG
TPEPLIGMEQ AMKFVRDNNQ NWSSRAIAIT SKGSKLDLLA HNENWLDIFD LPDWVGGRTS
ITGAVGLLPA ALIGADINKF LNGASQMDAL TRVKDIKNNP AALLSLAWFK SGNGKGLRDM
VVLPYRDRLE VFSRYLQQLV MESLGKKFDR DENQVNQGIA VYGNKGSTDQ HAYVQQLRDG
IDNFFVNFIE ILHDPLEIVE VKNKRPGDYL SGFLQGTRSA LTEGGRQNLT ITFKSFDESS
LGALIALFER AVSLYAELIN VNAYNQPGVE AGKKAATKII KLQKEIEELL DDGKQRTLNE
INDALSSDST ESIYLILRKL SENSDHYSMI GNQSNPDKLI ISKT
//
