G6PI_ACIBS
ID G6PI_ACIBS Reviewed; 556 AA.
AC B0VMS2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=ABSDF0081;
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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}.
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DR EMBL; CU468230; CAO99494.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VMS2; -.
DR SMR; B0VMS2; -.
DR EnsemblBacteria; CAO99494; CAO99494; ABSDF0081.
DR KEGG; abm:ABSDF0081; -.
DR HOGENOM; CLU_017947_3_1_6; -.
DR OMA; CPAYAYG; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001741; 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 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..556
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_1000125683"
FT ACT_SITE 360
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 391
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
FT ACT_SITE 519
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00473"
SQ SEQUENCE 556 AA; 62765 MW; AEAD0A2294128179 CRC64;
MSKSIEKFPK ELVSPIAQLH SLVEKNSKLH IKELFAAEQD RFQNYSVKFD QLVFDYSKHR
ITKSVLEQLF ALAKTKQLTH WIERLFSQDK VNCTEQRAAM HWALRLPSEY SKFPELTKQV
HTQLQRMYVL VEKIHAGQYR GATGEVIQDV VNIGVGGSDL GPQMVTHALC DFKVKTAKPL
NVHFVSTMDG SQLSDLLHQL RPETTLFIIS SKSFGTIDTL SNAQTVRQWL EKALGKHDRV
VKSHFIGVST KAEKMTEWGI APENQLLLWD WVGGRYSLWS CIGFPIALTI GIDGFQQLLA
GAHAVDEHFQ NTNFEQNIPV LMALLGIWNN NFLNIQTHAV LPYDGRLKYF AAYLQQLEME
SNGKSVQRDG QKVELDTCPI VWGEVGPNAQ HAFYQLLHQG TQAVSCDFIA PIQRYNADHF
TYVENAEALI EQHHLALSNC LAQSRLLAFG NEALDSAELK NLPIYKQYEG NQPSSTLLLK
ELNPYSLGML IALYEHKVFV QSVIWNINPF DQWGVEKGKQ IADQLLPILN GAQNDLSALD
ASTRGLIKIL LGKVDG
