ID   G6PI_ACIVR              Reviewed;         557 AA.
AC   Q9RMC1;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
OS   Acinetobacter venetianus (strain ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG
OS   45561 / CIP 110063 / KCTC 2702 / LMG 19082 / RAG-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1191460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31012 / DSM 23050 / BCRC 14357 / CCUG 45561 / CIP 110063 / KCTC
RC   2702 / LMG 19082 / RAG-1;
RA   Nakar D., Gutnick D.L.;
RT   "Genomic organization of the wce region of Acinetobacter lwoffii RAG-1
RT   required for emulsan biosynthesis.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000305}.
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DR   EMBL; AJ243431; CAB57211.1; -; Genomic_DNA.
DR   PIR; T44843; T44843.
DR   RefSeq; WP_004882099.1; NZ_KB849560.1.
DR   AlphaFoldDB; Q9RMC1; -.
DR   SMR; Q9RMC1; -.
DR   GeneID; 58196046; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
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   Gene3D; 1.10.1390.10; -; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
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; 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; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase.
FT   CHAIN           1..557
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180579"
FT   ACT_SITE        361
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT   ACT_SITE        520
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   557 AA;  62671 MW;  2D4FABC1AB595D26 CRC64;
     MNYKQPLIVK SQQQALSALR NLKMQTQDTH LNQFFSDDSG RFERFSVEQE QLVLDFSKHR
     IDQNVLNGLV DLAHAQDLTQ WIQRLFSLEE INYTEQRAAM HWALRVPEQN QQVLPEITAQ
     VHTQLERMYS LVEKIHAGQY RGATGEVIQD VVNIGVGGSD LGPLMVTHAL SDFKVVTAKP
     LDVHFVSTMD GSQLSDLLHQ LRPETTLFII SSKSFGTIDT LSNAQTVRQW LEKALGKNSH
     VLKHHFIGVS TKPDKMSEWG IAPENQLLLW DWVGGRYSLW SCIGLPIALT VGVDGFKQLL
     SGAYAIDQHF QTAPFAQNIP VLIGLLGVWN NNFLDIQTHA VLPYDGRLKY FAAYLQQLEM
     ESNGKSTQRS GEKVDSATCP IVWGEVGPNA QHAFYQLLHQ GTHKVSCDFI APVKRYNANH
     FTYAENAEAL IEQHHLALSN CLAQSRLLAF GNQALTADEI EDLPTYKQYE GNQPSSTILL
     KELNPYSLGM LIATYEHKVF VQSVLWNINP FDQWGVEKGK EIANQLLPIL NREQDDLSTF
     DASTQGLLKI LLGKNNG